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Reviewed, UniProtKB/Swiss-Prot A1JT62 (GHRB_YERE8)

Last modified January 19, 2010. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glyoxylate/hydroxypyruvate reductase B
    EC=1.1.1.79
    EC=1.1.1.81
Gene names
Name: ghrB
Ordered Locus Names: YE4159
OrganismYersinia enterocolitica serotype O:8 / biotype 1B (strain 8081) [Complete proteome] [HAMAP]
Taxonomic identifier393305 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length326 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively By similarity. HAMAP MF_01667

Catalytic activity

Glycolate + NADP+ = glyoxylate + NADPH. HAMAP MF_01667

D-glycerate + NAD(P)+ = hydroxypyruvate + NAD(P)H. HAMAP MF_01667

Subunit structure

Homodimer By similarity. HAMAP MF_01667

Subcellular location

Cytoplasm Probable HAMAP MF_01667.

Sequence similarities

Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. GhrB subfamily.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandNAD
NADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: HAMAP

   Molecular functionNAD or NADH binding

Inferred from electronic annotation. Source: InterPro

glyoxylate reductase (NADP) activity

Inferred from electronic annotation. Source: HAMAP

hydroxypyruvate reductase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 326326Glyoxylate/hydroxypyruvate reductase B HAMAP MF_01667
PRO_0000348405

Sites

Active site2371 By similarity
Active site2661 By similarity
Active site2851Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
A1JT62-1 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 44D7E34E4330849E

FASTA32635,256
        10         20         30         40         50         60 
MKPSIVLYKS IPADLHQRLE QHFTVNSFEG LSSDNQPELL SALQQAEGLI GSGGKIDQAF 

        70         80         90        100        110        120 
LERAPKLRAA STISVGYDNF DVDALSQRGI ALMHTPTVLT ETVADTMMAL VLSSARRVVE 

       130        140        150        160        170        180 
LAERVKAGEW QDSIGDDWFG VDVHHKTIGI LGMGRIGMAL AQRAHFGFSM PVLYTSRRPH 

       190        200        210        220        230        240 
EAAEKRFGAR RCSLDTLLAE VDFLCITLPM TEQTYHMIGP EQLAKMKSSA ILINAGRGPV 

       250        260        270        280        290        300 
VDEQALIAAL QDGTIHAAGL DVFAQEPLPV ESPLLKLPNV VAVPHIGSAT HETRYNMAAC 

       310        320 
AVDNLIAALT GTVTENCVNP QVLQQA 

« Hide

References

[1]"The complete genome sequence and comparative genome analysis of the high pathogenicity Yersinia enterocolitica strain 8081."
Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L., Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T., Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S., Sanders M., Whitehead S. expand/collapse author list , Quail M.A., Dougan G., Parkhill J., Prentice M.B.
PLoS Genet. 2:2039-2051(2006) [PubMed: 17173484] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM286415 Genomic DNA. Translation: CAL14175.1.
RefSeqYP_001008293.1.

3D structure databases

SMRA1JT62. Positions 1-324.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1JT62.

Genome annotation databases

GeneID4716553.
GenomeReviewsGene locus YE4159 in contig AM286415_GR.
KEGGyen:YE4159.
NMPDRfig|630.2.peg.4084.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1052.
HOGENOMHBG731446.
OMADSPLRTH.
PhylomeDBA1JT62.

Family and domain databases

HAMAPMF_01667. 2-Hacid_dh_C_GhrB.
[Tree]
InterProIPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR006140. D-isomer_2_OHA_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PfamPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]
PROSITEPS00065. D_2_HYDROXYACID_DH_1. 1 hit.
PS00670. D_2_HYDROXYACID_DH_2. False negative.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGHRB_YERE8
AccessionPrimary (citable) accession number: A1JT62
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: February 6, 2007
Last modified: January 19, 2010
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents