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UniProtKB/Swiss-Prot entry P0AC53


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

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Entry information
Entry name G6PD_ECOLI
Primary accession number P0AC53
Secondary accession numbers P22992 P78069 Q60134 Q60139
Integrated into Swiss-Prot on November 8, 2005
Sequence was last modified on November 8, 2005 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 31)
Name and origin of the protein
Protein name Glucose-6-phosphate 1-dehydrogenase
Synonyms G6PD
EC 1.1.1.49
Gene name
Name: zwf
OrderedLocusNames: b1852, JW1841
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=1704005 [NCBI, ExPASy, EBI, Israel, Japan]
Rowley D.L., Wolf R.E. Jr.;
"Molecular characterization of the Escherichia coli K-12 zwf gene encoding glucose 6-phosphate dehydrogenase.";
J. Bacteriol. 173:968-977(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1093/dnares/3.6.379; PubMed=9097040 [NCBI, ExPASy, EBI, Israel, Japan]
Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T.;
"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map.";
DNA Res. 3:379-392(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 72-368.
STRAIN=Various ECOR strains;
PubMed=7973728 [NCBI, ExPASy, EBI, Israel, Japan]
Guttman D.S., Dykhuizen D.E.;
"Clonal divergence in Escherichia coli as a result of recombination, not mutation.";
Science 266:1380-1383(1994).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 321-491.
STRAIN=K12;
DOI=10.1016/0378-1119(93)90362-7; PubMed=8344525 [NCBI, ExPASy, EBI, Israel, Japan]
Carter A.T., Pearson B.M., Dickinson J.R., Lancashire W.E.;
"Sequence of the Escherichia coli K-12 edd and eda genes of the Entner-Doudoroff pathway.";
Gene 130:155-156(1993).
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
M55005; AAA24775.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC74922.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA15660.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13783; AAA57018.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13784; AAA57019.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13785; AAA57020.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13786; AAA57021.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13787; AAA57022.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13788; AAA57023.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13789; AAA57024.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13790; AAA57025.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13791; AAA57026.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13792; AAA57027.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13793; AAA57028.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U13794; AAA57029.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X63694; CAA45220.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR D64947; D64947.
RefSeq AP_002472.1; -.
NP_416366.1; -.
3D structure databases
HSSP P11413; 1QKI. [HSSP ENTRY / PDB]
ModBase P0AC53.
Protein-protein interaction databases
IntAct P0AC53; 46.
Enzyme and pathway databases
BioCyc EcoCyc:GLU6PDEHYDROG-MON; -.
MetaCyc:GLU6PDEHYDROG-MON; -.
2D gel databases
SWISS-2DPAGE P0AC53; -.
ECO2DBASE F048.8; 6TH EDITION.
Organism-specific databases
EchoBASE EB1203; -.
EcoGene EG11221; zwf.
Ontologies
GO
GO:0004345; Molecular function: glucose-6-phosphate dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006006; Biological process: glucose metabolic process (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
InterPro IPR001282; Glc-6-P_DHase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR23429; G6PDH; 1.
Pfam PF02781; G6PD_C; 1.
PF00479; G6PD_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000110; G6PD; 1.
PRINTS PR00079; G6PDHDRGNASE.
ProDom PD001129; G6PD; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00871; zwf; 1.
PROSITE PS00069; G6P_DEHYDROGENASE; 1.
Genome annotation databases
GeneID 946370; -.
GenomeReviews AP009048_GR; JW1841.
U00096_GR; b1852.
KEGG ecj:JW1841; -.
eco:b1852; -.
Phylogenomic databases
HOGENOM P0AC53; -.
Genome annotation databases
CMR P0AC53; b1852.
Other
ProtoNet P0AC53.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Carbohydrate metabolism; Complete proteome; Glucose metabolism; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   491  491     Glucose-6-phosphate 1-dehydrogenase. PRO_0000068118
ACT_SITE   239   239        Proton acceptor (By similarity). 
BINDING   18    18        NADP (By similarity). 
BINDING   50    50        NADP (By similarity). 
BINDING   177   177        Substrate (By similarity). 
BINDING   181   181        Substrate (By similarity). 
BINDING   344   344        Substrate (By similarity). 
VARIANT   100   100  1     S -> N (in strain: ECOR 4 and ECOR 10). 
CONFLICT   268   293        LKSLRRIDRSNVREKTVRGQYTAGFA -> PEVSSPHRPLQRTRKNRTRAIYCVP (in Ref. 1; AAA24775). 
Sequence information
Length: 491 AA [This is the length of the unprocessed precursor] Molecular weight: 55704 Da [This is the MW of the unprocessed precursor] CRC64: 263F07D298EAFCD3 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAVTQTAQAC DLVIFGAKGD LARRKLLPSL YQLEKAGQLN PDTRIIGVGR ADWDKAAYTK 

        70         80         90        100        110        120 
VVREALETFM KETIDEGLWD TLSARLDFCN LDVNDTAAFS RLGAMLDQKN RITINYFAMP 

       130        140        150        160        170        180 
PSTFGAICKG LGEAKLNAKP ARVVMEKPLG TSLATSQEIN DQVGEYFEEC QVYRIDHYLG 

       190        200        210        220        230        240 
KETVLNLLAL RFANSLFVNN WDNRTIDHVE ITVAEEVGIE GRWGYFDKAG QMRDMIQNHL 

       250        260        270        280        290        300 
LQILCMIAMS PPSDLSADSI RDEKVKVLKS LRRIDRSNVR EKTVRGQYTA GFAQGKKVPG 

       310        320        330        340        350        360 
YLEEEGANKS SNTETFVAIR VDIDNWRWAG VPFYLRTGKR LPTKCSEVVV YFKTPELNLF 

       370        380        390        400        410        420 
KESWQDLPQN KLTIRLQPDE GVDIQVLNKV PGLDHKHNLQ ITKLDLSYSE TFNQTHLADA 

       430        440        450        460        470        480 
YERLLLETMR GIQALFVRRD EVEEAWKWVD SITEAWAMDN DAPKPYQAGT WGPVASVAMI 

       490 
TRDGRSWNEF E 

P0AC53 in FASTA format

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