ID   G6PD_BUCBP              Reviewed;         490 AA.
AC   Q89AI7;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-NOV-2008, entry version 44.
DE   RecName: Full=Glucose-6-phosphate 1-dehydrogenase;
DE            Short=G6PD;
DE            EC=1.1.1.49;
GN   Name=zwf; OrderedLocusNames=bbp_298;
OS   Buchnera aphidicola subsp. Baizongia pistaciae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=135842;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22426901; PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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; AE016826; AAO27023.1; -; Genomic_DNA.
DR   RefSeq; NP_777918.1; -.
DR   HSSP; P11413; 1QKI.
DR   GeneID; 1058476; -.
DR   GenomeReviews; AE016826_GR; bbp_298.
DR   KEGG; bab:bbp298; -.
DR   HOGENOM; Q89AI7; -.
DR   BioCyc; BAPH224915:BBP_298-MON; -.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001282; Glc-6-P_DHase.
DR   InterPro; IPR016040; NAD(P)-bd.
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    490       Glucose-6-phosphate 1-dehydrogenase.
FT                                /FTId=PRO_0000068114.
FT   ACT_SITE    237    237       Proton acceptor (By similarity).
FT   BINDING      16     16       NADP (By similarity).
FT   BINDING      48     48       NADP (By similarity).
FT   BINDING     175    175       Substrate (By similarity).
FT   BINDING     179    179       Substrate (By similarity).
FT   BINDING     345    345       Substrate (By similarity).
SQ   SEQUENCE   490 AA;  57318 MW;  F5EE7D9055965AD9 CRC64;
     MKNKNSGYDL VIFGAKGDLS CRKLLPSLYQ LEKKNKLCTH TRIIGVGRAN WDKIIYTNVV
     YKSLIKFLNE TIIESIWKKF SSRLEFCNLD INCLHNFKKL KQIIQQNNNI IINYLAMPPH
     TFGNICLGLE SINLNLEPTR IIIEKPLGSS LKTSININNK IGKFFKEKQI FRIDHYLGKE
     TIQNLLAFRF SNSLFYYNWN NKFIDHVQIT VSETIGVEGR FNYFDTVGQI KDMVQNHLLQ
     ILTITTMSTP IDCHENSIRD EKVKILKSLR PFNINNIHKN VILGQYTSGI INQKKVKSYL
     DETNNQEYQM NKYTETFVSM KIYIDNDQWS GVPFYLRTGK RLPKKCSEIV IFFKTPPLNI
     FSKNYNTLSK NKLILSLQPN EAIKIYILNK KPKLTSQYKL DLITLDFNYS KFYKKIQLSD
     AYEKLLLESM KGIQSLFVRR DEVELAWKWI DSTLQCLHLK PRLPDLYPAG TWGPARSKTM
     INNDGYEWNE
//