2-hydroxy-3-oxopropionate reductase - Escherichia coli (strain K12)

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P0ABQ2 (GARR_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 58. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
2-hydroxy-3-oxopropionate reductase
EC=1.1.1.60

Alternative name(s):
Tartronate semialdehyde reductase
Short name=TSAR

Gene names

Name:	garR
Synonyms:	yhaE
Ordered Locus Names:	b3125, JW5526

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	294 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	(R)-glycerate + NAD(P)⁺ = 2-hydroxy-3-oxopropanoate + NAD(P)H.
Pathway	Carbohydrate acid metabolism; D-galactarate degradation; D-glycerate from D-galactarate: step 3/3.
Sequence similarities	Belongs to the 3-hydroxyisobutyrate dehydrogenase family.
Sequence caution	The sequence AAA57928.1 differs from that shown. Reason: Erroneous initiation. The sequence BAA14238.1 differs from that shown. Reason: Erroneous initiation. The sequence BAE77172.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	D-galactarate catabolic process Inferred from direct assay Ref.4. Source: EcoCyc D-glucarate catabolic process Inferred from direct assay Ref.4. Source: EcoCyc glyoxylate metabolic process Inferred from electronic annotation. Source: InterPro pentose-phosphate shunt Inferred from electronic annotation. Source: InterPro valine metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	2-hydroxy-3-oxopropionate reductase activity Inferred from direct assay Ref.4. Source: EcoCyc 3-hydroxyisobutyrate dehydrogenase activity Inferred from electronic annotation. Source: InterPro coenzyme binding Inferred from electronic annotation. Source: InterPro nucleotide binding Inferred from electronic annotation. Source: InterPro phosphogluconate dehydrogenase (decarboxylating) activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 294

294

2-hydroxy-3-oxopropionate reductase

PRO_0000173059

Regions

Nucleotide binding

4 – 18

NAD By similarity

Sites

Active site

170

By similarity

Binding site

NAD By similarity

Binding site

238

NAD By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P0ABQ2 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 17DA392C2253278C
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FASTA

294

30,427

        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

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Precise mapping of the rnpB gene encoding the RNA component of RNase P in Escherichia coli K-12." Komine Y., Inokuchi H. J. Bacteriol. 173:1813-1816(1991) [PubMed: 1705543] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"The complete genome sequence of Escherichia coli K-12." 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. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Evolution of enzymatic activities in the enolase superfamily: characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coli." Hubbard B.K., Koch M., Palmer D.R., Babbitt P.C., Gerlt J.A. Biochemistry 37:14369-14375(1998) [PubMed: 9772162] [Abstract] Cited for: CHARACTERIZATION.
[5]	"A common regulator for the operons encoding the enzymes involved in D-galactarate, D-glucarate, and D-glycerate utilization in Escherichia coli." Monterrubio R., Baldoma L., Obradors N., Aguilar J., Badia J. J. Bacteriol. 182:2672-2674(2000) [PubMed: 10762278] [Abstract] Cited for: GENE NAME.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D90212 Genomic DNA. Translation: BAA14238.1. Different initiation. U18997 Genomic DNA. Translation: AAA57928.1. Different initiation. U00096 Genomic DNA. Translation: AAC76159.3. AP009048 Genomic DNA. Translation: BAE77172.1. Different initiation.
RefSeq	NP_417594.3. NC_000913.2.
3D structure databases
ProteinModelPortal	P0ABQ2.
SMR	P0ABQ2. Positions 1-294.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000003520; EBESCP00000003520; EBESCG00000002878. EBESCT00000018162; EBESCP00000017453; EBESCG00000017217.
GeneID	947631.
GenomeReviews	Gene locus JW5526 in contig AP009048_GR. Gene locus b3125 in contig U00096_GR.
KEGG	ecj:JW5526. eco:b3125.
PATRIC	32121664. VBIEscCol129921_3218.
Organism-specific databases
EchoBASE	EB1163.
EcoGene	EG11176. garR.
Phylogenomic databases
eggNOG	COG2084.
GeneTree	EBGT00050000009837.
HOGENOM	HBG729179.
OMA	WSRRRES.
PhylomeDB	P0ABQ2.
ProtClustDB	PRK11559.
Enzyme and pathway databases
BioCyc	EcoCyc:TSA-REDUCT-MONOMER. MetaCyc:TSA-REDUCT-MONOMER.
Gene expression databases
Genevestigator	P0ABQ2.
Family and domain databases
InterPro	IPR002204. 3-OH-isobutyrate_DH-rel_CS. IPR015815. 3hydroxyacid_DH/Rdtase. IPR008927. 6-PGluconate_DH_C-like. IPR006115. 6PGDH_NADP-bd. IPR013328. DH_multihelical. IPR016040. NAD(P)-bd_dom. IPR006398. Tartro_sem_red. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:1.10.1040.10. Opine_DH. 1 hit.
KO	K00042.
PANTHER	PTHR22981. 3hydroxy_acid_DH. 1 hit.
Pfam	PF03446. NAD_binding_2. 1 hit. [Graphical view]
SUPFAM	SSF48179. 6DGDH_C_like. 1 hit.
TIGRFAMs	TIGR01505. Tartro_sem_red. 1 hit.
PROSITE	PS00895. 3_HYDROXYISOBUT_DH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GARR_ECOLI

Accession

Primary (citable) accession number: P0ABQ2
Secondary accession number(s): P23523, Q2M984

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	November 8, 2005
Last modified:	January 25, 2012
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents