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UniProtKB/Swiss-Prot entry P11412


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

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Entry information
Entry name G6PD_YEAST
Primary accession number P11412
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1989
Sequence was last modified on January 23, 2007 (Sequence version 4)
Annotations were last modified on    July 22, 2008 (Entry version 84)
Name and origin of the protein
Protein name Glucose-6-phosphate 1-dehydrogenase
Synonyms G6PD
EC 1.1.1.49
Gene name
Name: ZWF1
Synonyms: MET19
OrderedLocusNames: YNL241C
ORFNames: N1110
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0378-1119(90)90248-P; PubMed=2269430 [NCBI, ExPASy, EBI, Israel, Japan]
Nogae I., Johnston M.;
"Isolation and characterization of the ZWF1 gene of Saccharomyces cerevisiae, encoding glucose-6-phosphate dehydrogenase.";
Gene 96:161-169(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2001672 [NCBI, ExPASy, EBI, Israel, Japan]
Thomas D., Cherest H., Surdin-Kerjan Y.;
"Identification of the structural gene for glucose-6-phosphate dehydrogenase in yeast. Inactivation leads to a nutritional requirement for organic sulfur.";
EMBO J. 10:547-553(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1002/(SICI)1097-0061(199609)12:10B<1071::AID-YEA4>3.3.CO;2-J; PubMed=8896273 [NCBI, ExPASy, EBI, Israel, Japan]
Pandolfo D., de Antoni A., Lanfranchi G., Valle G.;
"The DNA sequence of cosmid 14-5 from chromosome XIV reveals 21 open reading frames including a novel gene encoding a globin-like domain.";
Yeast 12:1071-1076(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=9169873 [NCBI, ExPASy, EBI, Israel, Japan]
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications.";
Nature 387:93-98(1997).
[5]
PROTEIN SEQUENCE OF 2-505.
PubMed=2040308 [NCBI, ExPASy, EBI, Israel, Japan]
Persson B., Joernvall H., Wood I., Jeffery J.;
"Functionally important regions of glucose-6-phosphate dehydrogenase defined by the Saccharomyces cerevisiae enzyme and its differences from the mammalian and insect forms.";
Eur. J. Biochem. 198:485-491(1991).
[6]
PROTEIN SEQUENCE OF 185-195.
DOI=10.1021/bi00324a019; PubMed=3922403 [NCBI, ExPASy, EBI, Israel, Japan]
Jeffery J., Hobbs L., Joernvall H.;
"Glucose-6-phosphate dehydrogenase from Saccharomyces cerevisiae: characterization of a reactive lysine residue labeled with acetylsalicylic acid.";
Biochemistry 24:666-671(1985).
[7]
PROTEIN SEQUENCE OF 2-7.
DOI=10.1016/0014-5793(90)81152-E; PubMed=2387402 [NCBI, ExPASy, EBI, Israel, Japan]
Egestad B., Estonius M., Danielsson O., Persson B., Cederlund E., Kaiser R., Holmquist B., Vallee B., Pares X., Jefferey J., Joernvall H.;
"Fast atom bombardment mass spectrometry and chemical analysis in determinations of acyl-blocked protein structures.";
FEBS Lett. 269:194-196(1990).
[8]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142 AND TYR-145, AND MASS SPECTROMETRY.
DOI=10.1021/pr060559j; PubMed=17330950 [NCBI, ExPASy, EBI, Israel, Japan]
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
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
M34709; AAA34619.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X57336; CAA40611.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z69381; CAA93357.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z71517; CAA96146.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S13744; S13744.
RefSeq NP_014158.1; -.
3D structure databases
HSSP P11413; 1QKI. [HSSP ENTRY / PDB]
ModBase P11412.
Protein-protein interaction databases
DIP DIP:5061N; -.
IntAct P11412; -.
2D gel databases
SWISS-2DPAGE P11412; -.
Organism-specific databases
CYGD YNL241c; -.
SGD S000005185; ZWF1.
Yeast-GFP YNL241C.
Gene expression databases
GermOnline YNL241C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from SGD).
GO:0004345; Molecular function: glucose-6-phosphate dehydrogenase activity (inferred from mutant phenotype from SGD).
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0009051; Biological process: pentose-phosphate shunt, oxidative branch (inferred from mutant phenotype from SGD).
GO:0042542; Biological process: response to hydrogen peroxide (inferred from mutant phenotype from SGD).
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.
BLOCKS P11412.
Proteomic databases
PeptideAtlas P11412; -.
Genome annotation databases
Ensembl YNL241C; Saccharomyces cerevisiae. [Contig view]
GeneID 855480; -.
GenomeReviews Y13139_GR; YNL241C.
KEGG sce:YNL241C; -.
NMPDR fig|4932.3.peg.5223; -.
Phylogenomic databases
HOGENOM P11412; -.
Other
LinkHub P11412; -.
ProtoNet P11412.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Carbohydrate metabolism; Complete proteome; Direct protein sequencing; Glucose metabolism; NADP; Oxidoreductase; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   505  504     Glucose-6-phosphate 1-dehydrogenase. PRO_0000068107
ACT_SITE   249   249        Proton acceptor (By similarity). 
BINDING   20    20        NADP (By similarity). 
BINDING   52    52        NADP (By similarity). 
BINDING   187   187        Substrate (By similarity). 
BINDING   191   191        Substrate. 
MOD_RES   2     2        N-acetylserine. 
MOD_RES   142   142        Phosphoserine. 
MOD_RES   145   145        Phosphotyrosine. 
CONFLICT   59    59        Missing (in Ref. 5; AA sequence). 
CONFLICT   175   175        P -> A (in Ref. 1; AAA34619). 
Sequence information
Length: 505 AA [This is the length of the unprocessed precursor] Molecular weight: 57522 Da [This is the MW of the unprocessed precursor] CRC64: 9FC23E6CE599454E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSEGPVKFEK NTVISVFGAS GDLAKKKTFP ALFGLFREGY LDPSTKIFGY ARSKLSMEED 

        70         80         90        100        110        120 
LKSRVLPHLK KPHGEADDSK VEQFFKMVSY ISGNYDTDEG FDELRTQIEK FEKSANVDVP 

       130        140        150        160        170        180 
HRLFYLALPP SVFLTVAKQI KSRVYAENGI TRVIVEKPFG HDLASARELQ KNLGPLFKEE 

       190        200        210        220        230        240 
ELYRIDHYLG KELVKNLLVL RFGNQFLNAS WNRDNIQSVQ ISFKERFGTE GRGGYFDSIG 

       250        260        270        280        290        300 
IIRDVMQNHL LQIMTLLTME RPVSFDPESI RDEKVKVLKA VAPIDTDDVL LGQYGKSEDG 

       310        320        330        340        350        360 
SKPAYVDDDT VDKDSKCVTF AAMTFNIENE RWEGVPIMMR AGKALNESKV EIRLQYKAVA 

       370        380        390        400        410        420 
SGVFKDIPNN ELVIRVQPDA AVYLKFNAKT PGLSNATQVT DLNLTYASRY QDFWIPEAYE 

       430        440        450        460        470        480 
VLIRDALLGD HSNFVRDDEL DISWGIFTPL LKHIERPDGP TPEIYPYGSR GPKGLKEYMQ 

       490        500 
KHKYVMPEKH PYAWPVTKPE DTKDN 

P11412 in FASTA format

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