...
 
[SUBCELLULAR LOCATION] Membrane {ECO:0000305}; Single-pass membrane
protein {ECO:0000305}.
 
On or before Jul 18, 2007 this sequence version replaced
gi:74758781, gi:74758761.
[FUNCTION] May be involved in transcriptional regulation.
[SUBCELLULAR LOCATION] Nucleus {ECO:0000305}.
[SIMILARITY] Belongs to the krueppel C2H2-type zinc-finger protein
family. {ECO:0000305}.
[SIMILARITY] Contains 17 C2H2-type zinc fingers.
{ECO:0000255|PROSITE-ProRule:PRU00042}.
[SEQUENCE CAUTION] Sequence=BAC87366.1; Type=Erroneous initiation;
Evidence={ECO:0000305}.
 
On or before Mar 21, 2006 this sequence version replaced
gi:7466501, gi:20140978.
[FUNCTION] Represses expression of mcbR.
{ECO:0000269|PubMed:18309357}.
 
On Mar 21, 2014 this sequence version replaced gi:75499808.
[FUNCTION] Mediates transport of starch oligosaccharides from the
surface of the outer membrane to the periplasm for subsequent
degradation. {ECO:0000269|PubMed:10986238,
ECO:0000269|PubMed:11717282, ECO:0000269|PubMed:8550519,
ECO:0000269|PubMed:9006015}.
[PATHWAY] Glycan degradation; starch degradation.
[SUBUNIT] Interacts with SusD. {ECO:0000269|PubMed:11717282}.
[SUBCELLULAR LOCATION] Cell outer membrane {ECO:0000250};
Multi-pass membrane protein {ECO:0000250}.
[INDUCTION] By maltose. {ECO:0000269|PubMed:8550519}.
[DISRUPTION PHENOTYPE] Abolished ability to grow on starch.
{ECO:0000269|PubMed:8550519}.
[SIMILARITY] Belongs to the TonB-dependent receptor family.
{ECO:0000305}.
[SEQUENCE CAUTION] Sequence=AAA95938.1; Type=Frameshift;
Positions=374, 380, 714, 724, 745; Evidence={ECO:0000305}.
 
On or before Nov 13, 2007 this sequence version replaced
gi:81897047, gi:81897180, gi:81899723, gi:81899486.
[ALTERNATIVE PRODUCTS] Event=Alternative splicing; Named
isoforms=4; Name=1; IsoId=Q8C9M2-1; Sequence=Displayed; Name=2;
IsoId=Q8C9M2-2; Sequence=VSP_028797; Name=3; IsoId=Q8C9M2-3;
Sequence=VSP_028797, VSP_028798, VSP_028799; Name=4;
IsoId=Q8C9M2-4; Sequence=VSP_028798, VSP_028799.
 
On Nov 11, 2005 this sequence version replaced gi:7462962.
[FUNCTION] Probably functions to regulate transcription of NAD
metabolic genes. Binds to DNA upstream of the probable
nadBII/nadA/nadC and niaRP operons in a nicotinic acid dependent
fashion. Nicotinic acid may be a corepressor.
[COFACTOR] Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Note=Binds 1 Ni(2+)
ion per monomer; it is not certain this is the physiological metal.
[SUBUNIT] Homodimer. {ECO:0000305|PubMed:17256761}.
 
[FUNCTION] Required for resistance to the phenazine antibiotic
D-alanylgriseoluteic acid (AGA), an antibiotic produced by
E.agglomerans itself, and thus protects the bacterium against
phenazine toxicity. Probably binds AGA and acts as a chaperone that
works in tandem with a membrane transporter for subsequent
antibiotic secretion. {ECO:0000269|PubMed:12139622,
ECO:0000269|PubMed:21849072}.
[SUBUNIT] Homodimer. {ECO:0000269|PubMed:21849072}.
[DISRUPTION PHENOTYPE] Loss of D-alanylgriseoluteic acid
resistance. {ECO:0000269|PubMed:12139622}.
 
...
 
[FUNCTION] Acetyltransferase involved in de novo biosynthesis of
UDP-N-acetylglucosamine (UDP-GlcNAc) in roots and is required for
maintaining normal root cell shape. UDP-GlcNAc is an essential
metabolite that serves as an initial sugar donor for N-glycan
synthesis and thus plays an important role in protein and lipid
glycosylation. {ECO:0000269|PubMed:15849305}.
[CATALYTIC ACTIVITY] Acetyl-CoA + D-glucosamine 6-phosphate = CoA +
N-acetyl-D-glucosamine 6-phosphate. {ECO:0000269|PubMed:15849305}.
[BIOPHYSICOCHEMICAL PROPERTIES] Kinetic parameters: KM=180 uM for
acetyl-coenzyme A {ECO:0000269|PubMed:15849305}; KM=145 uM for
glucosamine-6-phosphate {ECO:0000269|PubMed:15849305}.
[PATHWAY] Nucleotide-sugar biosynthesis;
UDP-N-acetyl-alpha-D-glucosamine biosynthesis;
N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine
6-phosphate (route I): step 1/2.
[SUBUNIT] Homodimer. {ECO:0000250}.
[SUBCELLULAR LOCATION] Endoplasmic reticulum membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
[TISSUE SPECIFICITY] Highly expressed in the root elongation zone
and at lower levels in leaves and grains.
{ECO:0000269|PubMed:15849305}.
[DISRUPTION PHENOTYPE] Short roots, disruption of microtubules and
shrinkage of cells in the root elongation zone.
{ECO:0000269|PubMed:15849305}.
[SIMILARITY] Belongs to the acetyltransferase family. GNA1
subfamily. {ECO:0000305}.
[SIMILARITY] Contains 1 N-acetyltransferase domain.
{ECO:0000255|PROSITE-ProRule:PRU00532}.
 
On Jan 20, 2006 this sequence version replaced gi:7435515.
[FUNCTION] May play a key role in the regulation of the
intracellular concentration of adenosylhomocysteine.
{ECO:0000255|HAMAP-Rule:MF_00563}.
[CATALYTIC ACTIVITY] S-adenosyl-L-homocysteine + H(2)O =
L-homocysteine + adenosine. {ECO:0000255|HAMAP-Rule:MF_00563}.
[COFACTOR] Name=NAD(+); Xref=ChEBI:CHEBI:57540;
Evidence={ECO:0000255|HAMAP-Rule:MF_00563}; Note=Binds 1 NAD(+) per
subunit. {ECO:0000255|HAMAP-Rule:MF_00563}.
[PATHWAY] Amino-acid biosynthesis; L-homocysteine biosynthesis;
L-homocysteine from S-adenosyl-L-homocysteine: step 1/1.
{ECO:0000255|HAMAP-Rule:MF_00563}.
[SUBCELLULAR LOCATION] Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00563}.
[SIMILARITY] Belongs to the adenosylhomocysteinase family.
{ECO:0000255|HAMAP-Rule:MF_00563}.
 
[COFACTOR] Name=Fe cation; Xref=ChEBI:CHEBI:24875; Note=Binds 1 Fe
cation per subunit.
[MISCELLANEOUS] May use 2-oxoglutarate as a cosubstrate.
{ECO:0000250}.
 
On Jul 28, 2009 this sequence version replaced gi:41712906.
[FUNCTION] Involved in some intermediate steps for the synthesis of
the antibiotic polyketide bacillaene which is involved in secondary
metabolism. {ECO:0000269|PubMed:16460000,
ECO:0000269|PubMed:17234808}.
[COFACTOR] Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
Evidence={ECO:0000305}; Note=Binds 5 phosphopantetheines
covalently. {ECO:0000305}.
[PATHWAY] Antibiotic biosynthesis; bacillaene biosynthesis.
[SUBCELLULAR LOCATION] Cytoplasm {ECO:0000269|PubMed:17190806}.
[MISCELLANEOUS] The acyl carrier 2 domain binds glycine.
[SIMILARITY] Belongs to the ATP-dependent AMP-binding enzyme
family. {ECO:0000305}.
[SIMILARITY] Contains 5 acyl carrier domains.
{ECO:0000255|PROSITE-ProRule:PRU00258}.
[CAUTION] Was originally thought to be two separate ORFs named pksJ
and pksK. {ECO:0000305}.
 
