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UniProtKB/Swiss-Prot entry Q5PLL9

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

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Entry information
Entry name GHRB_SALPA
Primary accession number Q5PLL9
Secondary accession numbers None
Integrated into Swiss-Prot on September 2, 2008
Sequence was last modified on January 4, 2005 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 25)
Name and origin of the protein
Protein name Glyoxylate/hydroxypyruvate reductase B
Synonyms EC 1.1.1.79
EC 1.1.1.81
Gene name
Name: ghrB
OrderedLocusNames: SPA3498
From
Salmonella paratyphi A [TaxID: 54388] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Salmonella.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 9150 / SARB42;
DOI=10.1038/ng1470; PubMed=15531882 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Comparison of genome degradation in Paratyphi A and Typhi, human-restricted serovars of Salmonella enterica that cause typhoid.";
Nat. Genet. 36:1268-1274(2004).
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
CP000026; AAV79304.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_152616.1; -.
3D structure databases
ModBase Q5PLL9.
Enzyme and pathway databases
BioCyc SENT295319:SPA3498-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: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_01667; -; 1.
PBIL [Tree]
InterPro IPR006139; D-isomer_2_OHA_DHase.
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 PF00389; 2-Hacid_dh; 1.
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; 1.
PS00671; D_2_HYDROXYACID_DH_3; 1.
BLOCKS Q5PLL9.
ProtoNet Q5PLL9.
Genome annotation databases
GeneID 3175617; -.
GenomeReviews CP000026_GR; SPA3498.
KEGG spt:SPA3498; -.
NMPDR fig|295319.3.peg.3195; -.
Phylogenomic databases
HOGENOM Q5PLL9; -.
Genome annotation databases
CMR Q5PLL9; SPA3498.
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   324  324     Glyoxylate/hydroxypyruvate reductase B. PRO_0000348394
ACT_SITE   237   237        By similarity. 
ACT_SITE   266   266        By similarity. 
ACT_SITE   285   285        Proton donor (By similarity). 
Sequence information
Length: 324 AA [This is the length of the unprocessed precursor] Molecular weight: 35352 Da [This is the MW of the unprocessed precursor] CRC64: 94F1AD2A2839EFDC [This is a checksum on the sequence] 
        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
Q5PLL9 in FASTA format

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