ID A0A163KNM9_ABSGL Unreviewed; 517 AA.
AC A0A163KNM9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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};
GN Name=ABSGL_15279.1 scaffold 16333 {ECO:0000313|EMBL:SAM09583.1};
OS Absidia glauca (Pin mould).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=4829 {ECO:0000313|EMBL:SAM09583.1};
RN [1] {ECO:0000313|EMBL:SAM09583.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAM09583.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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; LT555144; SAM09583.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A163KNM9; -.
DR STRING; 4829.A0A163KNM9; -.
DR InParanoid; A0A163KNM9; -.
DR OMA; ERAGYYE; -.
DR OrthoDB; 989808at2759; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000078561; 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:UP000078561}.
FT DOMAIN 24..205
FT /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF00479"
FT DOMAIN 207..494
FT /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02781"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10005"
SQ SEQUENCE 517 AA; 59010 MW; 577232784FC224DC CRC64;
MSTSAIQQIR DQVQHELHGA VTIVVLGASG DLAKKKTYPA LFGLFKNGFL PSNTHIVGYA
RTKMTHDQYL ERVTQYIKLG TEEDKAKLNA FKQVTSYQSG QYDQAESWIA LNQAIEQSEQ
DRQLQPAQRN RVYYMALPPS VFIPVAQGIK QHVYNATAIN RLVVEKPFGM DTESSNELGD
ALGALFKEEE IYRIDHYLGK EMVKNVMNLR FANIFFAHAW DRQFIDNVQI TFKEPFGTEG
RGGYFDDFGI IRDVMQNHLL QVLTLIAMER PISTDSEAIR DEKVKVLKCI RPIKLDNALL
GQYVGDLDGK KPGYLDDDSL KNKESQTPTF AALALFIENE RWEGVPFVLK AGKALNEAKV
EVRIQFKNVA GNLYDDTARN ELVIRIQPKE SVYMKFNSKQ PGLSYQTIQT DLDLSYHDRY
TDLAIPDAYE SLILDVLRND HSNFVRDDEL EASWKIFTPL LHAIDDPKQH LPLVTYPYGS
RGPQELNAFV EKFGYDRSNS DAYTWPRQSM APQQNKL
//