On or before Oct 5, 2012 this sequence version replaced
gi:81871354, gi:1708848.
[FUNCTION] May participate in the recruitment of inflammatory cells
by injured or infected tissue. GCP-2(1-78) and, more potent,
GCP-2(9-78) attract neutrophils and are involved in neutrophil
activation. {ECO:0000269|PubMed:10570306}.
[SUBCELLULAR LOCATION] Secreted.
[INDUCTION] By lipopolysaccharide (LPS).
[PTM] GCP-2(1-78) and GCP-2(9-78) are produced by proteolytic
cleavage after secretion from fibroblasts and epithelial cells.
GCP-2(9-78) is the most prominent form. A number of additional
N-terminal (processed between pos. 41 and 48) and C-terminal
(processed between pos. 118 and 132) processed forms have been
identified, probably also representing intermediate states.
{ECO:0000269|PubMed:10570306, ECO:0000269|PubMed:8759763}.
[SIMILARITY] Belongs to the intercrine alpha (chemokine CxC)
family. {ECO:0000305}.
 
On Oct 25, 2005 this sequence version replaced gi:76359.
[FUNCTION] Could be required for group III intron excision.
[SUBCELLULAR LOCATION] Plastid, chloroplast.
[SIMILARITY] To group II intron maturases. {ECO:0000305}.
 
On or before Jul 26, 2005 this sequence version replaced
gi:25349059, gi:25349051.
[SUBCELLULAR LOCATION] Cell inner membrane {ECO:0000250};
Multi-pass membrane protein {ECO:0000250}.
[SIMILARITY] Belongs to the TerC family. {ECO:0000305}.
 
On Sep 13, 2005 this sequence version replaced gi:7437142.
[FUNCTION] Catalyzes the NAD(+)-dependent oxidative deamination of
L-alanine to pyruvate, and the reverse reaction, the reductive
amination of pyruvate. Its physiological role is not known. Can not
use NADP(+) instead of NAD(+) as a cosubstrate. In the deamination
direction, can also efficiently use L-2-aminobutyrate as substrate.
In the reductive amination direction, also exhibits high activity
with 2-oxobutyrate and oxaloacetate as substrate. In contrast to
bacterial homologs, does not exhibit any ornithine cyclodeaminase
activity. {ECO:0000255|HAMAP-Rule:MF_00935,
ECO:0000269|PubMed:15516582}.
[CATALYTIC ACTIVITY] L-alanine + H(2)O + NAD(+) = pyruvate + NH(3)
+ NADH. {ECO:0000255|HAMAP-Rule:MF_00935,
ECO:0000269|PubMed:15516582}.
[BIOPHYSICOCHEMICAL PROPERTIES] Kinetic parameters: KM=0.71 mM for
L-alanine (at pH 8.5 and 82 degrees Celsius)
{ECO:0000269|PubMed:15516582}; KM=0.085 mM for L-2-aminobutyrate
(at pH 8.5 and 82 degrees Celsius) {ECO:0000269|PubMed:15516582};
KM=0.60 mM for NAD(+) (at pH 8.5 and 82 degrees Celsius)
{ECO:0000269|PubMed:15516582}; KM=0.16 mM for pyruvate (at pH 8.5
and 82 degrees Celsius) {ECO:0000269|PubMed:15516582}; KM=0.48 mM
for 2-oxobutyrate (at pH 8.5 and 82 degrees Celsius)
{ECO:0000269|PubMed:15516582}; KM=0.97 mM for oxaloacetate (at pH
8.5 and 82 degrees Celsius) {ECO:0000269|PubMed:15516582}; KM=0.02
mM for NADH (at pH 8.5 and 82 degrees Celsius)
{ECO:0000269|PubMed:15516582}; KM=17.3 mM for NH4(+) (at pH 8.5 and
82 degrees Celsius) {ECO:0000269|PubMed:15516582}; Note=kcat is 6.1
sec(-1) and 9.6 sec(-1) for the oxidative deamination of L-alanine
and L-2-aminobutyrate, respectively (at pH 8.5 and 82 degrees
Celsius). kcat is 118 sec(-1), 143 sec(-1) and 113 sec(-1) for the
reductive amination of pyruvate, 2-oxobutyrate and oxaloacetate,
respectively (at pH 8.5 and 82 degrees Celsius).; pH dependence:
Optimum pH is about 7.0 for both the deamination and amination
reactions. {ECO:0000269|PubMed:15516582}; Temperature dependence:
Optimum temperature is 82 degrees Celsius for the reductive
amination of pyruvate. Retains 30% of its maximum activity at 25
degrees Celsius. Completely loses its activity when incubated at 90
degrees Celsius for 2 hours. The thermostability of the enzyme is
increased by more than 10-fold by 1.5 M KCl to a half-life of 55
hours at 90 degrees Celsius. {ECO:0000269|PubMed:15516582}.
[SUBUNIT] Homodimer. {ECO:0000269|PubMed:15313611,
ECO:0000269|PubMed:15516582}.
[SIMILARITY] Belongs to the ornithine cyclodeaminase family.
Archaeal alanine dehydrogenase subfamily.
{ECO:0000255|HAMAP-Rule:MF_00935}.
 
On Jun 15, 2010 this sequence version replaced gi:158564318.
[SUBCELLULAR LOCATION] Nucleus
{ECO:0000255|PROSITE-ProRule:PRU00981}.
[SIMILARITY] Contains 1 bHLH (basic helix-loop-helix) domain.
{ECO:0000255|PROSITE-ProRule:PRU00981}.
[SEQUENCE CAUTION] Sequence=BAB14518.1; Type=Miscellaneous
discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};
Sequence=CAH18277.1; Type=Erroneous initiation; Note=Translation
N-terminally extended.; Evidence={ECO:0000305}.
 
[FUNCTION] tRNA-splicing ligase that acts by directly joining
spliced tRNA halves to mature-sized tRNAs by incorporating the
precursor-derived splice junction phosphate into the mature tRNA as
a canonical 3',5'-phosphodiester. May act as an RNA ligase with
broad substrate specificity, and may function toward other RNAs (By
similarity). {ECO:0000250}.
[COFACTOR] Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000250}; Note=Binds 2 manganese ions per subunit.
{ECO:0000250}.
[SUBUNIT] Monomer. {ECO:0000250}.
[MISCELLANEOUS] Ligation proceeds through 3 nucleotidyl transfer
steps, with 2',3'-cyclic phosphate termini being hydrolyzed to 3'-P
termini in a step that precedes 3'-P activation with GMP. In the
first nucleotidyl transfer step, RtcB reacts with GTP to form a
covalent RtcB-histidine-GMP intermediate with release of PPi; in
the second step, the GMP moiety is transferred to the RNA 3'-P; in
the third step, the 5'-OH from the opposite RNA strand attacks the
activated 3'-P to form a 3',5'-phosphodiester bond and release GMP
(By similarity). {ECO:0000250}.
[SIMILARITY] Belongs to the RtcB family. {ECO:0000305}.
 
[FUNCTION] Together with AlgI and AlgF, forms an inner membrane
complex which probably interacts with the alginate
polymerization-transport complex and adds acetyl groups at the O-2
and O-3 positions of mannuronate residues. Acetylation of alginate
is important for the architecture of biofilms and increases the
ability of alginate to act as a defense barrier (By similarity).
{ECO:0000250}.
[PATHWAY] Glycan biosynthesis; alginate biosynthesis.
[SUBCELLULAR LOCATION] Cell inner membrane {ECO:0000250};
Peripheral membrane protein {ECO:0000250}; Periplasmic side
{ECO:0000250}. Periplasm {ECO:0000250}.
[SIMILARITY] Belongs to the AlgJ family. {ECO:0000305}.
[SEQUENCE CAUTION] Sequence=AAN66903.1; Type=Erroneous initiation;
Evidence={ECO:0000305}.
 
