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Reviewed, UniProtKB/Swiss-Prot Q5PLL9 (GHRB_SALPA)

Last modified June 16, 2009. Version 29. 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: SPA3498
OrganismSalmonella paratyphi A [Complete proteome] [HAMAP]
Taxonomic identifier54388 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

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 By similarity.

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_0000348394

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q5PLL9-1 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 94F1AD2A2839EFDC

FASTA32435,352
        10         20         30         40         50         60 
MKPSIILYKT LPDDLLHRLE AHFTVTQVPN LHPETVARHA QAFASAQGLL GASETVNRAL 

        70         80         90        100        110        120 
LEKMPALRAA STISVGYDNV EVDALTARKI VLMHTPAVLT ETVADTVMAL MLATARRVVD 

       130        140        150        160        170        180 
VAERVKAGEW TESIGPAWFG VDVHHKTLGI VGMGRIGMAL AQRAHFGFTM PVLYHARRRH 

       190        200        210        220        230        240 
QEAEDRFNAR YCDLDTLLQE ADFVCVILPL TTETRHLFGT TQFARMKSSA IFINAGRGPV 

       250        260        270        280        290        300 
VDENALIAAL QNGEIYAAGL DVFEHEPLSV DSPLLNMSNV VAVPHIGSAT HETRYNMMAC 

       310        320 
AVDNLIDALQ GKIEKNCVNP QAAG 

« Hide

References

[1]"Comparison of genome degradation in Paratyphi A and Typhi, human-restricted serovars of Salmonella enterica that cause typhoid."
McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S., Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R., Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F. expand/collapse author list , Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W., Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M., Warren W., Florea L., Spieth J., Wilson R.K.
Nat. Genet. 36:1268-1274(2004) [PubMed: 15531882] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 9150 / SARB42.

Cross-references

Sequence databases

CP000026 Genomic DNA. Translation: AAV79304.1.
RefSeqYP_152616.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3175617.
GenomeReviewsGene locus SPA3498 in contig CP000026_GR.
KEGGspt:SPA3498.
NMPDRfig|295319.3.peg.3195.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ5PLL9.
OMAQ5PLL9. MARCAVE.

Enzyme and pathway databases

BioCycSENT295319:SPA3498-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_SALPA
AccessionPrimary (citable) accession number: Q5PLL9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: January 4, 2005
Last modified: June 16, 2009
This is version 29 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