ID   G6PD_AGGAC              Reviewed;         494 AA.
AC   P77809;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   02-SEP-2026, entry version 107.
DE   RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00966};
DE            Short=G6PD {ECO:0000255|HAMAP-Rule:MF_00966};
DE            EC=1.1.1.49 {ECO:0000255|HAMAP-Rule:MF_00966};
GN   Name=zwf {ECO:0000255|HAMAP-Rule:MF_00966};
OS   Aggregatibacter actinomycetemcomitans (Actinobacillus
OS   actinomycetemcomitans) (Haemophilus actinomycetemcomitans).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pasteurellales; Pasteurellaceae; Aggregatibacter.
OX   NCBI_TaxID=714;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43718 / FDC Y4 / Serotype b;
RX   PubMed=9020051; DOI=10.1006/bbrc.1996.5917;
RA   Yoshida Y., Nakano Y., Yamashita Y., Koga T.;
RT   "The gnd gene encoding a novel 6-phosphogluconate dehydrogenase and its
RT   adjacent region of Actinobacillus actinomycetemcomitans chromosomal DNA.";
RL   Biochem. Biophys. Res. Commun. 230:220-225(1997).
CC   -!- FUNCTION: Catalyzes the oxidation of glucose 6-phosphate to 6-
CC       phosphogluconolactone. {ECO:0000255|HAMAP-Rule:MF_00966}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-
CC         lactone + NADPH + H(+); 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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00966};
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC       1/3. {ECO:0000255|HAMAP-Rule:MF_00966}.
CC   -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00966}.
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DR   EMBL; D88189; BAA13554.1; -; Genomic_DNA.
DR   RefSeq; WP_250128558.1; NZ_JAJHPH010000017.1.
DR   AlphaFoldDB; P77809; -.
DR   SMR; P77809; -.
DR   STRING; 714.ACT75_04150; -.
DR   PaxDb; 714-ACT75_04150; -.
DR   eggNOG; COG0364; Bacteria.
DR   UniPathway; UPA00115; UER00408.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR   GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IEA:TreeGrafter.
DR   Gene3D; 3.30.360.10; Dihydrodipicolinate Reductase, domain 2; 1.
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; Glucose metabolism; NADP; Oxidoreductase.
FT   CHAIN           1..494
FT                   /note="Glucose-6-phosphate 1-dehydrogenase"
FT                   /id="PRO_0000068108"
FT   ACT_SITE        242
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         46
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         150
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         180
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         184
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         218
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         237
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         342
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
SQ   SEQUENCE   494 AA;  56385 MW;  B0B2A32F349936A2 CRC64;
     MKAENCCIVI FGASGDLTYR KLIPALYNLY KIDRLGEDFS VLGVARTELN DKSFREKMRQ
     TLIKNEGAKG ECLEQFCSHL YYQAVNTADK ADYAKLVPRL DELHDTYRTE GNTLYYLSTP
     PSLYGVIPEC LGEHGLNKED RGWKRLIVEK PFGYDRETAE ALDIQIHRFF EEHQIYRIDH
     YLGKETVQNL LVLRFSNGWF EPLWNRNFID YIEITGAESI GVEERGGYYD GSGAMRDMFQ
     NHLLQVLAMV AMEPPVIINA NSMRDEVAKV LHCLRPLTQE DVEHNLVLGQ YVAGEVDGEW
     VKGYLEEKGV PPYSTTETYM ALRCEIENWR WAGVPFYVRT GKRLPARVTE IVIHFKTTPH
     PVFSQNAPEN KLIIRIQPDE GISMRFGLKK PGAGFEAKEV SMDFRYADLA GATVMTAYER
     LLLDAMKGDA TLFARTDAVH AAWKFVQPIL NYKAQGGRLY DYEAGTWGPT AADKLIAKSG
     RVWRRPSGLM KKKV
//