G6PD_CHLPN
ID G6PD_CHLPN Reviewed; 512 AA.
AC Q9Z8U6; Q9JQ22;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 137.
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=CPn_0238, CP_0524, CPj0238, CpB0244;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) 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; AE001363; AAD18391.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF73682.1; -; Genomic_DNA.
DR EMBL; BA000008; BAA98448.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP98177.1; -; Genomic_DNA.
DR PIR; C72103; C72103.
DR PIR; F86520; F86520.
DR RefSeq; NP_224447.1; NC_000922.1.
DR RefSeq; WP_010882890.1; NZ_LN847257.1.
DR AlphaFoldDB; Q9Z8U6; -.
DR SMR; Q9Z8U6; -.
DR STRING; 115711.CP_0524; -.
DR EnsemblBacteria; AAD18391; AAD18391; CPn_0238.
DR EnsemblBacteria; AAF73682; AAF73682; CP_0524.
DR GeneID; 45050285; -.
DR KEGG; cpa:CP_0524; -.
DR KEGG; cpj:zwf; -.
DR KEGG; cpn:CPn_0238; -.
DR KEGG; cpt:CpB0244; -.
DR PATRIC; fig|115713.3.peg.268; -.
DR eggNOG; COG0364; Bacteria.
DR HOGENOM; CLU_013524_5_0_0; -.
DR OrthoDB; 1153269at2; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; 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.
FT CHAIN 1..512
FT /note="Glucose-6-phosphate 1-dehydrogenase"
FT /id="PRO_0000068116"
FT REGION 479..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 263
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 61
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 103..104
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 171
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT BINDING 258
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"
SQ SEQUENCE 512 AA; 58740 MW; EABC8DBFBC940BCE CRC64;
MTNVVQETIG GLNSPRTCPP CILVIFGATG DLTARKLLPA LYHLTKEGRL SDQFVCVGFA
RREKSNELFR QEMKQAVIQF SPSELDIKVW EDFQQRLFYH RSEFDNNMGY TSLKDSLEDL
DKTYGTRGNR LFYLSTPPQY FSRIIENLNK HKLFYKNQDQ GKPWSRVIIE KPFGRDLDSA
KQLQQCINEN LNENSVYHID HYLGKETVQN ILTTRFANTI FESCWNSQYI DHVQISLSET
IGIGSRGNFF EKSGMLRDMV QNHMMQLLCL LTMEPPTTFD ADEIRKEKIK ILQRISPFSE
GSSIVRGQYG PGTVQGVSVL GYREEENVDK DSRVETYVAL KTVINNPRWL GVPFYLRAGK
RLAKKSTDIS IIFKKSPYNL FAAEECSRCP IENDLLIIRI QPDEGVALKF NCKVPGTNNI
VRPVKMDFRY DSYFQTTTPE AYERLLCDCI IGDRTLFTGG DEVMASWKLF TPVLEEWDQD
SSPSFPNYPA GSSGPKEADA LIERDGRSWR PL