[FUNCTION] This is one of the proteins that binds to the 5S RNA in
the ribosome where it forms part of the central protuberance.
{ECO:0000255|HAMAP-Rule:MF_01334}.
[SUBUNIT] Part of the 50S ribosomal subunit; part of the 5S
rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA. Binds to the 5S
rRNA independently of L5 and L18.
{ECO:0000255|HAMAP-Rule:MF_01334}.
[SIMILARITY] Belongs to the ribosomal protein L25P family. CTC
subfamily. {ECO:0000255|HAMAP-Rule:MF_01334}.
 
[SUBCELLULAR LOCATION] Secreted {ECO:0000305|PubMed:23765379}.
[TISSUE SPECIFICITY] Component of the acid-insoluble and
acid-soluble organic matrix of the aragonitic skeleton (at protein
level). {ECO:0000269|PubMed:23765379}.
[SIMILARITY] Contains 14 LDL-receptor class A domains.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
[SIMILARITY] Contains 37 MAM domains.
{ECO:0000255|PROSITE-ProRule:PRU00128}.
[SIMILARITY] Contains 2 P-type (trefoil) domains.
{ECO:0000255|PROSITE-ProRule:PRU00779}.
 
[SIMILARITY] Belongs to the zinc-containing alcohol dehydrogenase
family. Quinone oxidoreductase subfamily. {ECO:0000305}.
 
On Apr 6, 2005 this sequence version replaced gi:7490733.
[SIMILARITY] Belongs to the UPF0047 family. {ECO:0000305}.
 
On Apr 6, 2005 this sequence version replaced gi:7430155.
[FUNCTION] Putative deacetylase. {ECO:0000250}.
[SIMILARITY] Belongs to the histone deacetylase family.
{ECO:0000305}.
 
...
 
On Jul 4, 2008 this sequence version replaced gi:81885171.
[SUBCELLULAR LOCATION] Cytoplasm {ECO:0000250}.
[ALTERNATIVE PRODUCTS] Event=Alternative splicing; Named
isoforms=2; Name=1; IsoId=Q6P3V7-1; Sequence=Displayed; Name=2;
IsoId=Q6P3V7-2; Sequence=VSP_034502, VSP_034503; Note=No
experimental confirmation available.
[SIMILARITY] Contains 6 TPR repeats. {ECO:0000305}.
 
On or before Mar 21, 2006 this sequence version replaced
gi:7492354, gi:1175391.
[SIMILARITY] Belongs to the transferase hexapeptide repeat family.
{ECO:0000305}.
 
On or before Jul 18, 2007 this sequence version replaced
gi:7466110, gi:3025010.
[SIMILARITY] To E.coli YbeT. {ECO:0000305}.
[SEQUENCE CAUTION] Sequence=AAB40845.1; Type=Erroneous initiation;
Note=Translation N-terminally shortened.; Evidence={ECO:0000305}.
 
On Mar 13, 2013 this sequence version replaced gi:75215506.
[FUNCTION] UV-B specific signaling component that acts as UV-B
photoreceptor and plays a key role in establishing UV-protective
responses in plants. Upon UV-B irradiation, UVR8 undergoes an
immediate switch from homodimer to monomer, accumulates in the
nucleus, interacts with the photomorphogenic repressor COP1 and
regulates the expression of the transcription factor HY5 by
associating with chromatin (through histone H2B binding) in the HY5
promoter region. UVR8 is involved in controlling aspects of leaf
growth and morphogenesis in response to UV-B, is required for
normal progression of endocycle and has a regulatory role in
stomatal differentiation. Is required for plant circadian clock
response to photomorphogenic UV-B light, partly through the
transcriptional activation of responsive clock genes. Promotes
photosynthetic efficiency at elevated levels of UV-B. Plays a role
in mediating the effects of UV-B radiation on pathogen resistance
by controlling the expression of the sinapate biosynthetic pathway.
The two tryptophans, Trp-285 and Trp-233, serve collectively as the
UV-B chromophore. {ECO:0000269|PubMed:16330762,
ECO:0000269|PubMed:17720867, ECO:0000269|PubMed:18055587,
ECO:0000269|PubMed:19165148, ECO:0000269|PubMed:19402876,
ECO:0000269|PubMed:21041653, ECO:0000269|PubMed:21395889,
ECO:0000269|PubMed:21454788, ECO:0000269|PubMed:22447155,
ECO:0000269|PubMed:22988111, ECO:0000269|PubMed:23012433,
ECO:0000269|PubMed:23161229}.
[SUBUNIT] Homodimer in the absence of UV-B, but absorption of UV-B
induces monomerization of UVR8 and interaction with COP1. Interacts
with RUP1, RUP2 and histone H2B. {ECO:0000269|PubMed:19165148,
ECO:0000269|PubMed:20031919, ECO:0000269|PubMed:21041653,
ECO:0000269|PubMed:21454788, ECO:0000269|PubMed:22323738,
ECO:0000269|PubMed:22388820, ECO:0000269|PubMed:22988111,
ECO:0000269|PubMed:23012433, ECO:0000269|PubMed:23129206}.
[INTERACTION] P43254:COP1; NbExp=3; IntAct=EBI-2407499, EBI-301649.
[SUBCELLULAR LOCATION] Nucleus. Cytoplasm, cytosol. Note=UV-B
promotes rapid accumulation of UVR8 in the nucleus.
[DISRUPTION PHENOTYPE] Hypersensitivity to UV-B.
{ECO:0000269|PubMed:12226503}.
[SIMILARITY] Contains 7 RCC1 repeats.
{ECO:0000255|PROSITE-ProRule:PRU00235}.
 
On Apr 26, 2005 this sequence version replaced gi:7487246.
[FUNCTION] Catalyzes the synthesis of indole-3-acetic acid
(IAA)-amino acid conjugates, providing a mechanism for the plant to
cope with the presence of excess auxin. Strongly reactive with Glu,
Gln, Trp, Asp, Ala, Leu, Phe, Gly, Tyr, Met, Ile and Val. Little or
no product formation with His, Ser, Thr, Arg, Lys, or Cys. Also
active on pyruvic and butyric acid analogs of IAA, PAA and the
synthetic auxin naphthaleneacetic acid (NAA). The two chlorinated
synthetic auxin herbicides 2,4-D and 3,6-dichloro-o-anisic acid
(dicamba) cannot be used as substrates.
{ECO:0000269|PubMed:15659623}.
[INDUCTION] By auxin. {ECO:0000269|PubMed:15659623}.
[SIMILARITY] Belongs to the IAA-amido conjugating enzyme family.
{ECO:0000305}.
 
