ID   G6PD_BORBU              Reviewed;         478 AA.
AC   O51581;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   16-JUN-2009, entry version 63.
DE   RecName: Full=Glucose-6-phosphate 1-dehydrogenase;
DE            Short=G6PD;
DE            EC=1.1.1.49;
GN   Name=zwf; OrderedLocusNames=BB_0636;
OS   Borrelia burgdorferi (Lyme disease spirochete).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia;
OC   Borrelia burgdorferi group.
OX   NCBI_TaxID=139;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / B31 / CIP 102532 / DSM 4680;
RX   MEDLINE=98065943; PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K.,
RA   Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D.,
RA   Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J.,
RA   Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D.,
RA   Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A.,
RA   Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K.,
RA   Roberts K.M., Hatch B., Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia
RT   burgdorferi.";
RL   Nature 390:580-586(1997).
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; AE000783; AAB91531.1; -; Genomic_DNA.
DR   PIR; C70179; C70179.
DR   RefSeq; NP_212770.1; -.
DR   HSSP; P11413; 1QKI.
DR   GeneID; 1195488; -.
DR   GenomeReviews; AE000783_GR; BB_0636.
DR   KEGG; bbu:BB0636; -.
DR   NMPDR; fig|224326.1.peg.1020; -.
DR   TIGR; BB_0636; -.
DR   HOGENOM; O51581; -.
DR   OMA; O51581; WADIEIC.
DR   BioCyc; BBUR224326:BB_0636-MON; -.
DR   BRENDA; 1.1.1.49; 142596.
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    478       Glucose-6-phosphate 1-dehydrogenase.
FT                                /FTId=PRO_0000068111.
FT   ACT_SITE    234    234       Proton acceptor (By similarity).
FT   BINDING      17     17       NADP (By similarity).
FT   BINDING      48     48       NADP (By similarity).
FT   BINDING     172    172       Substrate (By similarity).
FT   BINDING     176    176       Substrate (By similarity).
FT   BINDING     339    339       Substrate (By similarity).
SQ   SEQUENCE   478 AA;  56113 MW;  4DDBCE2861161C8A CRC64;
     MKERSVSNFD IVIFGVTGNL SRKKLIPSLF NLFKNKCISN FRVIGFSRKI FTDKEFRLYI
     KDSLWQEETD SLIEIFLNFF VYVFGDFNEK ESYKNLFKFL DRSRETIYYL STSPAFYGPI
     INHLKKYFLS EKLTLSKIVL EKPFGSSLET AKKLNSLLYS AFKEDQIYRI DHYLGKETVQ
     NIFTFRFGNS IFENIWNNRY VDFVQITVAE ELGLDGRVEY YDSVGALKDM VQNHILQLLS
     LVAMESPIKF DSEFIHDEKV KVLKSLRKIS KEDIKNYIVK GQYIGSQVQG VFKKGYKDET
     EFLGNSNTET YLAMKVFINN WRWSGVPFYL RTGKGLARKF SEIYIQFKKP SFTLFNNSSV
     DFSNALIFRI QPRDGIEIKF NTKKPGYNYE IQTANMEFSY HGAFKRLFDE AYERLLLDAF
     LGDGTLYATS DEIESSWEFV SDIANKWADI EICNYFYGSE GPKEIDSILE KDHFWRKI
//