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UniProtKB/Swiss-Prot entry A7ZTA0

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

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Entry information
Entry name GHRB_ECO24
Primary accession number A7ZTA0
Secondary accession numbers None
Integrated into Swiss-Prot on September 2, 2008
Sequence was last modified on October 23, 2007 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 10)
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: EcE24377A_4049
From
Escherichia coli O139:H28 (strain E24377A / ETEC) [TaxID: 331111] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/JB.00619-08; PubMed=18676672 [NCBI, ExPASy, EBI, Israel, Japan]
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.;
"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates.";
J. Bacteriol. 190:6881-6893(2008).
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
CP000800; ABV17627.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001465029.1; -.
3D structure databases
ModBase A7ZTA0.
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:0051287; Molecular function: NAD binding (inferred from electronic annotation from InterPro).
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.
Genome annotation databases
GeneID 5590663; -.
GenomeReviews CP000800_GR; EcE24377A_4049.
KEGG ecw:EcE24377A_4049; -.
CMR A7ZTA0; EcE24377A_4049.
Other
ProtoNet A7ZTA0.
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_0000348387
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: 35396 Da [This is the MW of the unprocessed precursor] CRC64: A6EB3399119DD250 [This is a checksum on the sequence] 
        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
A7ZTA0 in FASTA format

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