On or before Feb 13, 2009 this sequence version replaced
gi:74750630, gi:113015.
[CATALYTIC ACTIVITY] Long-chain-acyl-CoA + electron-transfer
flavoprotein = long-chain-2,3-dehydroacyl-CoA + reduced
electron-transfer flavoprotein.
[COFACTOR] Name=FAD; Xref=ChEBI:CHEBI:57692.
[PATHWAY] Lipid metabolism; mitochondrial fatty acid
beta-oxidation.
[SUBUNIT] Homotetramer.
[SUBCELLULAR LOCATION] Mitochondrion matrix.
[PTM] Acetylation at Lys-318 and Lys-322 in proximity of the
cofactor-binding sites strongly reduces catalytic activity. These
sites are deacetylated by SIRT3 (By similarity). {ECO:0000250}.
[DISEASE] Acyl-CoA dehydrogenase very long-chain deficiency
(ACADVLD) [MIM:201475]: An inborn error of mitochondrial fatty acid
beta-oxidation which leads to impaired long-chain fatty acid
beta-oxidation. It is clinically heterogeneous, with three major
phenotypes: a severe childhood form characterized by early onset,
high mortality and high incidence of cardiomyopathy; a milder
childhood form with later onset, characterized by hypoketotic
hypoglycemia, low mortality and rare cardiomyopathy; an adult form,
with isolated skeletal muscle involvement, rhabdomyolysis and
myoglobinuria, usually triggered by exercise or fasting. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
[MISCELLANEOUS] A number of straight-chain acyl-CoA dehydrogenases
of different substrate specificities are present in mammalian
tissues.
[SIMILARITY] Belongs to the acyl-CoA dehydrogenase family.
{ECO:0000305}.
 
On Jan 20, 2006 this sequence version replaced gi:1073902.
[FUNCTION] Involved in sulfonamide (sulfathiazole) and bicyclomycin
resistance. Probable membrane translocase (By similarity).
{ECO:0000250}.
[SUBCELLULAR LOCATION] Cell inner membrane {ECO:0000305};
Multi-pass membrane protein {ECO:0000305}.
[SIMILARITY] Belongs to the major facilitator superfamily. Bcr/CmlA
family. {ECO:0000305}.
 
On Aug 30, 2005 this sequence version replaced gi:7522014.
[FUNCTION] Has high binding affinity for fatty acids and retinoids.
[PTM] Nematode polyprotein allergens (NPAs) are synthesized as
large polypeptides that are subsequently proteolytically cleaved to
active polypeptide units.
[ALLERGEN] Causes an allergic reaction in human.
[SIMILARITY] Belongs to the NPA family. {ECO:0000305}.
 
[FUNCTION] L-nicotine is used as a growth substrate. Plays a role
in nicotine catabolism by cleaving a C-C bond in
2,6-dihydroxypseudooxynicotine. {ECO:0000269|PubMed:16321959,
ECO:0000269|PubMed:17275835}.
[CATALYTIC ACTIVITY]
1-(2,6-dihydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H(2)O =
2,6-dihydroxypyridine + 4-methylaminobutanoate.
{ECO:0000269|PubMed:16321959, ECO:0000269|PubMed:17275835}.
[BIOPHYSICOCHEMICAL PROPERTIES] Kinetic parameters: KM=6 uM for
2,6-dihydropseudooxynicotine {ECO:0000269|PubMed:16321959}; pH
dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:16321959}.
[PATHWAY] Alkaloid degradation; nicotine degradation;
2,6-dihydroxypyridine and 4-(methylamino)butanoate from
6-hydroxypseudooxynicotine: step 2/2. {ECO:0000269|PubMed:16321959,
ECO:0000269|PubMed:17275835, ECO:0000269|PubMed:5835946}.
[SUBUNIT] Homodimer. {ECO:0000269|PubMed:17275835}.
[SIMILARITY] Belongs to the UPF0255 family. {ECO:0000255}.
 
[FUNCTION] Catalyzes the conversion of uracil and
5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and
diphosphate. {ECO:0000255|HAMAP-Rule:MF_01218}.
[CATALYTIC ACTIVITY] UMP + diphosphate = uracil +
5-phospho-alpha-D-ribose 1-diphosphate.
{ECO:0000255|HAMAP-Rule:MF_01218}.
[COFACTOR] Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_01218}; Note=Binds 1 Mg(2+) ion
per subunit. The magnesium is bound as Mg-PRPP.
{ECO:0000255|HAMAP-Rule:MF_01218}.
[ENZYME REGULATION] Allosterically activated by GTP.
{ECO:0000255|HAMAP-Rule:MF_01218}.
[PATHWAY] Pyrimidine metabolism; UMP biosynthesis via salvage
pathway; UMP from uracil: step 1/1.
{ECO:0000255|HAMAP-Rule:MF_01218}.
[SIMILARITY] Belongs to the UPRTase family.
{ECO:0000255|HAMAP-Rule:MF_01218}.
 
[FUNCTION] Responsible for the transport of dicarboxylates such as
succinate, fumarate, and malate from the periplasm across the
membrane. {ECO:0000255|HAMAP-Rule:MF_01300}.
[SUBCELLULAR LOCATION] Cell inner membrane
{ECO:0000255|HAMAP-Rule:MF_01300}; Multi-pass membrane protein
{ECO:0000255|HAMAP-Rule:MF_01300}.
[SIMILARITY] Belongs to the sodium:dicarboxylate (SDF) symporter
(TC 2.A.23) family. {ECO:0000255|HAMAP-Rule:MF_01300}.
 
On Nov 8, 2005 this sequence version replaced gi:118412.
[SUBCELLULAR LOCATION] Cell inner membrane {ECO:0000250};
Multi-pass membrane protein {ECO:0000250}.
[SIMILARITY] Belongs to the DedA family. {ECO:0000305}.
 
On Feb 28, 2006 this sequence version replaced gi:7433862.
[FUNCTION] Synthesizes alpha-1,4-glucan chains using ADP-glucose.
{ECO:0000255|HAMAP-Rule:MF_00484}.
[CATALYTIC ACTIVITY] ADP-glucose + (1,4-alpha-D-glucosyl)(n) = ADP
+ (1,4-alpha-D-glucosyl)(n+1). {ECO:0000255|HAMAP-Rule:MF_00484}.
[PATHWAY] Glycan biosynthesis; glycogen biosynthesis.
{ECO:0000255|HAMAP-Rule:MF_00484}.
[SIMILARITY] Belongs to the glycosyltransferase 1 family.
Bacterial/plant glycogen synthase subfamily.
{ECO:0000255|HAMAP-Rule:MF_00484}.
 
On Jun 30, 2006 this sequence version replaced gi:2130265.
[SIMILARITY] Contains 1 glutamine amidotransferase type-1 domain.
{ECO:0000255|PROSITE-ProRule:PRU00605}.
 
[SIMILARITY] Belongs to the UPF0276 family.
{ECO:0000255|HAMAP-Rule:MF_00697}.
 
[FUNCTION] Catalyzes the transfer of the phosphoribosyl group of
5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield
N-(5'-phosphoribosyl)-anthranilate (PRA).
{ECO:0000255|HAMAP-Rule:MF_00211}.
[CATALYTIC ACTIVITY] N-(5-phospho-D-ribosyl)-anthranilate +
diphosphate = anthranilate + 5-phospho-alpha-D-ribose
1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00211}.
[COFACTOR] Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_00211}; Note=Binds 2 magnesium
ions per monomer. {ECO:0000255|HAMAP-Rule:MF_00211}.
[PATHWAY] Amino-acid biosynthesis; L-tryptophan biosynthesis;
L-tryptophan from chorismate: step 2/5.
{ECO:0000255|HAMAP-Rule:MF_00211}.
[SUBUNIT] Homodimer. {ECO:0000255|HAMAP-Rule:MF_00211}.
[SIMILARITY] Belongs to the anthranilate phosphoribosyltransferase
family. {ECO:0000255|HAMAP-Rule:MF_00211}.
 
[FUNCTION] Has endoribonuclease activity towards 23S and 16S rRNA
(in vitro). {ECO:0000269|PubMed:16945939}.
[COFACTOR] Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:16945939}; Note=Binds 2 Zn(2+) ions.
{ECO:0000269|PubMed:16945939}.
[ENZYME REGULATION] Inhibited by cadmium, cobalt, manganese,
magnesium, calcium and nickel ions. {ECO:0000269|PubMed:16945939}.
[SUBUNIT] Monomer. {ECO:0000269|PubMed:16945939}.
[SUBCELLULAR LOCATION] Cytoplasm {ECO:0000250}.
[SIMILARITY] Belongs to the metallo-beta-lactamase superfamily.
RNA-metabolizing metallo-beta-lactamase-like family. {ECO:0000305}.
 
