G6PD2_SCHPO
ID G6PD2_SCHPO Reviewed; 475 AA.
AC O59812;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase gcd1;
DE Short=G6PD;
DE EC=1.1.1.49 {ECO:0000250|UniProtKB:P11413};
GN Name=gcd1 {ECO:0000312|PomBase:SPCC794.01c}; Synonyms=zwf2;
GN ORFNames=SPCC794.01c;
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 [LARGE SCALE ANALYSIS].
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:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; CU329672; CAA19129.1; -; Genomic_DNA.
DR PIR; T41610; T41610.
DR RefSeq; NP_587749.1; NM_001022743.2.
DR AlphaFoldDB; O59812; -.
DR SMR; O59812; -.
DR BioGRID; 276136; 27.
DR STRING; 4896.SPCC794.01c.1; -.
DR MaxQB; O59812; -.
DR PaxDb; O59812; -.
DR EnsemblFungi; SPCC794.01c.1; SPCC794.01c.1:pep; SPCC794.01c.
DR PomBase; SPCC794.01c; -.
DR VEuPathDB; FungiDB:SPCC794.01c; -.
DR eggNOG; KOG0563; Eukaryota.
DR HOGENOM; CLU_013524_2_0_1; -.
DR InParanoid; O59812; -.
DR OMA; HEEMYMK; -.
DR PhylomeDB; O59812; -.
DR UniPathway; UPA00115; UER00408.
DR PRO; PR:O59812; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0047935; F:glucose 1-dehydrogenase (NADP+) activity; IDA:PomBase.
DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IBA:GO_Central.
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 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 PANTHER; PTHR23429; PTHR23429; 1.
DR Pfam; PF02781; G6PD_C; 1.
DR Pfam; PF00479; G6PD_N; 1.
DR PIRSF; PIRSF000110; G6PD; 1.
DR PRINTS; PR00079; G6PDHDRGNASE.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00871; zwf; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cytoplasm; Glucose metabolism; NADP;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..475
FT /note="Glucose-6-phosphate 1-dehydrogenase gcd1"
FT /id="PRO_0000337687"
FT ACT_SITE 238
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P11411"
FT BINDING 8..15
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 42
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 146
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 176..180
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 233
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 332
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
SQ SEQUENCE 475 AA; 53510 MW; C2CBB43BD6E70C45 CRC64;
MLSIIVFGAS GDLATKMTFP ALFALYVRKI IPEDFQIIGY ARSKLSQEAA NKIVTAHIPI
DDTVGASQKA LNTFVEHYKY VPGTYDKPES FEMLNSIIAE KETAPASECT RIFYLVLPPH
LFAPVSELIK SKAHPNGMVT RLIVEKPIGF DYKSADAILS DLSKHWSAKD TFKVDHFLGE
DMIDGFTAIR FANSMFEPIW NREHIESVRV DFREDFGCEG RGGYFEGAGI LRDVVQNHLL
QLLTLLCIEE PKSQDAEDII KCKVDFLKSL HPVSKEDIVY GQYTKSANGK VPGYRELDGV
ADDSEVSTFC ALQLRSEAPR WKGIPIIISA GKGLDRDYFE ARITFKRREG GMFPTVDSSN
VLVLRVYPKE FIALKGHIKQ PGFSRQIVPV TLDVKYPEAF PDTWIHKAYE VVIADAINGK
HTHFISDDEV RTSWKIFDDV LDTTGDLSPL PYAFGSHHGP DATLEFFKKR NLEWD
