ID   Q2VF42_HUMAN            Unreviewed;       475 AA.
AC   Q2VF42;
DT   10-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   10-JAN-2006, sequence version 1.
DT   24-JAN-2024, entry version 104.
DE   RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000256|RuleBase:RU362120};
DE            EC=1.1.1.49 {ECO:0000256|RuleBase:RU362120};
DE   Flags: Fragment;
GN   Name=G6PD {ECO:0000313|EMBL:ABB90566.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:ABB90566.1};
RN   [1] {ECO:0000313|EMBL:ABB90566.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ALB_74_B {ECO:0000313|EMBL:ABC25776.1}, DKT_331_B
RC   {ECO:0000313|EMBL:ABC25747.1}, GNA_02_B {ECO:0000313|EMBL:ABC25816.1},
RC   IVC_04_B {ECO:0000313|EMBL:ABC25737.1}, IVC_18_B
RC   {ECO:0000313|EMBL:ABC25757.1}, IVC_20_B {ECO:0000313|EMBL:ABC25811.1},
RC   IVC_23_B {ECO:0000313|EMBL:ABB90566.1}, JK_1029_B
RC   {ECO:0000313|EMBL:ABC25766.1}, JK_1033_B
RC   {ECO:0000313|EMBL:ABC25771.1}, JK_736_B {ECO:0000313|EMBL:ABC25742.1},
RC   JK_741_B {ECO:0000313|EMBL:ABC25826.1}, JR_013_B
RC   {ECO:0000313|EMBL:ABC25791.1}, JR_323_B {ECO:0000313|EMBL:ABC25801.1},
RC   KOH_188_B {ECO:0000313|EMBL:ABC25732.1}, LD_156_B
RC   {ECO:0000313|EMBL:ABC25806.1}, MKA_21_B {ECO:0000313|EMBL:ABC25821.1},
RC   MKA_29_B {ECO:0000313|EMBL:ABC25761.1}, SHO_14_B
RC   {ECO:0000313|EMBL:ABC25752.1}, SHO_30_B {ECO:0000313|EMBL:ABC25796.1},
RC   and SHO_46_B {ECO:0000313|EMBL:ABC25781.1};
RX   PubMed=16020776; DOI=10.1534/genetics.105.048140;
RA   Saunders M.A., Slatkin M., Garner C., Hammer M.F., Nachman M.W.;
RT   "The extent of linkage disequilibrium caused by selection on G6PD in
RT   humans.";
RL   Genetics 171:1219-1229(2005).
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:ARBA00001220};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15842;
CC         Evidence={ECO:0000256|ARBA:ARBA00001220};
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; DQ173568; ABB90566.1; -; Genomic_DNA.
DR   EMBL; DQ173592; ABC25732.1; -; Genomic_DNA.
DR   EMBL; DQ173593; ABC25737.1; -; Genomic_DNA.
DR   EMBL; DQ173594; ABC25742.1; -; Genomic_DNA.
DR   EMBL; DQ173595; ABC25747.1; -; Genomic_DNA.
DR   EMBL; DQ173596; ABC25752.1; -; Genomic_DNA.
DR   EMBL; DQ173597; ABC25757.1; -; Genomic_DNA.
DR   EMBL; DQ173598; ABC25761.1; -; Genomic_DNA.
DR   EMBL; DQ173599; ABC25766.1; -; Genomic_DNA.
DR   EMBL; DQ173600; ABC25771.1; -; Genomic_DNA.
DR   EMBL; DQ173601; ABC25776.1; -; Genomic_DNA.
DR   EMBL; DQ173602; ABC25781.1; -; Genomic_DNA.
DR   EMBL; DQ173603; ABC25786.1; -; Genomic_DNA.
DR   EMBL; DQ173604; ABC25791.1; -; Genomic_DNA.
DR   EMBL; DQ173605; ABC25796.1; -; Genomic_DNA.
DR   EMBL; DQ173606; ABC25801.1; -; Genomic_DNA.
DR   EMBL; DQ173607; ABC25806.1; -; Genomic_DNA.
DR   EMBL; DQ173608; ABC25811.1; -; Genomic_DNA.
DR   EMBL; DQ173609; ABC25816.1; -; Genomic_DNA.
DR   EMBL; DQ173610; ABC25821.1; -; Genomic_DNA.
DR   EMBL; DQ173611; ABC25826.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2VF42; -.
DR   PeptideAtlas; Q2VF42; -.
DR   UniPathway; UPA00115; UER00408.
DR   ChiTaRS; G6PD; human.
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}.
FT   DOMAIN          1..170
FT                   /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00479"
FT   DOMAIN          172..463
FT                   /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02781"
FT   BINDING         165
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10005"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABB90566.1"
SQ   SEQUENCE   475 AA;  54824 MW;  08ADCEDEAF05B277 CRC64;
     GDLAKKKIYP TIWWLFRDGL LPENTFIVGY ARSRLTVADI RKQSEPFFKA TPEEKLKLED
     FFARNSYVAG QYDDAASYQR LNSHMNALHL GSQANRLFYL ALPPTVYEAV TKNIHESCMS
     QIGWNRIIVE KPFGRDLQSS DRLSNHISSL FREDQIYRID HYLGKEMVQN LMVLRFANRI
     FGPIWNRDNI ACVILTFKEP FGTEGRGGYF DEFGIIRDVM QNHLLQMLCL VAMEKPASTN
     SDDVRDEKVK VLKCISEVQA NNVVLGQYVG NPDGEGEATK GYLDDPTVPR GSTTATFAAV
     VLYVENERWD GVPFILRCGK ALNERKAEVR LQFHDVAGDI FHQQCKRNEL VIRVQPNEAV
     YTKMMTKKPG MFFNPEESEL DLTYGNRYKN VKLPDAYERL ILDVFCGSQM HFVRSDELRE
     AWRIFTPLLH QIELEKPKPI PYIYGSRGPT EADELMKRVG FQYEGTYKWV NPHKL
//