On or before Mar 30, 2010 this sequence version replaced
gi:75165163, gi:11282349.
[FUNCTION] Involved in pectin biosynthesis. Catalyzes the transfer
of galacturonic acid from uridine 5'-diphosphogalacturonic acid
onto the pectic polysaccharide homogalacturonan.
{ECO:0000269|PubMed:16540543}.
[CATALYTIC ACTIVITY] UDP-D-galacturonate +
((1->4)-alpha-D-galacturonosyl)(n) = UDP +
((1->4)-alpha-D-galacturonosyl)(n+1).
{ECO:0000269|PubMed:16540543}.
[PATHWAY] Glycan metabolism; pectin biosynthesis.
[SUBCELLULAR LOCATION] Golgi apparatus membrane {ECO:0000250};
Single-pass type II membrane protein {ECO:0000250}.
[TISSUE SPECIFICITY] Expressed in seedlings, inflorescences,
flowers, siliques, pollen, roots, stems and leaves.
{ECO:0000269|PubMed:10809443, ECO:0000269|PubMed:16540543,
ECO:0000269|PubMed:19825675}.
[SIMILARITY] Belongs to the glycosyltransferase 8 family.
{ECO:0000305}.
[SEQUENCE CAUTION] Sequence=AAK62572.1; Type=Frameshift;
Positions=611; Evidence={ECO:0000305}; Sequence=AAN18196.1;
Type=Frameshift; Positions=611; Evidence={ECO:0000305}.
 
On Dec 27, 2005 this sequence version replaced gi:129244.
[SUBCELLULAR LOCATION] Periplasm {ECO:0000250}.
[SIMILARITY] Contains 2 BON domains.
{ECO:0000255|PROSITE-ProRule:PRU00229}.
[SEQUENCE CAUTION] Sequence=AAN83877.1; Type=Erroneous initiation;
Evidence={ECO:0000305}.
 
On Jan 20, 2006 this sequence version replaced gi:7467919.
[CATALYTIC ACTIVITY] Acetyl-CoA + phosphate = CoA + acetyl
phosphate.
[PATHWAY] Metabolic intermediate biosynthesis; acetyl-CoA
biosynthesis; acetyl-CoA from acetate: step 2/2.
[SUBCELLULAR LOCATION] Cytoplasm {ECO:0000305}.
[SIMILARITY] Belongs to the phosphate acetyltransferase and
butyryltransferase family. {ECO:0000305}.
 
On Jan 20, 2006 this sequence version replaced gi:1074196.
[SUBCELLULAR LOCATION] Cell inner membrane {ECO:0000305};
Multi-pass membrane protein {ECO:0000305}.
[SIMILARITY] Belongs to the BCCT transporter (TC 2.A.15) family.
{ECO:0000305}.
 
On Mar 15, 2005 this sequence version replaced gi:1077853.
 
[FUNCTION] The heterodimer acts as both an ATP-dependent DNA
helicase and an ATP-dependent, dual-direction single-stranded
exonuclease. Recognizes the chi site generating a DNA molecule
suitable for the initiation of homologous recombination. The AddB
nuclease domain is not required for chi fragment generation; this
subunit has 5' -> 3' nuclease activity.
{ECO:0000255|HAMAP-Rule:MF_01452}.
[CATALYTIC ACTIVITY] ATP + H(2)O = ADP + phosphate.
{ECO:0000255|HAMAP-Rule:MF_01452}.
[COFACTOR] Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000255|HAMAP-Rule:MF_01452}; Note=Binds 1 [4Fe-4S]
cluster. {ECO:0000255|HAMAP-Rule:MF_01452}.
[COFACTOR] Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_01452}.
[SUBUNIT] Heterodimer of AddA and AddB.
{ECO:0000255|HAMAP-Rule:MF_01452}.
[SIMILARITY] Belongs to the helicase family. AddB/RexB type 1
subfamily. {ECO:0000255|HAMAP-Rule:MF_01452}.
 
On Apr 5, 2013 this sequence version replaced gi:75166335.
[FUNCTION] Catalyzes the NAD-dependent decarboxylation of
UDP-glucuronic acid to UDP-xylose. Necessary for the biosynthesis
of the core tetrasaccharide in glycosaminoglycan biosynthesis.
{ECO:0000269|PubMed:12481102, ECO:0000269|PubMed:16817893}.
[CATALYTIC ACTIVITY] UDP-D-glucuronate = UDP-D-xylose + CO(2).
[COFACTOR] Name=NAD(+); Xref=ChEBI:CHEBI:57540;
Evidence={ECO:0000269|PubMed:12481102}.
[BIOPHYSICOCHEMICAL PROPERTIES] Kinetic parameters: KM=0.51 mM for
UDP-D-glucuronate at 30 degrees Celsius
{ECO:0000269|PubMed:12481102}; pH dependence: Optimum pH is 5.5 at
30 degrees Celsius. {ECO:0000269|PubMed:12481102}; Temperature
dependence: Optimum temperature is 30 degrees Celsius.
{ECO:0000269|PubMed:12481102}.
[PATHWAY] Nucleotide-sugar biosynthesis; UDP-alpha-D-xylose
biosynthesis; UDP-alpha-D-xylose from UDP-alpha-D-glucuronate: step
1/1.
[SUBCELLULAR LOCATION] Cytoplasm {ECO:0000269|PubMed:15655675}.
[ALTERNATIVE PRODUCTS] Event=Alternative splicing; Named
isoforms=1; Comment=A number of isoforms are produced. According to
EST sequences.; Name=1; IsoId=Q9FIE8-1; Sequence=Displayed.
[TISSUE SPECIFICITY] Ubiquitous. {ECO:0000269|PubMed:12481102}.
[SIMILARITY] Belongs to the NAD(P)-dependent epimerase/dehydratase
family. UDP-glucuronic acid decarboxylase subfamily. {ECO:0000305}.
 
[FUNCTION] Responsible for methylating the 5'-cap structure of
mRNAs. {ECO:0000250}.
[CATALYTIC ACTIVITY] S-adenosyl-L-methionine + G(5')pppR-RNA =
S-adenosyl-L-homocysteine + m(7)G(5')pppR-RNA.
{ECO:0000255|PROSITE-ProRule:PRU00895}.
[SUBCELLULAR LOCATION] Nucleus {ECO:0000250}.
[SIMILARITY] Belongs to the class I-like SAM-binding
methyltransferase superfamily. mRNA cap 0 methyltransferase family.
{ECO:0000255|PROSITE-ProRule:PRU00895}.
[SIMILARITY] Contains 1 mRNA cap 0 methyltransferase domain.
{ECO:0000255|PROSITE-ProRule:PRU00895}.
 
[FUNCTION] May be involved in head or eye development; development
of the clypeolabrum and several head sensory organs.
{ECO:0000269|PubMed:10381573, ECO:0000269|PubMed:9724757}.
[SUBCELLULAR LOCATION] Nucleus
{ECO:0000255|PROSITE-ProRule:PRU00108}.
[ALTERNATIVE PRODUCTS] Event=Alternative splicing; Named
isoforms=3; Name=A; IsoId=Q95RW8-1; Sequence=Displayed; Note=No
experimental confirmation available.; Name=B; IsoId=Q95RW8-2;
Sequence=VSP_002258; Name=C; IsoId=Q95RW8-3; Sequence=VSP_002259;
Note=No experimental confirmation available.
[TISSUE SPECIFICITY] Expressed during early development of the
head. First expressed in a band around the anterior end of stage 5
blastoderm embryo, at 93% to 85% egg length. By gastrula stage,
site of expression shifts to the dorsal-anterior region. At stage
12, expression is found in the clypeolabrum, the stomodaeum, and in
ectoderm dorsal to the future supraesophageal ganglion.
{ECO:0000269|PubMed:10381573, ECO:0000269|PubMed:9724757}.
[DEVELOPMENTAL STAGE] Expressed during embryonic development.
{ECO:0000269|PubMed:10381573, ECO:0000269|PubMed:9724757}.
[SIMILARITY] Belongs to the SIX/Sine oculis homeobox family.
{ECO:0000305}.
[SIMILARITY] Contains 1 homeobox DNA-binding domain.
{ECO:0000255|PROSITE-ProRule:PRU00108}.
 
