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Reviewed, UniProtKB/Swiss-Prot Q3Z393 (GHRA_SHISS)

Last modified June 16, 2009. Version 24. 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: SSON_1042
OrganismShigella sonnei (strain Ss046) [Complete proteome] [HAMAP]
Taxonomic identifier300269 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

Protein attributes

Sequence length312 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_01666

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

Subcellular location

Cytoplasm Probable.

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_0000348377

Sites

Active site2271 By similarity
Active site2751Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3Z393-1 [UniParc].

Last modified September 2, 2008. Version 2.
Checksum: 5B2F966D11DC6B40

FASTA31235,343
        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 
RVCGQVDRAR GY 

« Hide

References

[1]"Genome dynamics and diversity of Shigella species, the etiologic agents of bacillary dysentery."
Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J., Xu J. expand/collapse author list , Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J., Jin Q.
Nucleic Acids Res. 33:6445-6458(2005) [PubMed: 16275786] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000038 Genomic DNA. Translation: AAZ87769.1. Different initiation.
RefSeqYP_310004.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3670012.
GenomeReviewsGene locus SSON_1042 in contig CP000038_GR.
KEGGssn:SSON_1042.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ3Z393.

Enzyme and pathway databases

BioCycSSON300269:SSO_1042-MON.

Family and domain databases

HAMAPMF_01666.
[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_SHISS
AccessionPrimary (citable) accession number: Q3Z393
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: September 2, 2008
Last modified: June 16, 2009
This is version 24 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