G6PD_NOSP7
ID G6PD_NOSP7 Reviewed; 509 AA.
AC P48848; B2J6J9;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=Npun_F4025;
OS Nostoc punctiforme (strain ATCC 29133 / PCC 73102).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=63737;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7870816; DOI=10.1104/pp.107.1.267;
RA Summers M.L., Meeks J.C., Chu S., Wolf R.E. Jr.;
RT "Nucleotide sequence of an operon in Nostoc sp. strain ATCC 29133 encoding
RT four genes of the oxidative pentose phosphate cycle.";
RL Plant Physiol. 107:267-268(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29133 / PCC 73102;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Meeks J.C., Elhai J.,
RA Campbell E.L., Thiel T., Longmire J., Potts M., Atlas R.;
RT "Complete sequence of chromosome of Nostoc punctiforme ATCC 29133.";
RL Submitted (APR-2008) 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; L32796; AAA50770.1; -; Genomic_DNA.
DR EMBL; CP001037; ACC82404.1; -; Genomic_DNA.
DR RefSeq; WP_012410371.1; NC_010628.1.
DR AlphaFoldDB; P48848; -.
DR SMR; P48848; -.
DR STRING; 63737.Npun_F4025; -.
DR PRIDE; P48848; -.
DR EnsemblBacteria; ACC82404; ACC82404; Npun_F4025.
DR KEGG; npu:Npun_F4025; -.
DR eggNOG; COG0364; Bacteria.
DR HOGENOM; CLU_013524_5_0_3; -.
DR OMA; VEICVYE; -.
DR OrthoDB; 1153269at2; -.
DR PhylomeDB; P48848; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000001191; 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..509
FT /note="Glucose-6-phosphate 1-dehydrogenase"
FT /id="PRO_0000068130"
FT ACT_SITE 259
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 62
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 104..105
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 167
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 235
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 254
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 359
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 364
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
SQ SEQUENCE 509 AA; 58268 MW; 7FA3196A3199A8AA CRC64;
MVSLLENPLR VGLQQQGMPE PQIIVIFGAS GDLTWRKLVP ALYKLRRERR IPPETTIVGV
ARREWSHEYF REQMQKGMEE AHPDVDLGEL WQDFSQGLFY SPGDIDNPES YQKLKTLLSE
LDEKRGTRGN RMFYLSVAPS FFPEAIKQLG SGGMLEDPYK HRLVIEKPFG RDLASAQSLN
QVVQKYCKEH QVYRIDHYLG KETVQNLLVF RFANAIFEPL WNRQFVDHVQ ITVAETVGVE
DRAGYYESAG ALRDMLQNHL MQLYCLTAME APNAMDADSI RTEKVKVLQA TRLADVHNLS
RSAVRGQYSA GWMKGQAVPG YRTEPGVDPN STTPTYVAMK FLVDNWRWKG VPFYLRTGKR
MPKKVSEIAI HFREVPSRMF QSAAQQTNAN ILTMRIQPNE GISLRFDVKM PGAEFRTRSV
DMDFSYGSFG IQATSDAYDR LFLDCMMGDQ TLFTRADEVE AAWQVVTPAL SVWDAPADPT
TIPQYEAGTW EPEQAELLIN QDGRRWRRL
