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Database: UniProt
Entry: I1PME7_ORYGL
LinkDB: I1PME7_ORYGL
Original site: I1PME7_ORYGL 
ID   I1PME7_ORYGL            Unreviewed;       505 AA.
AC   I1PME7;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000256|RuleBase:RU362120};
DE            EC=1.1.1.49 {ECO:0000256|RuleBase:RU362120};
OS   Oryza glaberrima (African rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4538 {ECO:0000313|EnsemblPlants:ORGLA04G0136600.1, ECO:0000313|Proteomes:UP000007306};
RN   [1] {ECO:0000313|Proteomes:UP000007306}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IRGC 96717 {ECO:0000313|Proteomes:UP000007306};
RA   Wing R.A., Yu Y., Rounsley S., Reddy-Marri P., Goicoechea J.L.,
RA   Sisneros N., Lee S., Song X., Angelova A., Kudrna D.P., de Baynast K.,
RA   Zuccolo A.;
RT   "The complete genome of Oryza glaberrima.";
RL   Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:ORGLA04G0136600.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (JUN-2015) to UniProtKB.
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. {ECO:0000256|RuleBase:RU362120}.
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|ARBA:ARBA00004937, ECO:0000256|RuleBase:RU362120}.
CC   -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009975, ECO:0000256|RuleBase:RU362120}.
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DR   AlphaFoldDB; I1PME7; -.
DR   SMR; I1PME7; -.
DR   STRING; 4538.I1PME7; -.
DR   EnsemblPlants; ORGLA04G0136600.1; ORGLA04G0136600.1; ORGLA04G0136600.
DR   Gramene; ORGLA04G0136600.1; ORGLA04G0136600.1; ORGLA04G0136600.
DR   eggNOG; KOG0563; Eukaryota.
DR   HOGENOM; CLU_013524_2_3_1; -.
DR   OMA; TLIYDCL; -.
DR   UniPathway; UPA00115; UER00408.
DR   Proteomes; UP000007306; Unassembled WGS sequence.
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; IEA:UniProtKB-KW.
DR   GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IEA:UniProt.
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:SF8; 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 {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|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362120}.
FT   DOMAIN          33..210
FT                   /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00479"
FT   DOMAIN          212..490
FT                   /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02781"
FT   BINDING         205
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10005"
SQ   SEQUENCE   505 AA;  57699 MW;  14238D7D6F712815 CRC64;
     MSGGSSPRSR RSSFNSLSRD LELPSEQGCL SVIVLGASGD LAKKKTFPAL FHLFAQGFIQ
     SGEVHIFGYA RSNLSDDGLR ERIRGYLKGA SEEHLSDFLQ HIKYVSGSYD SGEGFEKLNK
     EISEYEKSNK SESPRRLFYL ALPPSVYPSV CKMIRTYCMN PSGWTRVIVE KPFGKDLDSA
     EELSAQLGEL FDENQLYRID HYLGKELVQN LLVLRFANRL FLPLWNRDNI DNIQIVFRED
     FGTDGRGGYF DQYGIIRDII QNHLLQVFCL VAMEKPVSLK PEHIRDEKVK VLQSVNPIKH
     DEVVLGQYEG YKDDPTVPDD SNTPTFASVV LRVHNERWEG VPFILKAGKA LSSRKAEVRV
     QFKDVPGDIF KCKRQGRNEF VIRLQPSEAM YMKLTVKKPG LEMATEQSEL DLSYGMRYQN
     VKIPEAYERL ILDTIRGDQQ HFVRRDELKA AWQIFTPLLH DIDEGKVKSI PYQPGSRGPK
     EADELSERVG YMQTHGYIWI PPTLA
//
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