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   16-JUN-2009, entry version 58.
DE   RecName: Full=Glucose-6-phosphate 1-dehydrogenase;
DE            Short=G6PD;
DE            EC=1.1.1.49;
GN   Name=zwf; OrderedLocusNames=CT_185;
OS   Chlamydia trachomatis.
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia.
OX   NCBI_TaxID=813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   MEDLINE=99000809; 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.,
RA   Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans:
RT   Chlamydia trachomatis.";
RL   Science 282:754-759(1998).
CC   -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate + NADP(+) = D-glucono-
CC       1,5-lactone 6-phosphate + NADPH.
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage):
CC       step 1/3.
CC   -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase
CC       family.
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DR   EMBL; AE001273; AAC67777.1; -; Genomic_DNA.
DR   PIR; B71546; B71546.
DR   RefSeq; NP_219689.2; -.
DR   HSSP; P11413; 1QKI.
DR   PHCI-2DPAGE; O84188; -.
DR   GeneID; 884944; -.
DR   GenomeReviews; AE001273_GR; CT_185.
DR   KEGG; ctr:CT185; -.
DR   HOGENOM; O84188; -.
DR   OMA; O84188; QRADNIE.
DR   BioCyc; CTRA315277:CT185-MON; -.
DR   BRENDA; 1.1.1.49; 108.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:EC.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001282; Glc-6-P_DH.
DR   InterPro; IPR019796; Glc-6-P_DH_AS.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR23429; G6PDH; 1.
DR   Pfam; PF02781; G6PD_C; 1.
DR   Pfam; PF00479; G6PD_N; 1.
DR   PIRSF; PIRSF000110; G6PD; 1.
DR   PRINTS; PR00079; G6PDHDRGNASE.
DR   ProDom; PD001129; G6PD; 1.
DR   TIGRFAMs; TIGR00871; zwf; 1.
DR   PROSITE; PS00069; G6P_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Complete proteome; Glucose metabolism; NADP;
KW   Oxidoreductase.
FT   CHAIN         1    439       Glucose-6-phosphate 1-dehydrogenase.
FT                                /FTId=PRO_0000068117.
FT   ACT_SITE    192    192       Proton acceptor (By similarity).
FT   BINDING      17     17       NADP (By similarity).
FT   BINDING     130    130       Substrate (By similarity).
FT   BINDING     134    134       Substrate (By similarity).
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
//