ID B6K1N7_SCHJY Unreviewed; 477 AA.
AC B6K1N7;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000256|RuleBase:RU362120};
DE EC=1.1.1.49 {ECO:0000256|RuleBase:RU362120};
GN Name=gcd1 {ECO:0000313|JaponicusDB:SJAG_02148};
GN ORFNames=SJAG_02148 {ECO:0000313|EMBL:EEB07068.1};
OS Schizosaccharomyces japonicus (strain yFS275 / FY16936) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=402676 {ECO:0000313|EMBL:EEB07068.1, ECO:0000313|Proteomes:UP000001744};
RN [1] {ECO:0000313|EMBL:EEB07068.1, ECO:0000313|Proteomes:UP000001744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=yFS275 / FY16936 {ECO:0000313|Proteomes:UP000001744};
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
CC -!- FUNCTION: Catalyzes the rate-limiting step of the oxidative pentose-
CC phosphate pathway, which represents a route for the dissimilation of
CC carbohydrates besides glycolysis. The main function of this enzyme is
CC to provide reducing power (NADPH) and pentose phosphates for fatty acid
CC and nucleic acid synthesis. {ECO:0000256|ARBA:ARBA00025382}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-
CC lactone + H(+) + NADPH; Xref=Rhea:RHEA:15841, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57955, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:61548; EC=1.1.1.49;
CC Evidence={ECO:0000256|ARBA:ARBA00000740,
CC ECO:0000256|RuleBase:RU362120};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC 1/3. {ECO:0000256|RuleBase:RU362120}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC {ECO:0000256|RuleBase:RU362120}.
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DR EMBL; KE651166; EEB07068.1; -; Genomic_DNA.
DR RefSeq; XP_002173361.1; XM_002173325.2.
DR AlphaFoldDB; B6K1N7; -.
DR STRING; 402676.B6K1N7; -.
DR EnsemblFungi; EEB07068; EEB07068; SJAG_02148.
DR GeneID; 7052077; -.
DR JaponicusDB; SJAG_02148; gcd1.
DR VEuPathDB; FungiDB:SJAG_02148; -.
DR eggNOG; KOG0563; Eukaryota.
DR HOGENOM; CLU_013524_2_0_1; -.
DR OMA; HEEMYMK; -.
DR OrthoDB; 989808at2759; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000001744; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0047935; F:glucose 1-dehydrogenase (NADP+) activity; IEA:EnsemblFungi.
DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IBA:GO_Central.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_00966; G6PD; 1.
DR InterPro; IPR001282; G6P_DH.
DR InterPro; IPR022675; G6P_DH_C.
DR InterPro; IPR022674; G6P_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR00871; zwf; 1.
DR PANTHER; PTHR23429; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE G6PD; 1.
DR PANTHER; PTHR23429:SF19; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE GCD1; 1.
DR Pfam; PF02781; G6PD_C; 1.
DR Pfam; PF00479; G6PD_N; 1.
DR PIRSF; PIRSF000110; G6PD; 1.
DR PRINTS; PR00079; G6PDHDRGNASE.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU362120};
KW Glucose metabolism {ECO:0000256|ARBA:ARBA00022526,
KW ECO:0000256|RuleBase:RU362120}; NADP {ECO:0000256|RuleBase:RU362120};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362120};
KW Reference proteome {ECO:0000313|Proteomes:UP000001744}.
FT DOMAIN 5..183
FT /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF00479"
FT DOMAIN 188..476
FT /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02781"
SQ SEQUENCE 477 AA; 54655 MW; 176091ACFED61E8F CRC64;
MLTIIVFGGS GHVAKTMIYP ALFLLYARQL LPSNSKIIGF ARSDLSREDF EMRVVSRVSK
ESFPFYTNDT ITAFVEHCVY FRGSYTDENS FVKLNDYIKG FEAENLSSRA KRIFYLGIPP
SLIKSVSMAL AKLDQNLNGD NRLIIEKPVG DSLESARDLL EHIRSVWPIE NTYKVDHYLG
MEMFDALLMM RFANPLFANV WTSEFVESIH VTLREQASCE GRSGYYDSSG VLRDNVQNHL
LQLLCSVAMD EPKSLEQSDV AAAKIAFLRS IRPLEEKDLL LGQYIKSKDR QTVGYRELEG
VAKDSNTPTF AVCQLHVDND RWKGVPIVIS SGKGLKDSFC EVRIVFKNRE NGLFRNKPNM
YNRFIAQIFP RMIASFELNV KEPGFTFMMT KVASTMDYQQ SFSRGNMPLP YERVLWDVIN
SSHSHFVTDE EILLEWQIVD KVLDLPNKKP PLPYQFGSDC GPRAVEDFMK ERNMSWD
//