[FUNCTION] sn-glycerol-3-phosphate and glycerophosphoryl
diester-binding protein interacts with the binding
protein-dependent transport system UgpACE. {ECO:0000250}.
[SUBUNIT] The complex is composed of two ATP-binding proteins
(UgpC), two transmembrane proteins (UgpA and UgpE) and a
solute-binding protein (UgpB). {ECO:0000305}.
[SUBCELLULAR LOCATION] Periplasm {ECO:0000305}.
[SIMILARITY] Belongs to the bacterial solute-binding protein 1
family. {ECO:0000305}.
 
On or before Sep 27, 2005 this sequence version replaced gi:80215,
gi:1706414.
[FUNCTION] Catalyzes the reversible deamination of L-leucine to
4-methyl-2-oxopentanoate. {ECO:0000269|PubMed:3069133}.
[CATALYTIC ACTIVITY] L-leucine + H(2)O + NAD(+) =
4-methyl-2-oxopentanoate + NH(3) + NADH.
{ECO:0000269|PubMed:3069133}.
[PATHWAY] Amino-acid degradation; L-leucine degradation;
4-methyl-2-oxopentanoate from L-leucine (dehydrogenase route): step
1/1.
[SUBUNIT] Homohexamer. {ECO:0000269|PubMed:3069133}.
[BIOTECHNOLOGY] This enzyme has been successfully altered through
several rounds of protein engineering to an enantioselective amine
dehydrogenase. Instead of the wild-type alpha-keto acid, the new
amine dehydrogenase now accepts the analogous ketone, methyl
isobutyl ketone (MIBK), which corresponds to exchange of the
carboxy group by a methyl group, to produce chiral
(R)-1,3-dimethylbutylamine via a reductive amination reaction. This
represents a suitable enzymatic production route for the asymmetric
synthesis of amines from prochiral ketones and free ammonia, which
is one of the top aspirational reactions challenging the
pharmaceutical industry. {ECO:0000269|PubMed:22396126}.
[SIMILARITY] Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
{ECO:0000305}.
[SEQUENCE CAUTION] Sequence=AAA22570.1; Type=Frameshift;
Positions=365; Evidence={ECO:0000305}.
 
[CATALYTIC ACTIVITY] ATP + L-asparagine + tRNA(Asn) = AMP +
diphosphate + L-asparaginyl-tRNA(Asn).
{ECO:0000255|HAMAP-Rule:MF_00534}.
[SUBUNIT] Homodimer. {ECO:0000255|HAMAP-Rule:MF_00534}.
[SUBCELLULAR LOCATION] Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00534}.
[SIMILARITY] Belongs to the class-II aminoacyl-tRNA synthetase
family. {ECO:0000255|HAMAP-Rule:MF_00534}.
 
[FUNCTION] Part of the ABC transporter complex LolCDE involved in
the translocation of mature outer membrane-directed lipoproteins,
from the inner membrane to the periplasmic chaperone, LolA.
Responsible for the formation of the LolA-lipoprotein complex in an
ATP-dependent manner. {ECO:0000255|HAMAP-Rule:MF_01708}.
[SUBUNIT] The complex is composed of two ATP-binding proteins
(LolD) and two transmembrane proteins (LolC and LolE).
{ECO:0000255|HAMAP-Rule:MF_01708}.
[SUBCELLULAR LOCATION] Cell inner membrane
{ECO:0000255|HAMAP-Rule:MF_01708}; Peripheral membrane protein
{ECO:0000255|HAMAP-Rule:MF_01708}.
[SIMILARITY] Belongs to the ABC transporter superfamily.
Lipoprotein translocase (TC 3.A.1.125) family.
{ECO:0000255|HAMAP-Rule:MF_01708}.
[SIMILARITY] Contains 1 ABC transporter domain.
{ECO:0000255|HAMAP-Rule:MF_01708}.
 
[FUNCTION] This protein catalyzes the committed step to the
synthesis of the acidic phospholipids.
{ECO:0000255|HAMAP-Rule:MF_01437}.
[CATALYTIC ACTIVITY] CDP-diacylglycerol + sn-glycerol 3-phosphate =
CMP + 3(3-sn-phosphatidyl)-sn-glycerol 1-phosphate.
{ECO:0000255|HAMAP-Rule:MF_01437}.
[PATHWAY] Phospholipid metabolism; phosphatidylglycerol
biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step
1/2. {ECO:0000255|HAMAP-Rule:MF_01437}.
[SUBCELLULAR LOCATION] Cell inner membrane
{ECO:0000255|HAMAP-Rule:MF_01437}; Multi-pass membrane protein
{ECO:0000255|HAMAP-Rule:MF_01437}.
[SIMILARITY] Belongs to the CDP-alcohol phosphatidyltransferase
class-I family. {ECO:0000255|HAMAP-Rule:MF_01437}.
 
On Jul 17, 2007 this sequence version replaced gi:1075219.
[FUNCTION] Endoribonuclease that plays a central role in RNA
processing and decay. Required for the maturation of 5S and 16S
rRNAs and the majority of tRNAs. Also involved in the degradation
of most mRNAs. {ECO:0000255|HAMAP-Rule:MF_00970}.
[CATALYTIC ACTIVITY] Endonucleolytic cleavage of single-stranded
RNA in A- and U-rich regions. {ECO:0000255|HAMAP-Rule:MF_00970}.
[COFACTOR] Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000255|HAMAP-Rule:MF_00970}; Note=Binds 2 Zn(2+)
ions per homotetramer. {ECO:0000255|HAMAP-Rule:MF_00970}.
[COFACTOR] Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_00970}; Note=Binds 1 Mg(2+) ion
per subunit. {ECO:0000255|HAMAP-Rule:MF_00970}.
[SUBUNIT] Component of the RNA degradosome, which is a multiprotein
complex involved in RNA processing and mRNA degradation. Within the
RNA degradosome, Rnase E assembles into a homotetramer formed by a
dimer of dimers. {ECO:0000255|HAMAP-Rule:MF_00970}.
[SUBCELLULAR LOCATION] Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00970}.
Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00970}; Peripheral
membrane protein {ECO:0000255|HAMAP-Rule:MF_00970}; Cytoplasmic
side {ECO:0000255|HAMAP-Rule:MF_00970}.
[SIMILARITY] Belongs to the RNase E/G family. RNase E subfamily.
{ECO:0000255|HAMAP-Rule:MF_00970}.
[SIMILARITY] Contains 1 S1 motif domain.
{ECO:0000255|HAMAP-Rule:MF_00970}.
[SEQUENCE CAUTION] Sequence=AAC22072.1; Type=Erroneous initiation;
Note=Translation N-terminally shortened.; Evidence={ECO:0000305}.
 
[FUNCTION] Transcription regulator that activates transcription by
stimulating RNA polymerase (RNAP) recycling in case of stress
conditions such as supercoiled DNA or high salt concentrations.
Probably acts by releasing the RNAP, when it is trapped or
immobilized on tightly supercoiled DNA. Does not activate
transcription on linear DNA. Probably not involved in DNA repair.
{ECO:0000255|HAMAP-Rule:MF_01821}.
[SUBUNIT] Interacts with the RNAP. Has a higher affinity for the
core RNAP than for the holoenzyme. Its ATPase activity is
stimulated by binding to RNAP. {ECO:0000255|HAMAP-Rule:MF_01821}.
[SIMILARITY] Belongs to the SNF2/RAD54 helicase family. RapA
subfamily. {ECO:0000255|HAMAP-Rule:MF_01821}.
[SIMILARITY] Contains 1 helicase ATP-binding domain.
{ECO:0000255|HAMAP-Rule:MF_01821}.
[SIMILARITY] Contains 1 helicase C-terminal domain.
{ECO:0000255|HAMAP-Rule:MF_01821}.
 
