G6PD_ZYMMO
ID G6PD_ZYMMO Reviewed; 485 AA.
AC P21907; Q5NQL3;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 136.
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=ZMO0367;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=2254282; DOI=10.1128/jb.172.12.7227-7240.1990;
RA Barnell W.O., Yi K.C., Conway T.;
RT "Sequence and genetic organization of a Zymomonas mobilis gene cluster that
RT encodes several enzymes of glucose metabolism.";
RL J. Bacteriol. 172:7227-7240(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RA Ahn J.Y., Kang H.S.;
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
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; M60615; AAA27692.1; -; Genomic_DNA.
DR EMBL; AF313764; AAG29865.1; -; Genomic_DNA.
DR EMBL; AE008692; AAV88991.1; -; Genomic_DNA.
DR PIR; B37855; B37855.
DR RefSeq; WP_011240288.1; NZ_CP035711.1.
DR AlphaFoldDB; P21907; -.
DR SMR; P21907; -.
DR STRING; 264203.ZMO0367; -.
DR EnsemblBacteria; AAV88991; AAV88991; ZMO0367.
DR GeneID; 58026216; -.
DR KEGG; zmo:ZMO0367; -.
DR eggNOG; COG0364; Bacteria.
DR HOGENOM; CLU_013524_5_0_5; -.
DR OMA; PDEGIQM; -.
DR OrthoDB; 1153269at2; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000001173; 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..485
FT /note="Glucose-6-phosphate 1-dehydrogenase"
FT /id="PRO_0000068138"
FT ACT_SITE 236
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 89..90
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 144
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 334
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
SQ SEQUENCE 485 AA; 53859 MW; C326FC605ED92430 CRC64;
MTNTVSTMIL FGSTGDLSQR MLLPSLYGLD ADGLLADDLR IVCTSRSEYD TDGFRDFAEK
ALDRFVASDR LNDDAKAKFL NKLFYATVDI TDPTQFGKLA DLCGPVEKGI AIYLSTAPSL
FEGAIAGLKQ AGLAGPTSRL ALEKPLGQDL ASSDHINDAV LKVFSEKQVY RIDHYLGKET
VQNLLTLRFG NALFEPLWNS KGIDHVQISV AETVGLEGRI GYFDGSGSLR DMVQSHILQL
VALVAMEPPA HMEANAVRDE KVKVFRALRP INNDTVFTHT VTGQYGAGVS GGKEVAGYID
ELGQPSDTET FVAIKAHVDN WRWQGVPFYI RTGKRLPARR SEIVVQFKPV PHSIFSSSGG
ILQPNKLRIV LQPDETIQIS MMVKEPGLDR NGAHMREVWL DLSLTDVFKD RKRRIAYERL
MLDLIEGDAT LFVRRDEVEA QWVWIDGIRE GWKANSMKPK TYVSGTWGPS TAIALAERDG
VTWYD
