G6PD_HAEIN
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 03-AUG-2022, entry version 137.
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; Proteobacteria; 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 RefSeq; WP_005694154.1; 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 OMA; PDEGIQM; -.
DR PhylomeDB; P44311; -.
DR BioCyc; HINF71421:G1GJ1-570-MON; -.
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; IBA:GO_Central.
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 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 PANTHER; PTHR23429; PTHR23429; 1.
DR Pfam; PF02781; G6PD_C; 1.
DR Pfam; PF00479; G6PD_N; 1.
DR PIRSF; PIRSF000110; G6PD; 1.
DR PRINTS; PR00079; G6PDHDRGNASE.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00871; zwf; 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
