ID A0A1X7QW62_9SACH Unreviewed; 480 AA.
AC A0A1X7QW62;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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 ORFNames=KASA_0Q00165G {ECO:0000313|EMBL:SMN17683.1};
OS Kazachstania saulgeensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1789683 {ECO:0000313|EMBL:SMN17683.1, ECO:0000313|Proteomes:UP000196158};
RN [1] {ECO:0000313|EMBL:SMN17683.1, ECO:0000313|Proteomes:UP000196158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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|RuleBase:RU362120}.
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DR EMBL; FXLY01000002; SMN17683.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7QW62; -.
DR STRING; 1789683.A0A1X7QW62; -.
DR OrthoDB; 989808at2759; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000196158; 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; 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.
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|RuleBase:RU362120};
KW Reference proteome {ECO:0000313|Proteomes:UP000196158}.
FT DOMAIN 17..193
FT /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF00479"
FT DOMAIN 199..477
FT /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02781"
SQ SEQUENCE 480 AA; 54500 MW; 9AF4998F5E935F33 CRC64;
MPVANQTIAF EKNTAFVLFG ASGDLAKKET FPALFGLYSE GALDPSTKIF CYARSKLTVD
NLRENCKQYC RPSTGGNDKF KMDQFFKMVT YISGAYDTDD GYLRLKGEIE AFEKERGVTQ
PHRIFYLAIP PTIFLTVAGQ LKKNIYATNG ITRVIVEKPF GNDLDTSREL QKGFKPLFRE
DEIFKIDHFL GKDDLKRLLA VRFANPFLNG TWNKDYIECI QVWFKEPFGA EGRGGYFDVV
GIIRDVMQNH LLQILTVALM EEPVANKAEA IRDAKVTLLK SMEKLGPKNV VSVGQYGRST
DGKLPSYLDD DTVLNKESKC LTFTEITMDV HNDRWEGVPI VMRAGKGLDE DRVEIRMKYK
KNVSGMFAGC TPNEFVIQFH PERKIYMTFN TTAPGFVDNV HQVSLDMTYS DKYAKDWVPE
AYERLIRDAF LGNPANYVRD DELDVSWDIF TPLLNYVEGP DAPEPEIYPY GSTGPKGILE
//
