ID   G6PD_CHLTR              Reviewed;         439 AA.
AC   O84188;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   27-MAR-2024, entry version 132.
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=CT_185;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
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; AE001273; AAC67777.1; -; Genomic_DNA.
DR   PIR; B71546; B71546.
DR   RefSeq; NP_219689.3; NC_000117.1.
DR   RefSeq; WP_024125993.1; NC_000117.1.
DR   AlphaFoldDB; O84188; -.
DR   SMR; O84188; -.
DR   STRING; 272561.CT_185; -.
DR   EnsemblBacteria; AAC67777; AAC67777; CT_185.
DR   GeneID; 884944; -.
DR   KEGG; ctr:CT_185; -.
DR   PATRIC; fig|272561.5.peg.199; -.
DR   HOGENOM; CLU_013524_5_1_0; -.
DR   InParanoid; O84188; -.
DR   OrthoDB; 9802739at2; -.
DR   UniPathway; UPA00115; UER00408.
DR   Proteomes; UP000000431; 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..439
FT                   /note="Glucose-6-phosphate 1-dehydrogenase"
FT                   /id="PRO_0000068117"
FT   ACT_SITE        192
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         100
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         130
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         134
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         288
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
SQ   SEQUENCE   439 AA;  51063 MW;  E091DE335A4D1189 CRC64;
     MKLAVQHFSH SSEIDIRVWE SLENRIFYHQ ANFSDAEGYS VLKAYLEQLD QQYGTQGNRL
     FYLSTPPDYF QEIIRNLNRH QLFYHEQGAQ QPWSRLIIEK PFGVNLETAR ELQQCIDANI
     DEESVYRIDH YLGKETVQNI LTIRFANTLF ESCWNSQYID HVQISVSESI GIGSRGNFFE
     KSGMLRDMVQ NHLTQLLCLL TMEPPSEFFS EEIKKEKIKI LKKILPIREE DAVRGQYGEG
     IVQDVSVLGY REEENVDPNS SVETYVALKL FIDNPRWKGV PFYLQAGKRL PKRTTDIAVI
     FKKSSYNLFN AENCPLCPLE NDLLIIRIQP DEGVALQFNC KVPGTNKLVR PVKMDFRYDS
     YFNTVTPEAY ERLLCDCILG DRTLFTSNEE VLASWELFSP LLEKWSQVRP IFPNYMAGSL
     RPQEADELLS RDGKAWRPY
//