ID A0A316W631_9BASI Unreviewed; 424 AA.
AC A0A316W631;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000256|ARBA:ARBA00020444, ECO:0000256|RuleBase:RU362120};
DE EC=1.1.1.49 {ECO:0000256|ARBA:ARBA00013019, ECO:0000256|RuleBase:RU362120};
DE Flags: Fragment;
GN ORFNames=IE81DRAFT_320535 {ECO:0000313|EMBL:PWN45337.1};
OS Ceraceosorus guamensis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX NCBI_TaxID=1522189 {ECO:0000313|EMBL:PWN45337.1, ECO:0000313|Proteomes:UP000245783};
RN [1] {ECO:0000313|EMBL:PWN45337.1, ECO:0000313|Proteomes:UP000245783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4658 {ECO:0000313|EMBL:PWN45337.1,
RC ECO:0000313|Proteomes:UP000245783};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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|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 EMBL; KZ819356; PWN45337.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316W631; -.
DR STRING; 1522189.A0A316W631; -.
DR InParanoid; A0A316W631; -.
DR OrthoDB; 989808at2759; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000245783; 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:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
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 {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:UP000245783}.
FT DOMAIN 3..117
FT /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF00479"
FT DOMAIN 119..404
FT /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02781"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10005"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PWN45337.1"
SQ SEQUENCE 424 AA; 47501 MW; 9617E9A017490A95 CRC64;
AKKKFLSLSS YIPGAYDDDK AFANLNSELE KIEKDNKGKS TNRLFYMALP PNVFTVVAAG
LKKNCYVEQG NNRIVIEKPF GKDLESSREM MGKLKDLWKE EETFRIDHYL GKEMVKNLLV
MRFGNPVVDV GLNNKFVDNV QITFKEPFGT EGRGGYFDEF GIIRDIQQNH LTQVLSLLAM
DAPKSLGAED IRDQKVKVLE SVPPIDAKDV LIGQYSAANG KPGYKDDDTV PKDSNCPTFA
ALVLWVNNER WKGVPFVLKA GKALDEGQVS IRVQYKDAEG PLKGAARNEL VLRVQPNEAV
YYKINAKTPG LEGSFSSSLP ADLDLTYKQR FENIRIPEAY EALILDALNG DHSNFVRDDE
LDASWKIFTP ILHAIDAGKV QVSSYPYGSR GPSELNEFLA KYGYRRSDGY EWPKTNVANV
SGKM
//
