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Protein

2-hydroxy-3-oxopropionate reductase

Gene

garR

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reduction of tatronate semialdehyde to D-glycerate.UniRule annotation1 Publication

Catalytic activityi

D-glycerate + NAD(P)+ = 2-hydroxy-3-oxopropanoate + NAD(P)H.UniRule annotation1 Publication

Pathwayi: galactarate degradation

This protein is involved in step 3 of the subpathway that synthesizes D-glycerate from galactarate.UniRule annotation1 Publication
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Galactarate dehydratase (L-threo-forming) (garD)
  2. 5-keto-4-deoxy-D-glucarate aldolase (garL)
  3. 2-hydroxy-3-oxopropionate reductase (garR)
This subpathway is part of the pathway galactarate degradation, which is itself part of Carbohydrate acid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glycerate from galactarate, the pathway galactarate degradation and in Carbohydrate acid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei95 – 951NADUniRule annotation
Active sitei170 – 1701UniRule annotation
Binding sitei238 – 2381NADUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi4 – 1815NADUniRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • D-glucarate catabolic process Source: EcoCyc
  • galactarate catabolic process Source: EcoCyc
  • glyoxylate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciEcoCyc:TSA-REDUCT-MONOMER.
ECOL316407:JW5526-MONOMER.
MetaCyc:TSA-REDUCT-MONOMER.
UniPathwayiUPA00565; UER00631.

Names & Taxonomyi

Protein namesi
Recommended name:
2-hydroxy-3-oxopropionate reductaseUniRule annotation (EC:1.1.1.60UniRule annotation1 Publication)
Alternative name(s):
Tartronate semialdehyde reductase1 PublicationUniRule annotation
Short name:
TSAR1 PublicationUniRule annotation
Gene namesi
Name:garR1 PublicationUniRule annotation
Synonyms:yhaE
Ordered Locus Names:b3125, JW5526
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11176. garR.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2942942-hydroxy-3-oxopropionate reductasePRO_0000173059Add
BLAST

Proteomic databases

EPDiP0ABQ2.
PaxDbiP0ABQ2.
PRIDEiP0ABQ2.

Expressioni

Inductioni

Induced by D-galactarate, D-glucarate and D-glycerate.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi4259488. 17 interactions.
DIPiDIP-9742N.
STRINGi511145.b3125.

Structurei

3D structure databases

ProteinModelPortaliP0ABQ2.
SMRiP0ABQ2. Positions 1-294.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the 3-hydroxyisobutyrate dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CF3. Bacteria.
COG2084. LUCA.
HOGENOMiHOG000219608.
InParanoidiP0ABQ2.
KOiK00042.
OMAiCYDIMKA.
OrthoDBiEOG6XDH0X.
PhylomeDBiP0ABQ2.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
HAMAPiMF_02032. Tartronate_sem_reduc.
InterProiIPR002204. 3-OH-isobutyrate_DH-rel_CS.
IPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR006115. 6PGDH_NADP-bd.
IPR015815. HIBADH-related.
IPR016040. NAD(P)-bd_dom.
IPR029154. NADP-bd.
IPR006398. Tartro_sem_red.
[Graphical view]
PfamiPF14833. NAD_binding_11. 1 hit.
PF03446. NAD_binding_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000103. HIBADH. 1 hit.
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01505. tartro_sem_red. 1 hit.
PROSITEiPS00895. 3_HYDROXYISOBUT_DH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0ABQ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVGFIGLGI MGKPMSKNLL KAGYSLVVAD RNPEAIADVI AAGAETASTA
60 70 80 90 100
KAIAEQCDVI ITMLPNSPHV KEVALGENGI IEGAKPGTVL IDMSSIAPLA
110 120 130 140 150
SREISEALKA KGIDMLDAPV SGGEPKAIDG TLSVMVGGDK AIFDKYYDLM
160 170 180 190 200
KAMAGSVVHT GEIGAGNVTK LANQVIVALN IAAMSEALTL ATKAGVNPDL
210 220 230 240 250
VYQAIRGGLA GSTVLDAKAP MVMDRNFKPG FRIDLHIKDL ANALDTSHGV
260 270 280 290
GAQLPLTAAV MEMMQALRAD GLGTADHSAL ACYYEKLAKV EVTR
Length:294
Mass (Da):30,427
Last modified:November 8, 2005 - v1
Checksum:i17DA392C2253278C
GO

Sequence cautioni

The sequence AAA57928.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAA14238.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAE77172.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_417594.3. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC76159; AAC76159; b3125.
BAE77172; BAE77172; BAE77172.
GeneIDi947631.
KEGGiecj:JW5526.
eco:b3125.
PATRICi32121664. VBIEscCol129921_3218.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_417594.3. NC_000913.3.

3D structure databases

ProteinModelPortaliP0ABQ2.
SMRiP0ABQ2. Positions 1-294.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259488. 17 interactions.
DIPiDIP-9742N.
STRINGi511145.b3125.

Proteomic databases

EPDiP0ABQ2.
PaxDbiP0ABQ2.
PRIDEiP0ABQ2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76159; AAC76159; b3125.
BAE77172; BAE77172; BAE77172.
GeneIDi947631.
KEGGiecj:JW5526.
eco:b3125.
PATRICi32121664. VBIEscCol129921_3218.

Organism-specific databases

EchoBASEiEB1163.
EcoGeneiEG11176. garR.

Phylogenomic databases

eggNOGiENOG4105CF3. Bacteria.
COG2084. LUCA.
HOGENOMiHOG000219608.
InParanoidiP0ABQ2.
KOiK00042.
OMAiCYDIMKA.
OrthoDBiEOG6XDH0X.
PhylomeDBiP0ABQ2.

Enzyme and pathway databases

UniPathwayiUPA00565; UER00631.
BioCyciEcoCyc:TSA-REDUCT-MONOMER.
ECOL316407:JW5526-MONOMER.
MetaCyc:TSA-REDUCT-MONOMER.

Miscellaneous databases

PROiP0ABQ2.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
HAMAPiMF_02032. Tartronate_sem_reduc.
InterProiIPR002204. 3-OH-isobutyrate_DH-rel_CS.
IPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR006115. 6PGDH_NADP-bd.
IPR015815. HIBADH-related.
IPR016040. NAD(P)-bd_dom.
IPR029154. NADP-bd.
IPR006398. Tartro_sem_red.
[Graphical view]
PfamiPF14833. NAD_binding_11. 1 hit.
PF03446. NAD_binding_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000103. HIBADH. 1 hit.
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01505. tartro_sem_red. 1 hit.
PROSITEiPS00895. 3_HYDROXYISOBUT_DH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
  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] [Europe PMC] [Abstract]
    Cited for: GENE NAME, INDUCTION.

Entry informationi

Entry nameiGARR_ECOLI
AccessioniPrimary (citable) accession number: P0ABQ2
Secondary accession number(s): P23523, Q2M984
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: March 16, 2016
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.