ID   G6PD_TREPA              Reviewed;         515 AA.
AC   O83491;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   16-JUN-2009, entry version 59.
DE   RecName: Full=Glucose-6-phosphate 1-dehydrogenase;
DE            Short=G6PD;
DE            EC=1.1.1.49;
GN   Name=zwf; OrderedLocusNames=TP_0478;
OS   Treponema pallidum.
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema.
OX   NCBI_TaxID=160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nichols;
RX   MEDLINE=98332770; PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA   Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA   Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M.,
RA   Utterback T.R., McDonald L.A., Artiach P., Bowman C., Cotton M.D.,
RA   Fujii C., Garland S.A., Hatch B., Horst K., Roberts K.M., Sandusky M.,
RA   Weidman J.F., Smith H.O., Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis
RT   spirochete.";
RL   Science 281:375-388(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; AE000520; AAC65465.1; -; Genomic_DNA.
DR   PIR; D71319; D71319.
DR   RefSeq; NP_218919.1; -.
DR   HSSP; P11413; 1QKI.
DR   IntAct; O83491; 1.
DR   GeneID; 2611128; -.
DR   GenomeReviews; AE000520_GR; TP_0478.
DR   KEGG; tpa:TP0478; -.
DR   NMPDR; fig|243276.1.peg.478; -.
DR   TIGR; TP_0478; -.
DR   HOGENOM; O83491; -.
DR   OMA; O83491; TAMEAPA.
DR   BioCyc; TPAL243276:TP_0478-MON; -.
DR   BRENDA; 1.1.1.49; 142600.
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    515       Glucose-6-phosphate 1-dehydrogenase.
FT                                /FTId=PRO_0000068137.
FT   ACT_SITE    252    252       Proton acceptor (By similarity).
FT   BINDING      21     21       NADP (By similarity).
FT   BINDING      53     53       NADP (By similarity).
FT   BINDING     190    190       Substrate (By similarity).
FT   BINDING     194    194       Substrate (By similarity).
SQ   SEQUENCE   515 AA;  58032 MW;  22936A1609EBD798 CRC64;
     MGKISGSGTV APHILVIFGA SGDLAARKLI PSLWDLFEQE LLPRTFGILG AGRTALSTES
     FRARLAEAVT KHAVRTPHDP ARLTEFLQKI HYFSFDPTDS VAFADFATYV RTLDQSLHTE
     GNFIFYLATP PSLYETIPTQ LAMHHLNREQ GNFRRVVIEK PFGYNLETAQ HLNASLRAHF
     QENQTYRIDH YLGKETVQNI LVTRFANPLF EPTWNRTHID YVEITASESL GVENRGGYYD
     QSGALRDMIQ NHLLLLLGII AMEAPAVVSS SRLRDEIVKV FDCLRPMGER DVMQHTVRAQ
     YVAGKIRGVA VPGYLEESGV DPRSCTETFA ALKCYIDNWR WMDVPFYLRT GKRLPTGVTE
     VIVHYRTLPI ALFEHIERPC AREGNALVIR IQPDEGIQLK IDLKEPGAGF KTIPVSVDFQ
     YSALTYSHLP SAYERLLLDC MNGDNTLYHR DDAVESAWRF IDPILAAWKS NKSPLLTYPA
     GSWGPKAADD LIKGSAPRWH HPSSTLLSDD FACRL
//