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Reviewed, UniProtKB/Swiss-Prot Q8FCF1 (GHRB_ECOL6)

Last modified January 19, 2010. Version 45. 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: c4372
OrganismEscherichia coli O6 [Complete proteome] [HAMAP]
Taxonomic identifier217992 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length324 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 – 324324Glyoxylate/hydroxypyruvate reductase B HAMAP MF_01667
PRO_0000348389

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q8FCF1-1 [UniParc].

Last modified September 2, 2008. Version 2.
Checksum: A6E3919F53933250

FASTA32435,396
        10         20         30         40         50         60 
MKPSVILYKA LPDDLLQRLQ EHFTVHQVAN LSPQTVEQNA AIFAEAEGLL GSNENVDAAL 

        70         80         90        100        110        120 
LEKMPKLRAT STISVGYDNF DVDALTARKI LLMHTPTVLT ETVADTLMAL VLSTARRVVE 

       130        140        150        160        170        180 
VAERVKAGEW TASIGPDWYG TDVHHKTLGI VGMGRIGMAL AQRAHFGFNM PILYNARRHH 

       190        200        210        220        230        240 
KEAEERFNAR YCNLDTLLQE SDFVCLILPL TDETHHLFGA EQFAKMKSSA IFINAGRGPV 

       250        260        270        280        290        300 
VDENALIAAL QKGEIHAAGL DVFEQEPLSV DSPLLSMANV VAVPHIGSAT HETRYGMAAC 

       310        320 
AVDNLIDALQ GKVEKNCVNP HVAD 

« Hide

References

[1]"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli."
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014075 Genomic DNA. Translation: AAN82808.1. Different initiation.
RefSeqNP_756234.2.

3D structure databases

HSSPHSSP built from PDB template 2DBZ based on UniProtKB O58320.
ModBaseSearch...

Genome annotation databases

GeneID1037406.
GenomeReviewsGene locus c4372 in contig AE014075_GR.
KEGGecc:c4372.
NMPDRfig|199310.1.peg.4277.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG731446.

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. False negative.
PS00670. D_2_HYDROXYACID_DH_2. 1 hit.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGHRB_ECOL6
AccessionPrimary (citable) accession number: Q8FCF1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: September 2, 2008
Last modified: January 19, 2010
This is version 45 of the entry and version 2 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