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UniProtKB/Swiss-Prot entry P0ABQ2


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GARR_ECOLI
Primary accession number P0ABQ2
Secondary accession numbers P23523 Q2M984
Integrated into Swiss-Prot on November 8, 2005
Sequence was last modified on November 8, 2005 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 30)
Name and origin of the protein
Protein name 2-hydroxy-3-oxopropionate reductase
Synonyms EC 1.1.1.60
Tartronate semialdehyde reductase
TSAR
Gene name
Name: garR
Synonyms: yhaE
OrderedLocusNames: b3125, JW5526
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=1705543 [NCBI, ExPASy, EBI, Israel, Japan]
Komine Y., Inokuchi H.;
"Precise mapping of the rnpB gene encoding the RNA component of RNase P in Escherichia coli K-12.";
J. Bacteriol. 173:1813-1816(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[4]
CHARACTERIZATION.
DOI=10.1021/bi981124f; PubMed=9772162 [NCBI, ExPASy, EBI, Israel, Japan]
Hubbard B.K., Koch M., Palmer D.R., Babbitt P.C., Gerlt J.A.;
"Evolution of enzymatic activities in the enolase superfamily: characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coli.";
Biochemistry 37:14369-14375(1998).
[5]
GENE NAME.
DOI=10.1128/JB.182.9.2672-2674.2000; PubMed=10762278 [NCBI, ExPASy, EBI, Israel, Japan]
Monterrubio R., Baldoma L., Obradors N., Aguilar J., Badia J.;
"A common regulator for the operons encoding the enzymes involved in D-galactarate, D-glucarate, and D-glycerate utilization in Escherichia coli.";
J. Bacteriol. 182:2672-2674(2000).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D90212; BAA14238.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U18997; AAA57928.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC76159.3; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE77172.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq AP_003671.1; -.
NP_417594.3; -.
3D structure databases
SMR P0ABQ2; 1-294.
ModBase P0ABQ2.
Enzyme and pathway databases
BioCyc EcoCyc:TSA-REDUCT-MON; -.
MetaCyc:TSA-REDUCT-MON; -.
Organism-specific databases
EchoBASE EB1163; -.
EcoGene EG11176; garR.
Ontologies
GO
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR002204; 3-OH-isobutyrate_DHase-rel_CS.
IPR015815; 3hydroxyacid_DHase/Rdtase.
IPR006183; 6-phosphogluconate_DHase.
IPR006115; 6PGDH_NAD-bd.
IPR013328; DHase_multihelical.
IPR016040; NAD(P)-bd.
IPR006398; Tartro_sem_red.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
G3DSA:1.10.1040.10; Opine_DH; 1.
PANTHER PTHR22981; 3hydroxy_acid_DH; 1.
Pfam PF03446; NAD_binding_2; 1.
Pfam graphical view of domain structure.
PRINTS PR00076; 6PGDHDRGNASE.
TIGRFAMs TIGR01505; tartro_sem_red; 1.
PROSITE PS00895; 3_HYDROXYISOBUT_DH; 1.
BLOCKS P0ABQ2.
ProtoNet P0ABQ2.
Genome annotation databases
GeneID 947631; -.
GenomeReviews U00096_GR; b3125.
AP009048_GR; JW5526.
KEGG ecj:JW5526; -.
eco:b3125; -.
Phylogenomic databases
HOGENOM P0ABQ2; -.
Genome annotation databases
CMR P0ABQ2; b3125.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   294  294     2-hydroxy-3-oxopropionate reductase. PRO_0000173059
ACT_SITE   170   170        By similarity. 
Sequence information
Length: 294 AA [This is the length of the unprocessed precursor] Molecular weight: 30427 Da [This is the MW of the unprocessed precursor] CRC64: 17DA392C2253278C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKVGFIGLGI MGKPMSKNLL KAGYSLVVAD RNPEAIADVI AAGAETASTA KAIAEQCDVI 

        70         80         90        100        110        120 
ITMLPNSPHV KEVALGENGI IEGAKPGTVL IDMSSIAPLA SREISEALKA KGIDMLDAPV 

       130        140        150        160        170        180 
SGGEPKAIDG TLSVMVGGDK AIFDKYYDLM KAMAGSVVHT GEIGAGNVTK LANQVIVALN 

       190        200        210        220        230        240 
IAAMSEALTL ATKAGVNPDL VYQAIRGGLA GSTVLDAKAP MVMDRNFKPG FRIDLHIKDL 

       250        260        270        280        290 
ANALDTSHGV GAQLPLTAAV MEMMQALRAD GLGTADHSAL ACYYEKLAKV EVTR 

P0ABQ2 in FASTA format

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