ID   G6PD_SYNE7              Reviewed;         511 AA.
AC   P29686; Q31KQ5;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 2.
DT   25-NOV-2008, entry version 56.
DE   RecName: Full=Glucose-6-phosphate 1-dehydrogenase;
DE            Short=G6PD;
DE            EC=1.1.1.49;
GN   Name=zwf; OrderedLocusNames=Synpcc7942_2334;
OS   Synechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2).
OC   Bacteria; Cyanobacteria; Chroococcales; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=92353398; PubMed=1643289; DOI=10.1007/BF00027085;
RA   Scanlan D.J., Newman J., Sebaihia M., Mann N.H., Carr N.G.;
RT   "Cloning and sequence analysis of the glucose-6-phosphate
RT   dehydrogenase gene from the cyanobacterium Synechococcus PCC 7942.";
RL   Plant Mol. Biol. 19:877-880(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC
RT   7942.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; U33285; AAA98847.1; -; Genomic_DNA.
DR   EMBL; CP000100; ABB58364.1; -; Genomic_DNA.
DR   PIR; S23520; DEYCG6.
DR   RefSeq; YP_401351.1; -.
DR   HSSP; P11413; 1QKI.
DR   GeneID; 3774617; -.
DR   GenomeReviews; CP000100_GR; Synpcc7942_2334.
DR   KEGG; syf:Synpcc7942_2334; -.
DR   HOGENOM; P29686; -.
DR   BioCyc; SELO1140:SYNPCC7942_2334-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    511       Glucose-6-phosphate 1-dehydrogenase.
FT                                /FTId=PRO_0000068134.
FT   ACT_SITE    260    260       Proton acceptor (By similarity).
FT   BINDING      31     31       NADP (By similarity).
FT   BINDING      63     63       NADP (By similarity).
FT   BINDING     198    198       Substrate (By similarity).
FT   BINDING     202    202       Substrate (By similarity).
FT   BINDING     365    365       Substrate (By similarity).
FT   CONFLICT    506    511       RRWRRL -> AVGVVSRIPATQLNSSGDV (in Ref.
FT                                1).
SQ   SEQUENCE   511 AA;  58095 MW;  9F16062520B51B10 CRC64;
     MTPKLLENPL RIGLRQDKVP EPQILVIFGA TGDLTQRKLV PAIYEMHLER RLPPELTIVG
     VARRDWSDDY FREHLRQGVE QFGGGIQAEE VWNTFAQGLF FAPGNIDDPQ FYQTLRDRLA
     NLDELRGTRG NRTFYLSVAP RFFGEAAKQL GAAGMLADPA KTRLVVEKPF GRDLSSAQVL
     NAILQNVCRE SQIYRIDHYL GKETVQNLLV FRFANAIFEP LWNRQYIDHV QITVAETVGL
     EGRAGYYETA GALRDMVQNH LMQLFSLTAM EPPNSLGADG IRNEKVKVVQ ATRLADIDDL
     SLSAVRGQYK AGWMNGRSVP AYRDEEGADP QSFTPTYVAM KLLVDNWRWQ GVPFYLRTGK
     RMPKKVTEIA IQFKTVPHLM FQSATQKVNS PNVLVLRIQP NEGVSLRFEV KTPGSSQRTR
     SVDMDFRYDT AFGSPTQEAY SRLLVDCMLG DQTLFTRADE VEASWRVVTP LLESWDDPRQ
     AAGISFYEAG TWEPAEAEQL INRDGRRWRR L
//