G6PD_DICD3
ID G6PD_DICD3 Reviewed; 491 AA.
AC P37986; E0SB89;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 119.
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};
GN OrderedLocusNames=Dda3937_03574;
OS Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Dickeya.
OX NCBI_TaxID=198628;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=3937;
RX PubMed=8145647; DOI=10.1111/j.1365-2958.1994.tb00290.x;
RA Hugouvieux-Cotte-Pattat N., Robert-Baudouy J.;
RT "Molecular analysis of the Erwinia chrysanthemi region containing the kdgA
RT and zwf genes.";
RL Mol. Microbiol. 11:67-75(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3937;
RX PubMed=21217001; DOI=10.1128/jb.01513-10;
RA Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N.,
RA Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D.,
RA Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K.,
RA Rauscher L., Rodriguez-Palenzuela P., Toussaint A., Holeva M.C., He S.Y.,
RA Douet V., Boccara M., Blanco C., Toth I., Anderson B.D., Biehl B.S.,
RA Mau B., Flynn S.M., Barras F., Lindeberg M., Birch P.R., Tsuyumu S.,
RA Shi X., Hibbing M., Yap M.N., Carpentier M., Dassa E., Umehara M.,
RA Kim J.F., Rusch M., Soni P., Mayhew G.F., Fouts D.E., Gill S.R.,
RA Blattner F.R., Keen N.T., Perna N.T.;
RT "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937.";
RL J. Bacteriol. 193:2076-2077(2011).
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; X74866; CAA52858.1; -; Genomic_DNA.
DR EMBL; CP002038; ADM98358.1; -; Genomic_DNA.
DR PIR; S37053; S37053.
DR RefSeq; WP_013317812.1; NC_014500.1.
DR AlphaFoldDB; P37986; -.
DR SMR; P37986; -.
DR STRING; 198628.Dda3937_03574; -.
DR PRIDE; P37986; -.
DR EnsemblBacteria; ADM98358; ADM98358; Dda3937_03574.
DR GeneID; 9733588; -.
DR KEGG; ddd:Dda3937_03574; -.
DR PATRIC; fig|198628.6.peg.2134; -.
DR eggNOG; COG0364; Bacteria.
DR HOGENOM; CLU_013524_5_0_6; -.
DR OMA; VEICVYE; -.
DR OrthoDB; 1153269at2; -.
DR BioCyc; DDAD198628:DDA3937_RS10135-MON; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000006859; Chromosome.
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:UniProtKB-KW.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniRule.
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..491
FT /note="Glucose-6-phosphate 1-dehydrogenase"
FT /id="PRO_0000068121"
FT ACT_SITE 239
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 50
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 92..93
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 147
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 215
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 339
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 344
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
SQ SEQUENCE 491 AA; 56034 MW; 67BE0D8DCA97D5A6 CRC64;
MAVTSTAQAC DLVIFGAKGD LARRKLLPSL YQLEKAGHIH PETRIIGVGR AEWDRDAYIK
VVREALETFL KEPLDPALWT TLSNRLDFCN LDVEDTEGFK RLGTMLDQQN RTTINYFAMP
PSTFGAICRG LGQAGLNKEP ARVVMEKPLG TNLASSRVIN NQVAEFFNEC QVYRIDHYLG
KETVLNLLAL RFANSLFANN WDNRTIDHVQ ITVAEEVGIE GRWGYFDQAG QMRDMIQNHL
LQILTMIAMS PPADLSTDRI RDEKVKVLRS LRRIDRSNVH EVTVRGQYTS GFVQGKKVPG
YLEEEGANKT SNTETFVAIR VDIDDWRWSG VPFYLRTGKR LPSKCSEVVV YFKNPALNLF
HDSYQQLPQN KLIIRLQPDE GVEIQILNKI PGLDHKHRLQ TTKLDLSFSE TFNQQHLADA
YERLLLETMR GIQALFVRRD EVEEAWKWVD SIMDAWAMDN DSPKPYQAGT WGPVASVAMI
TRDGRSWNEV E
