G6PD_NOSS1
ID G6PD_NOSS1 Reviewed; 509 AA.
AC P48992;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 125.
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=all4019;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8566707; DOI=10.1111/j.1574-6968.1995.tb07882.x;
RA Newman J., Karakaya H., Scanlan D.J., Mann N.H.;
RT "A comparison of gene organization in the zwf region of the genomes of the
RT cyanobacteria Synechococcus sp. PCC 7942 and Anabaena sp. PCC 7120.";
RL FEMS Microbiol. Lett. 133:187-193(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
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; U33282; AAA98853.1; -; Genomic_DNA.
DR EMBL; BA000019; BAB75718.1; -; Genomic_DNA.
DR PIR; AD2308; AD2308.
DR RefSeq; WP_010998159.1; NZ_RSCN01000023.1.
DR AlphaFoldDB; P48992; -.
DR SMR; P48992; -.
DR STRING; 103690.17133154; -.
DR PRIDE; P48992; -.
DR EnsemblBacteria; BAB75718; BAB75718; BAB75718.
DR KEGG; ana:all4019; -.
DR eggNOG; COG0364; Bacteria.
DR OMA; VEICVYE; -.
DR OrthoDB; 1153269at2; -.
DR SABIO-RK; P48992; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000002483; 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_0000068109"
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"
FT CONFLICT 417
FT /note="T -> S (in Ref. 1; AAA98853)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 509 AA; 58304 MW; FEC3CFBF7119E977 CRC64;
MVSLLENPLR VGLQQQGMPE PQIIVIFGAS GDLTWRKLVP ALYKLRRERR IPPETTIVGV
ARREWSHEYF REQMQKGMEE AHSSVELGEL WQDFSQGLFY CPGDIDNPES YQKLKNLLSE
LDEKRGTRGN RMFYLSVAPN FFPEAIKQLG GAGMLDDPYK HRLVIEKPFG RDLASAQSLN
AVVQKYCKEH QVYRIDHYLG KETVQNLLVF RFANAIFEPL WNRQFVDHVQ ITVAETVGVE
DRAGYYEKAG ALRDMLQNHL MQLYCLTAME APNSMDADSI RTEKVKVLQA TRLADVHNLS
RSAIRGQYSA GWMKGQQVPG YRTEPGVDPN SSTPTYVGMK FLVDNWRWQG VPFYLRTGKR
MPKKVSEISI HFRDVPSRMF QSAAQQRNAN ILAMRIQPNE GISLRFDVKM PGAEFRTRSV
DMDFSYGSFG IEATSDAYDR LFLDCMMGDQ TLFTRADEVE AAWQVVTPAL SVWDSPADPA
TIPQYEAGTW EPAEAEFLIN QDGRRWRRL
