G6PD_SYNE7
ID G6PD_SYNE7 Reviewed; 511 AA.
AC P29686; Q31KQ5;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 126.
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=Synpcc7942_2334;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1643289; DOI=10.1007/bf00027085;
RA Scanlan D.J., Newman J., Sebaihia M., Mann N.H., Carr N.G.;
RT "Cloning and sequence analysis of the glucose-6-phosphate dehydrogenase
RT gene from the cyanobacterium Synechococcus PCC 7942.";
RL Plant Mol. Biol. 19:877-880(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; U33285; AAA98847.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB58364.1; -; Genomic_DNA.
DR PIR; S23520; DEYCG6.
DR RefSeq; WP_011244078.1; NC_007604.1.
DR AlphaFoldDB; P29686; -.
DR SMR; P29686; -.
DR STRING; 1140.Synpcc7942_2334; -.
DR PRIDE; P29686; -.
DR EnsemblBacteria; ABB58364; ABB58364; Synpcc7942_2334.
DR KEGG; syf:Synpcc7942_2334; -.
DR eggNOG; COG0364; Bacteria.
DR HOGENOM; CLU_013524_5_0_3; -.
DR OMA; VEICVYE; -.
DR OrthoDB; 1153269at2; -.
DR BioCyc; SYNEL:SYNPCC7942_2334-MON; -.
DR UniPathway; UPA00115; UER00408.
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.
FT CHAIN 1..511
FT /note="Glucose-6-phosphate 1-dehydrogenase"
FT /id="PRO_0000068134"
FT ACT_SITE 260
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 63
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 168
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 198
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 255
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 360
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 365
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT CONFLICT 506..511
FT /note="RRWRRL -> AVGVVSRIPATQLNSSGDV (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 511 AA; 58095 MW; 9F16062520B51B10 CRC64;
MTPKLLENPL RIGLRQDKVP EPQILVIFGA TGDLTQRKLV PAIYEMHLER RLPPELTIVG
VARRDWSDDY FREHLRQGVE QFGGGIQAEE VWNTFAQGLF FAPGNIDDPQ FYQTLRDRLA
NLDELRGTRG NRTFYLSVAP RFFGEAAKQL GAAGMLADPA KTRLVVEKPF GRDLSSAQVL
NAILQNVCRE SQIYRIDHYL GKETVQNLLV FRFANAIFEP LWNRQYIDHV QITVAETVGL
EGRAGYYETA GALRDMVQNH LMQLFSLTAM EPPNSLGADG IRNEKVKVVQ ATRLADIDDL
SLSAVRGQYK AGWMNGRSVP AYRDEEGADP QSFTPTYVAM KLLVDNWRWQ GVPFYLRTGK
RMPKKVTEIA IQFKTVPHLM FQSATQKVNS PNVLVLRIQP NEGVSLRFEV KTPGSSQRTR
SVDMDFRYDT AFGSPTQEAY SRLLVDCMLG DQTLFTRADE VEASWRVVTP LLESWDDPRQ
AAGISFYEAG TWEPAEAEQL INRDGRRWRR L
