ID   G6PD_SCHPO              Reviewed;         500 AA.
AC   O00091; Q9UT26;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   27-MAR-2024, entry version 164.
DE   RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000312|PomBase:SPAC3A12.18};
DE            Short=G6PD;
DE            EC=1.1.1.49 {ECO:0000250|UniProtKB:P11413};
GN   Name=zwf1 {ECO:0000312|PomBase:SPAC3A12.18};
GN   ORFNames=SPAC3A12.18, SPAC9.01;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
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 (By similarity).
CC       {ECO:0000250|UniProtKB:P11413}.
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:0000250|UniProtKB:P11413};
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC       1/3. {ECO:0000250|UniProtKB:P11413}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; CU329670; CAB08746.1; -; Genomic_DNA.
DR   PIR; T39186; T39186.
DR   RefSeq; NP_593344.2; NM_001018776.2.
DR   AlphaFoldDB; O00091; -.
DR   SMR; O00091; -.
DR   BioGRID; 279629; 3.
DR   IntAct; O00091; 1.
DR   MINT; O00091; -.
DR   STRING; 284812.O00091; -.
DR   iPTMnet; O00091; -.
DR   MaxQB; O00091; -.
DR   PaxDb; 4896-SPAC3A12-18-1; -.
DR   EnsemblFungi; SPAC3A12.18.1; SPAC3A12.18.1:pep; SPAC3A12.18.
DR   GeneID; 2543200; -.
DR   KEGG; spo:SPAC3A12.18; -.
DR   PomBase; SPAC3A12.18; zwf1.
DR   VEuPathDB; FungiDB:SPAC3A12.18; -.
DR   eggNOG; KOG0563; Eukaryota.
DR   HOGENOM; CLU_013524_2_3_1; -.
DR   InParanoid; O00091; -.
DR   OMA; ERAGYYE; -.
DR   PhylomeDB; O00091; -.
DR   Reactome; R-SPO-5628897; TP53 Regulates Metabolic Genes.
DR   Reactome; R-SPO-71336; Pentose phosphate pathway.
DR   UniPathway; UPA00115; UER00408.
DR   PRO; PR:O00091; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IDA:PomBase.
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; IPR019796; G6P_DH_AS.
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:SF0; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE; 1.
DR   PANTHER; PTHR23429; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE G6PD; 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.
DR   PROSITE; PS00069; G6P_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cytoplasm; Glucose metabolism; NADP;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..500
FT                   /note="Glucose-6-phosphate 1-dehydrogenase"
FT                   /id="PRO_0000068106"
FT   ACT_SITE        247
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P11411"
FT   BINDING         18..25
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P11413"
FT   BINDING         52
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P11413"
FT   BINDING         155
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P11413"
FT   BINDING         155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P11413"
FT   BINDING         185..189
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P11413"
FT   BINDING         223
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P11413"
FT   BINDING         242
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P11413"
FT   BINDING         341
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P11413"
FT   BINDING         375
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P11413"
SQ   SEQUENCE   500 AA;  57204 MW;  6706DD0847762A22 CRC64;
     MSSANLSIKE NGAMVVFGAS GDLSKKKTFP ALFSLFSEGR LPKDIRIVGY ARSKIEHEDF
     LDRITQNIKI DEEDSQAKEK LEEFKKRCSY YRGSYDKPED FEGLNSHLCE REGDRSTHNR
     IFYLALPPDV FVSVATNLKK KCVPEKGIAR LVIEKPFGVD LKSAQELQSQ LAPLFDEKEI
     YRIDHYLGKE MVQNLVHLRF CNPVISHLWD KNSISSVQIT FKEPIGTEGR GGYFDSSTIV
     RDIVQNHLVQ ILTLLTMETP TTFSADDLRD EKVKVLRRTR LGDLKDIVLG QYVKSKDGKK
     PGYLDDETVP KGSRCPTYSA IPCFIDTERW RGVPFLLKAG KAMDIGKVEI RVQFKAAANG
     LFKDAYHNEL VIRVQPDEAI YFKMNIKQPG LSEAPLLTDL DLTYSRRFKN MKLHEAYEAL
     FLDAFAGDQS RFARIDELEC AWSLVDPLLK YMEEEKPVPE PYEYGSDGPE CLYSFLKKFG
     YIYDSPDYYD YPVMSVPSDH
//