G6PD_PSEAE
ID G6PD_PSEAE Reviewed; 489 AA.
AC O68282;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
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=1.1.1.363 {ECO:0000269|PubMed:9537370};
DE AltName: Full=Glucose-6-phosphate dehydrogenase (NAD(P)(+)) {ECO:0000305};
GN Name=zwf {ECO:0000255|HAMAP-Rule:MF_00966}; OrderedLocusNames=PA3183;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=9537370; DOI=10.1128/jb.180.7.1741-1749.1998;
RA Ma J.-F., Hager P.W., Howell M.L., Phibbs P.V. Jr., Hassett D.J.;
RT "Cloning and characterization of the Pseudomonas aeruginosa zwf gene
RT encoding glucose-6-phosphate dehydrogenase, an enzyme important in
RT resistance to methyl viologen (paraquat).";
RL J. Bacteriol. 180:1741-1749(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Catalyzes the oxidation of glucose 6-phosphate to 6-
CC phosphogluconolactone. Can utilize either NADP(+) or NAD(+).
CC {ECO:0000255|HAMAP-Rule:MF_00966, ECO:0000269|PubMed:9537370}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose 6-phosphate + NAD(+) = 6-phospho-D-glucono-1,5-
CC lactone + H(+) + NADH; Xref=Rhea:RHEA:38215, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:57955,
CC ChEBI:CHEBI:61548; EC=1.1.1.363;
CC Evidence={ECO:0000269|PubMed:9537370};
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=1.1.1.363;
CC Evidence={ECO:0000269|PubMed:9537370};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=530 uM for glucose 6-phosphate (with NADP)
CC {ECO:0000269|PubMed:9537370};
CC KM=57 uM for NADP {ECO:0000269|PubMed:9537370};
CC KM=333 uM for NAD {ECO:0000269|PubMed:9537370};
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 -!- SUBUNIT: Homotetramer. {ECO:0000305|PubMed:9537370}.
CC -!- INDUCTION: Transcription is maximal during early logarithmic phase when
CC inducing substrates such as glycerol, glucose or gluconate are
CC abundant. Transcription decreases during stationary phase.
CC {ECO:0000269|PubMed:9537370}.
CC -!- DISRUPTION PHENOTYPE: Mutant is unable to grow on minimal medium
CC supplemented with mannitol and shows increased sensitivity to the
CC redox-active superoxide-generating agent methyl viologen (paraquat).
CC {ECO:0000269|PubMed:9537370}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_00966}.
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DR EMBL; AF029673; AAC38311.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06571.1; -; Genomic_DNA.
DR PIR; A83248; A83248.
DR RefSeq; NP_251873.1; NC_002516.2.
DR RefSeq; WP_003113442.1; NZ_QZGE01000023.1.
DR AlphaFoldDB; O68282; -.
DR SMR; O68282; -.
DR STRING; 287.DR97_4753; -.
DR PaxDb; O68282; -.
DR PRIDE; O68282; -.
DR EnsemblBacteria; AAG06571; AAG06571; PA3183.
DR GeneID; 882681; -.
DR KEGG; pae:PA3183; -.
DR PATRIC; fig|208964.12.peg.3327; -.
DR PseudoCAP; PA3183; -.
DR HOGENOM; CLU_013524_5_0_6; -.
DR InParanoid; O68282; -.
DR OMA; EGMRFIP; -.
DR PhylomeDB; O68282; -.
DR BioCyc; PAER208964:G1FZ6-3243-MON; -.
DR BRENDA; 1.1.1.363; 5087.
DR SABIO-RK; O68282; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000002438; 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 1: Evidence at protein level;
KW Carbohydrate metabolism; Glucose metabolism; NAD; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..489
FT /note="Glucose-6-phosphate 1-dehydrogenase"
FT /id="PRO_0000068131"
FT ACT_SITE 237
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 49
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 145
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 337
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 489 AA; 55620 MW; 755849EB33BF9486 CRC64;
MPDVRVLPCT LALFGALGDL ALRKLFPALY QLDRENLLHR DTRVLALARD EGAPAEHLAT
LEQRLRLAVP AKEWDDVVWQ RFRERLDYLS MDFLDPQAYV GLREAVDDEL PLVAYFATPA
SVFGGICENL AAAGLAERTR VVLEKPIGHD LESSREVNEA VARFFPESRI YRIDHYLGKE
TVQNLIALRF ANSLFETQWN QNHISHVEIT VAEKVGIEGR WGYFDQAGQL RDMVQNHLLQ
LLCLIAMDPP SDLSADSIRD EKVKVLRALE PIPAEQLASR VVRGQYTAGF SDGKAVPGYL
EEEHANRDSD AETFVALRVD IRNWRWSGVP FYLRTGKRMP QKLSQIVIHF KEPPHYIFAP
EQRSLISNRL IIRLQPDEGI SLQVMTKDQG LGKGMQLRTG PLQLSFSETY HAARIPDAYE
RLLLEVTQGN QYLFVRKDEV EFAWKWCDQL IAGWERLSEA PKPYPAGSWG PVASVALVAR
DGRSWYGDF
