ID   G6PD_SYNY3              Reviewed;         509 AA.
AC   P73411;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, 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=slr1843;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC   Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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; BA000022; BAA17451.1; -; Genomic_DNA.
DR   PIR; S77348; S77348.
DR   AlphaFoldDB; P73411; -.
DR   SMR; P73411; -.
DR   IntAct; P73411; 1.
DR   STRING; 1148.gene:10498315; -.
DR   PaxDb; 1148-1652530; -.
DR   EnsemblBacteria; BAA17451; BAA17451; BAA17451.
DR   KEGG; syn:slr1843; -.
DR   eggNOG; COG0364; Bacteria.
DR   InParanoid; P73411; -.
DR   PhylomeDB; P73411; -.
DR   UniPathway; UPA00115; UER00408.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IBA:GO_Central.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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   NCBIfam; TIGR00871; zwf; 1.
DR   PANTHER; PTHR23429:SF0; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE; 1.
DR   PANTHER; PTHR23429; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE G6PD; 1.
DR   Pfam; PF02781; G6PD_C; 1.
DR   Pfam; PF00479; G6PD_N; 1.
DR   PIRSF; PIRSF000110; G6PD; 1.
DR   PRINTS; PR00079; G6PDHDRGNASE.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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_0000068135"
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         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;  57886 MW;  EC24FE8D1AFFC238 CRC64;
     MVTLLENPFR TGLRQERTPE PLILTIFGAS GDLTQRKLVP AIYQMKRERR LPPELTVVGF
     ARRDWSHDHF REQMRKGIEE FSTGIGSEDL WNEFAQGLFY CSGNMDDPES YLKLKNFLGE
     LDEKRNTRGN RVFYLAVSPN FFPPGIKQLG AAGMLSDPVK SRIVIEKPFG RDLSSAQSLN
     RVVQSVCKEN QVYRIDHYLG KETVQNLMVF RFANAIFEPL WNRQFVDHVQ ITVAETVGVE
     ERAGYYESAG ALRDMVQNHL MQLFCLTAMD PPNAIDADSI RNEKVKVLQA TRLADINNLE
     NAGIRGQYKA GWMGGKPVPG YREEPGVDPS STTPTFAALK LMVDNWRWQG VPFYLRTGKR
     MPKKVSEIAI QFRQVPLLIF QSVAHQANPN VLSLRIQPNE GISLRFEAKM PGSELRTRTV
     DMDFSYGSSF GVAAADAYHR LLLDCMLGDQ TLFTRADEVE EAWRVVTPVL SAWDAPSDPL
     SMPLYEAGTW EPAEAEWLIN KDGRRWRRL
//