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Reviewed, UniProtKB/Swiss-Prot P58220 (GHRB_ECO57)

Last modified June 16, 2009. Version 54. 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: tkrA
Ordered Locus Names: Z4978, ECs4438
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length324 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

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

Catalytic activity

Glycolate + NADP+ = glyoxylate + NADPH. HAMAP MF_01667

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

Subunit structure

Homodimer Probable.

Subcellular location

Cytoplasm Probable.

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_0000076030

Sites

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

Sequences

Sequence LengthMass (Da)Tools
P58220-1 [UniParc].

Last modified July 11, 2001. Version 1.
Checksum: A6EB3399119DD250

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 YCDLDTLLQE SDFVCLILPL TDETHHLFGA EQFAKMKSSA IFINAGRGPV 

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

       310        320 
AVDNLIDALQ GKVEKNCVNP HVAD 

« Hide

References

Cross-references

Sequence databases

AE005174 Genomic DNA. Translation: AAG58702.1. Different initiation.
BA000007 Genomic DNA. Translation: BAB37861.1. Different initiation.
PIRB86030.
F91183.
RefSeqNP_290138.2.
NP_312465.2.

3D structure databases

HSSPHSSP built from PDB template 1GDH based on UniProtKB P36234.
ModBaseSearch...

Genome annotation databases

GeneID915671.
961060.
GenomeReviewsGene locus Z4978 in contig AE005174_GR.
Gene locus ECs4438 in contig BA000007_GR.
KEGGece:Z4978.
ecs:ECs4438.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP58220.

Enzyme and pathway databases

BioCycECOL83334:ECS4438-MON.

Family and domain databases

HAMAPMF_01667.
[Tree]
InterProIPR006139. D-isomer_2_OHA_DH.
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_ECO57
AccessionPrimary (citable) accession number: P58220
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2001
Last sequence update: July 11, 2001
Last modified: June 16, 2009
This is version 54 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