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UniProtKB/Swiss-Prot entry Q31Z89


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GHRA_SHIBS
Primary accession number Q31Z89
Secondary accession numbers None
Integrated into Swiss-Prot on September 2, 2008
Sequence was last modified on September 2, 2008 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 20)
Name and origin of the protein
Protein name Glyoxylate/hydroxypyruvate reductase A
Synonyms EC 1.1.1.79
EC 1.1.1.81
2-ketoacid reductase
Gene name
Name: ghrA
OrderedLocusNames: SBO_2035
From
Shigella boydii serotype 4 (strain Sb227) [TaxID: 300268] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Shigella.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1093/nar/gki954; PubMed=16275786 [NCBI, ExPASy, EBI, Israel, Japan]
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., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J., Jin Q.;
"Genome dynamics and diversity of Shigella species, the etiologic agents of bacillary dysentery.";
Nucleic Acids Res. 33:6445-6458(2005).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
CP000036; ABB66619.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_408447.1; -.
3D structure databases
ModBase Q31Z89.
Enzyme and pathway databases
BioCyc SBOY300268:SBO_2035-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from HAMAP).
GO:0048037; Molecular function: cofactor binding (inferred from electronic annotation from InterPro).
GO:0030267; Molecular function: glyoxylate reductase (NADP) activity (inferred from electronic annotation from HAMAP).
GO:0016618; Molecular function: hydroxypyruvate reductase activity (inferred from electronic annotation from HAMAP).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
HAMAP MF_01666; -; 1.
PBIL [Tree]
InterPro IPR006140; D-isomer_2_OHA_DHase_NAD-bd.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
Pfam PF02826; 2-Hacid_dh_C; 1.
Pfam graphical view of domain structure.
PROSITE PS00065; D_2_HYDROXYACID_DH_1; FALSE_NEG.
PS00670; D_2_HYDROXYACID_DH_2; FALSE_NEG.
PS00671; D_2_HYDROXYACID_DH_3; 1.
ProtoNet Q31Z89.
Genome annotation databases
GeneID 3781018; -.
GenomeReviews CP000036_GR; SBO_2035.
KEGG sbo:SBO_2035; -.
Phylogenomic databases
HOGENOM Q31Z89; -.
Genome annotation databases
CMR Q31Z89; SBO_2035.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; NAD; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   312  312     Glyoxylate/hydroxypyruvate reductase A. PRO_0000348375
ACT_SITE   227   227        By similarity. 
ACT_SITE   275   275        Proton donor (By similarity). 
Sequence information
Length: 312 AA [This is the length of the unprocessed precursor] Molecular weight: 35373 Da [This is the MW of the unprocessed precursor] CRC64: AB2A95B0A4D9689D [This is a checksum on the sequence]
        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 EYHWEDFTIG 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 

Q31Z89 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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