ID A0A0E0FS40_ORYNI Unreviewed; 591 AA.
AC A0A0E0FS40;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000256|RuleBase:RU362120};
DE EC=1.1.1.49 {ECO:0000256|RuleBase:RU362120};
OS Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4536 {ECO:0000313|EnsemblPlants:ONIVA01G32620.2};
RN [1] {ECO:0000313|EnsemblPlants:ONIVA01G32620.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA01G32620.2};
RA Wing R.A., Hsing Y.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ONIVA01G32620.2}
RP IDENTIFICATION.
RC STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA01G32620.2};
RG EnsemblPlants;
RL Submitted (APR-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; A0A0E0FS40; -.
DR STRING; 4536.A0A0E0FS40; -.
DR EnsemblPlants; ONIVA01G32620.2; ONIVA01G32620.2; ONIVA01G32620.
DR Gramene; ONIVA01G32620.2; ONIVA01G32620.2; ONIVA01G32620.
DR eggNOG; KOG0563; Eukaryota.
DR OMA; PDEGIQM; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000006591; 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:SF13; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE 1, CHLOROPLASTIC; 1.
DR PANTHER; PTHR23429; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE G6PD; 1.
DR Pfam; PF02781; G6PD_C; 1.
DR Pfam; PF00479; G6PD_N; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000006591}.
FT DOMAIN 88..280
FT /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF00479"
FT DOMAIN 283..587
FT /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02781"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10005"
SQ SEQUENCE 591 AA; 66514 MW; 2D7DA442D049D135 CRC64;
MAGTGLRFRQ GAIFFSGAHA AAHPRTRTPH HHCSPQRTHD ARGRCRLTAK SANGRPQISA
SFRDVAIDGA QSEDGAPEQG GSTVSITVVG ASGDLAKKKI FPALFALYYE DCLPEHFTVF
GYARSKMSDE ELRNMISLTL TCRIDQRENC SDKMEQFLKR CFYQSGQYNS EEGFSELDRK
LKEKENGYDC EAHANTYHQA GKVPNRLFYL SIPPNIFVDV VRSASRTASS QDGWTRFIVE
KPFGRDSESS GELTRNLKKY LAEEQIFRID HYLGKELVEN LSVLRFSNLV FEPLWSRNYI
RNVQLIFSED FGTEGRGGYF DNYGIIRDIM QNHLLQILAL FAMETPVSLD AEDIRNEKVK
VLRSMRQLRL EDVVVGQYKG HSKGGKTYPA YVDDPTVPSG SITPTFAAAA LFIDNARWDG
VPFLMKAGKA LHTRRAEIRV QFRRVPGNLY GRRRRSVGGG GTTATRELEK ATNELVLRVQ
PDEAIYLKIN SKVPGLGMRL DSSDLNLLYS ERYPAEIPDA YERLLLDAIE GERRLFIRSD
ELDAAWAIFT PVLADLEANK VAPELYPYGS RGPVGAHYLA ANHNVRWGDI S
//