On Jun 13, 2006 this sequence version replaced gi:7467131.
[FUNCTION] Has DNA endonuclease activity. Binds DNA.
{ECO:0000269|PubMed:21276852}.
[SIMILARITY] Contains 1 Smr domain.
{ECO:0000255|PROSITE-ProRule:PRU00321}.
 
[FUNCTION] Catalyzes the NADPH-dependent formation of
L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation
of L-aspartyl-4-phosphate. {ECO:0000255|HAMAP-Rule:MF_02121}.
[CATALYTIC ACTIVITY] L-aspartate 4-semialdehyde + phosphate +
NADP(+) = L-4-aspartyl phosphate + NADPH.
{ECO:0000255|HAMAP-Rule:MF_02121}.
[PATHWAY] Amino-acid biosynthesis; L-lysine biosynthesis via DAP
pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4.
{ECO:0000255|HAMAP-Rule:MF_02121}.
[PATHWAY] Amino-acid biosynthesis; L-methionine biosynthesis via de
novo pathway; L-homoserine from L-aspartate: step 2/3.
{ECO:0000255|HAMAP-Rule:MF_02121}.
[PATHWAY] Amino-acid biosynthesis; L-threonine biosynthesis;
L-threonine from L-aspartate: step 2/5.
{ECO:0000255|HAMAP-Rule:MF_02121}.
[SUBUNIT] Homodimer. {ECO:0000255|HAMAP-Rule:MF_02121}.
[SIMILARITY] Belongs to the aspartate-semialdehyde dehydrogenase
family. {ECO:0000255|HAMAP-Rule:MF_02121}.
 
On Jan 20, 2006 this sequence version replaced gi:11348617.
[FUNCTION] Has a glutathione-disulfide oxidoreductase activity in
the presence of NADPH and glutathione reductase. Reduces low
molecular weight disulfides and proteins (By similarity).
{ECO:0000250}.
[SUBUNIT] Monomer. {ECO:0000250}.
[SUBCELLULAR LOCATION] Cytoplasm {ECO:0000250}.
[SIMILARITY] Belongs to the glutaredoxin family. {ECO:0000305}.
[SIMILARITY] Contains 1 glutaredoxin domain.
{ECO:0000255|PROSITE-ProRule:PRU00686}.
 
On Apr 12, 2005 this sequence version replaced gi:85515.
[FUNCTION] Vasotocin is an antidiuretic hormone.
[SUBCELLULAR LOCATION] Secreted.
[SIMILARITY] Belongs to the vasopressin/oxytocin family.
{ECO:0000305}.
 
[CATALYTIC ACTIVITY] ATP + L-leucine + tRNA(Leu) = AMP +
diphosphate + L-leucyl-tRNA(Leu).
{ECO:0000255|HAMAP-Rule:MF_00049}.
[SUBCELLULAR LOCATION] Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00049}.
[SIMILARITY] Belongs to the class-I aminoacyl-tRNA synthetase
family. {ECO:0000255|HAMAP-Rule:MF_00049}.
 
[FUNCTION] Catalyzes the condensation of
(S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to
4-hydroxy-tetrahydrodipicolinate (HTPA).
{ECO:0000255|HAMAP-Rule:MF_00418}.
[CATALYTIC ACTIVITY] Pyruvate + L-aspartate-4-semialdehyde =
(4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate + H(2)O.
{ECO:0000255|HAMAP-Rule:MF_00418}.
[PATHWAY] Amino-acid biosynthesis; L-lysine biosynthesis via DAP
pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
{ECO:0000255|HAMAP-Rule:MF_00418}.
[SUBUNIT] Homotetramer; dimer of dimers.
{ECO:0000255|HAMAP-Rule:MF_00418}.
[SUBCELLULAR LOCATION] Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00418}.
[SIMILARITY] Belongs to the DapA family.
{ECO:0000255|HAMAP-Rule:MF_00418}.
[CAUTION] Was originally thought to be a dihydrodipicolinate
synthase (DHDPS), catalyzing the condensation of
(S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to
dihydrodipicolinate (DHDP). However, it was shown in E.coli that
the product of the enzymatic reaction is not dihydrodipicolinate
but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid
(HTPA), and that the consecutive dehydration reaction leading to
DHDP is not spontaneous but catalyzed by DapB. {ECO:0000305}.
 
On Sep 27, 2005 this sequence version replaced gi:25283171.
[CATALYTIC ACTIVITY] (R)-3-hydroxybutanoate + NAD(+) = acetoacetate
+ NADH.
[SIMILARITY] Belongs to the short-chain dehydrogenases/reductases
(SDR) family. {ECO:0000305}.
 
[FUNCTION] MotA and MotB comprise the stator element of the
flagellar motor complex. Required for rotation of the flagellar
motor. Probable transmembrane proton channel (By similarity).
{ECO:0000250}.
[SUBUNIT] Each stator complex is composed of 4 MotA and 2 MotB
subunits. 2 A subunits and 1 B subunit are thought to form a single
ion channel, so that each stator complex contains two channels (By
similarity). {ECO:0000250}.
[SUBCELLULAR LOCATION] Cell inner membrane {ECO:0000250};
Multi-pass membrane protein {ECO:0000305}.
[SIMILARITY] Belongs to the MotA family. {ECO:0000305}.
 
On Oct 11, 2005 this sequence version replaced gi:548909.
[FUNCTION] Involved in the import of serine into the cell. May be
required for phage C1 adsorption by interacting with DrcB. May also
be involved in ampicillin sensitivity (By similarity).
{ECO:0000250}.
[SUBCELLULAR LOCATION] Cell inner membrane {ECO:0000250};
Multi-pass membrane protein {ECO:0000250}.
[INDUCTION] By leucine and by growth in rich medium. {ECO:0000250}.
[SIMILARITY] Belongs to the amino acid/polyamine transporter 2
family. SdaC/TdcC subfamily. {ECO:0000305}.
 
On Jul 5, 2005 this sequence version replaced gi:77679.
[FUNCTION] May be involved in pilus retraction.
[SUBCELLULAR LOCATION] Cytoplasm {ECO:0000305}.
[SIMILARITY] Belongs to the GSP E family. {ECO:0000305}.
 
On or before Apr 26, 2005 this sequence version replaced
gi:11348453, gi:2500054.
[FUNCTION] May play a role in the repair of endogenous alkylation
damage. {ECO:0000250}.
[SIMILARITY] Belongs to the RecA family. RadA subfamily.
{ECO:0000305}.
 
[FUNCTION] May be required for assembly of mitochondrial
respiratory chain complexes. {ECO:0000250}.
[SUBCELLULAR LOCATION] Mitochondrion intermembrane space
{ECO:0000250}.
[SIMILARITY] Belongs to the hcp beta-lactamase family.
{ECO:0000305}.
[SIMILARITY] Contains 5 Sel1-like repeats. {ECO:0000305}.
 
[FUNCTION] Bidirectionally degrades single-stranded DNA into large
acid-insoluble oligonucleotides, which are then degraded further
into small acid-soluble oligonucleotides.
{ECO:0000255|HAMAP-Rule:MF_00337}.
[CATALYTIC ACTIVITY] Exonucleolytic cleavage in either 5'- to 3'-or
3'- to 5'-direction to yield nucleoside 5'-phosphates.
{ECO:0000255|HAMAP-Rule:MF_00337}.
[SUBUNIT] Heterooligomer composed of large and small subunits.
{ECO:0000255|HAMAP-Rule:MF_00337}.
[SUBCELLULAR LOCATION] Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00337}.
[SIMILARITY] Belongs to the XseB family.
{ECO:0000255|HAMAP-Rule:MF_00337}.
 
