ID   G6PD_HAEIN              Reviewed;         494 AA.
AC   P44311;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 143.
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}; OrderedLocusNames=HI_0558;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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 + 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; 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; L42023; AAC22213.1; -; Genomic_DNA.
DR   PIR; E64077; E64077.
DR   RefSeq; NP_438715.1; NC_000907.1.
DR   AlphaFoldDB; P44311; -.
DR   SMR; P44311; -.
DR   STRING; 71421.HI_0558; -.
DR   EnsemblBacteria; AAC22213; AAC22213; HI_0558.
DR   KEGG; hin:HI_0558; -.
DR   PATRIC; fig|71421.8.peg.578; -.
DR   eggNOG; COG0364; Bacteria.
DR   HOGENOM; CLU_013524_5_0_6; -.
DR   OrthoDB; 9802739at2; -.
DR   PhylomeDB; P44311; -.
DR   BioCyc; HINF71421:G1GJ1-570-MONOMER; -.
DR   UniPathway; UPA00115; UER00408.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IBA:GO_Central.
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;
KW   Reference proteome.
FT   CHAIN           1..494
FT                   /note="Glucose-6-phosphate 1-dehydrogenase"
FT                   /id="PRO_0000068122"
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;  56189 MW;  142F81FFB87FBADF CRC64;
     MQTDNNCIVI FGASGDLTHR KLIPALYNLY KIGRLSENFS VLGVARSDLN DETFREKMRE
     ALIHNEETTP ETLDAFCSHL YYQAVNTSDA QDYGKLVPRL DDLHDKYQTC GNTFYYMSTP
     PSLYGVIPEC LAAHGLNTEE YGWKRIIVEK PFGYDEKTAQ TLDVQIHRFF EEHQIYRIDH
     YLGKETVQNL LVLRFSNGWF EPLWNRNFID YVEITGAESI GVEERGGYYD GSGAMRDMFQ
     NHLLQVLAMV AMEPPAIINA NSMRDEVAKV MHSLRPLTSE DMENNLVLGQ YTAAEINGKM
     EKGYLEEKGV PANSRTETYI ALRCEIENWR WAGVPFYVRT GKRLPARVTE IVIHFKTTPH
     PVFSQNAPEN KLIIRIQPDE AISMRFGLKK PGAGFEAKEV SMDFRYADLA GAQVLTAYER
     LLLDAMKGDA TLFARTDAVH AAWKFVQPIL DYKANGGRIH EYEAGTWGPV AADKLIAKQG
     KVWRKPSGLM KKKV
//