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Reviewed, UniProtKB/Swiss-Prot A7ZYY6 (GHRA_ECOHS)

Last modified January 19, 2010. Version 17. 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 A
    EC=1.1.1.79
    EC=1.1.1.81
Alternative name(s):
    2-ketoacid reductase
Gene names
Name: ghrA
Ordered Locus Names: EcHS_A1151
OrganismEscherichia coli O9:H4 (strain HS) [Complete proteome] [HAMAP]
Taxonomic identifier331112 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length312 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_01666

Catalytic activity

Glycolate + NADP+ = glyoxylate + NADPH. HAMAP MF_01666

D-glycerate + NAD(P)+ = hydroxypyruvate + NAD(P)H. HAMAP MF_01666

Subcellular location

Cytoplasm Probable HAMAP MF_01666.

Sequence similarities

Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. GhrA 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 functioncofactor 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 – 312312Glyoxylate/hydroxypyruvate reductase A HAMAP MF_01666
PRO_0000348356

Sites

Active site2271 By similarity
Active site2751Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
A7ZYY6-1 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 5B2F96722CDC6B40

FASTA31235,315
        10         20         30         40         50         60 
MDIIFYHPTF DTQWWIEALR KAIPQARVRA WKSGDNDSAD YALVWHPPVE MLAGRDLKAV 

        70         80         90        100        110        120 
FALGAGVDSI LSKLQAHPEM LNPSVPLFRL EDTGMGEQMQ EYAVSQVLHW FRRFDDYRIQ 

       130        140        150        160        170        180 
QNSSHWQPLP EYHREDFTIG ILGAGVLGSK VAQSLQTWRF PLRCWSRTRK SWPGVQSFAG 

       190        200        210        220        230        240 
REELSAFLSQ CRVLINLLPN TPETVGIINQ QLLEKLPDGA YLLNLARGVH VVEDDLLAAL 

       250        260        270        280        290        300 
DSGKVKGAML DVFNREPLPP ESPLWQHPRV TITPHVAAIT RPAEAVEYIS RTIAQLEKGE 

       310 
KVCGQVDRAR GY 

« Hide

References

[1]"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000802 Genomic DNA. Translation: ABV05490.1.
RefSeqYP_001457873.1.

3D structure databases

SMRA7ZYY6. Positions 1-312.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7ZYY6.

Genome annotation databases

GeneID5591305.
GenomeReviewsGene locus EcHS_A1151 in contig CP000802_GR.
KEGGecx:EcHS_A1151.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0111.
HOGENOMHBG731446.
OMAYALVWRA.

Family and domain databases

HAMAPMF_01666. 2-Hacid_dh_C_GhrA.
[Tree]
InterProIPR006140. D-isomer_2_OHA_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PfamPF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]
PROSITEPS00065. D_2_HYDROXYACID_DH_1. False negative.
PS00670. D_2_HYDROXYACID_DH_2. False negative.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGHRA_ECOHS
AccessionPrimary (citable) accession number: A7ZYY6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: October 23, 2007
Last modified: January 19, 2010
This is version 17 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