[FUNCTION] Catalyzes the NADPH-dependent reduction of
glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
{ECO:0000255|HAMAP-Rule:MF_00087}.
[CATALYTIC ACTIVITY] L-glutamate 1-semialdehyde + NADP(+) +
tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.
{ECO:0000255|HAMAP-Rule:MF_00087}.
[PATHWAY] Porphyrin-containing compound metabolism;
protoporphyrin-IX biosynthesis; 5-aminolevulinate from
L-glutamyl-tRNA(Glu): step 1/2. {ECO:0000255|HAMAP-Rule:MF_00087}.
[SUBUNIT] Homodimer. {ECO:0000255|HAMAP-Rule:MF_00087}.
[DOMAIN] Possesses an unusual extended V-shaped dimeric structure
with each monomer consisting of three distinct domains arranged
along a curved 'spinal' alpha-helix. The N-terminal catalytic
domain specifically recognizes the glutamate moiety of the
substrate. The second domain is the NADPH-binding domain, and the
third C-terminal domain is responsible for dimerization.
{ECO:0000255|HAMAP-Rule:MF_00087}.
[MISCELLANEOUS] During catalysis, the active site Cys acts as a
nucleophile attacking the alpha-carbonyl group of tRNA-bound
glutamate with the formation of a thioester intermediate between
enzyme and glutamate, and the concomitant release of tRNA(Glu). The
thioester intermediate is finally reduced by direct hydride
transfer from NADPH, to form the product GSA.
{ECO:0000255|HAMAP-Rule:MF_00087}.
[SIMILARITY] Belongs to the glutamyl-tRNA reductase family.
{ECO:0000255|HAMAP-Rule:MF_00087}.
 
On Nov 8, 2005 this sequence version replaced gi:125330.
[FUNCTION] Involved in lipopolysaccharide (LPS) biosynthesis.
Catalyzes the transfer of two 3-deoxy-D-manno-octulosonate (Kdo)
residues from CMP-Kdo to lipid IV(A), the
tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A (By
similarity). {ECO:0000250}.
[CATALYTIC ACTIVITY] Lipid IV(A) + CMP-alpha-Kdo =
alpha-Kdo-(2->6)-lipid IV(A) + CMP.
[CATALYTIC ACTIVITY] Alpha-Kdo-(2->6)-lipid IV(A) + CMP-alpha-Kdo =
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IV(A) + CMP.
[PATHWAY] Glycolipid biosynthesis; KDO(2)-lipid A biosynthesis;
KDO(2)-lipid A from CMP-3-deoxy-D-manno-octulosonate and lipid
IV(A): step 1/4.
[PATHWAY] Glycolipid biosynthesis; KDO(2)-lipid A biosynthesis;
KDO(2)-lipid A from CMP-3-deoxy-D-manno-octulosonate and lipid
IV(A): step 2/4.
[PATHWAY] Bacterial outer membrane biogenesis; LPS core
biosynthesis.
[SUBCELLULAR LOCATION] Cell inner membrane {ECO:0000250};
Single-pass membrane protein {ECO:0000250}; Cytoplasmic side
{ECO:0000250}.
[SIMILARITY] Belongs to the glycosyltransferase group 1 family.
Glycosyltransferase 30 subfamily. {ECO:0000305}.
 
On Dec 1, 2006 this sequence version replaced gi:121051.
[FUNCTION] Fatty acid transfer between phosphatidylcholine and
cholesterol.
[CATALYTIC ACTIVITY] Phosphatidylcholine + a sterol =
1-acylglycerophosphocholine + a sterol ester.
[SIMILARITY] Belongs to the 'GDSL' lipolytic enzyme family.
{ECO:0000305}.
[SEQUENCE CAUTION] Sequence=CAA30260.1; Type=Frameshift;
Positions=268, 302; Evidence={ECO:0000305}.
 
On Jul 5, 2005 this sequence version replaced gi:1073892.
[FUNCTION] DEAD-box RNA helicase involved in various cellular
processes at low temperature, including ribosome biogenesis, mRNA
degradation and translation initiation.
{ECO:0000255|HAMAP-Rule:MF_00964}.
[CATALYTIC ACTIVITY] ATP + H(2)O = ADP + phosphate.
{ECO:0000255|HAMAP-Rule:MF_00964}.
[SUBCELLULAR LOCATION] Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00964}.
[SIMILARITY] Belongs to the DEAD box helicase family. DeaD
subfamily. {ECO:0000255|HAMAP-Rule:MF_00964}.
[SIMILARITY] Contains 1 helicase ATP-binding domain.
{ECO:0000255|HAMAP-Rule:MF_00964}.
[SIMILARITY] Contains 1 helicase C-terminal domain.
{ECO:0000255|HAMAP-Rule:MF_00964}.
 
[FUNCTION] Catalyzes the reversible oxidation of malate to
oxaloacetate. {ECO:0000255|HAMAP-Rule:MF_01517}.
[CATALYTIC ACTIVITY] (S)-malate + NAD(+) = oxaloacetate + NADH.
{ECO:0000255|HAMAP-Rule:MF_01517}.
[SUBUNIT] Homodimer. {ECO:0000255|HAMAP-Rule:MF_01517}.
[SIMILARITY] Belongs to the LDH/MDH superfamily. MDH type 2 family.
{ECO:0000255|HAMAP-Rule:MF_01517}.
 
[FUNCTION] Required for the formation of a threonylcarbamoyl group
on adenosine at position 37 (t(6)A37) in tRNAs that read codons
beginning with adenine. Is involved in the transfer of the
threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the
N6 group of A37, together with TsaE and TsaB. TsaD likely plays a
direct catalytic role in this reaction.
{ECO:0000255|HAMAP-Rule:MF_01445}.
[CATALYTIC ACTIVITY] L-threonylcarbamoyladenylate + adenine(37) in
tRNA = AMP + N(6)-L-threonylcarbamoyladenine(37) in tRNA.
{ECO:0000255|HAMAP-Rule:MF_01445}.
[COFACTOR] Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000255|HAMAP-Rule:MF_01445}; Note=Binds 1 Fe(2+) ion
per subunit. {ECO:0000255|HAMAP-Rule:MF_01445}.
[SUBCELLULAR LOCATION] Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01445}.
[SIMILARITY] Belongs to the KAE1 / TsaD family.
{ECO:0000255|HAMAP-Rule:MF_01445}.
 
[FUNCTION] RNA polymerase that catalyzes the synthesis of short RNA
molecules used as primers for DNA polymerase during DNA
replication. {ECO:0000255|HAMAP-Rule:MF_00974}.
[COFACTOR] Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000255|HAMAP-Rule:MF_00974}; Note=Binds 1 zinc ion
per monomer. {ECO:0000255|HAMAP-Rule:MF_00974}.
[COFACTOR] Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_00974}; Note=Binds two Mg(2+)
per subunit. {ECO:0000255|HAMAP-Rule:MF_00974}.
[SUBUNIT] Monomer. Interacts with DnaB.
{ECO:0000255|HAMAP-Rule:MF_00974}.
[DOMAIN] Contains an N-terminal zinc-binding domain, a central core
domain that contains the primase activity, and a C-terminal
DnaB-binding domain. {ECO:0000255|HAMAP-Rule:MF_00974}.
[SIMILARITY] Belongs to the DnaG primase family.
{ECO:0000255|HAMAP-Rule:MF_00974}.
[SIMILARITY] Contains 1 Toprim domain.
{ECO:0000255|HAMAP-Ru