ID   G6PDC_SPIOL             Reviewed;         574 AA.
AC   O24357;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 62.
DE   RecName: Full=Glucose-6-phosphate 1-dehydrogenase, chloroplastic;
DE            Short=G6PD;
DE            EC=1.1.1.49;
DE   Flags: Precursor;
GN   Name=G6PD;
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   Caryophyllales; Amaranthaceae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Matador; TISSUE=Leaf;
RA   Fink A., Diogon T., Perroud P.F., Crespi P., Greppin H.;
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the rate-limiting step of the oxidative
CC       pentose-phosphate pathway, which represents a route for the
CC       dissimilation of carbohydrates besides glycolysis. The main
CC       function of this enzyme is to provide reducing power (NADPH) and
CC       pentose phosphates for fatty acid and nucleic acid synthesis which
CC       are involved in membrane synthesis and cell division. May be
CC       involved in nitrite reduction.
CC   -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate + NADP(+) = D-glucono-
CC       1,5-lactone 6-phosphate + NADPH.
CC   -!- ENZYME REGULATION: Regulated by metabolites. Post-translationally
CC       inactivated by cysteine-mediated redox modification via the
CC       ferredoxin-thioredoxin system in the light and this avoids futile
CC       cycles with photosynthetic CO2 fixation (By similarity).
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage):
CC       step 1/3.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast (By similarity).
CC   -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase
CC       family.
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DR   EMBL; AJ000182; CAA03939.1; -; mRNA.
DR   PIR; T09088; T09088.
DR   HSSP; P11413; 1QKI.
DR   BRENDA; 1.1.1.49; 286.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Chloroplast; Disulfide bond;
KW   Glucose metabolism; NADP; Oxidoreductase; Plastid; Transit peptide.
FT   TRANSIT       1      ?       Chloroplast (Potential).
FT   CHAIN         ?    574       Glucose-6-phosphate 1-dehydrogenase,
FT                                chloroplastic.
FT                                /FTId=PRO_0000010439.
FT   ACT_SITE    322    322       Proton acceptor (By similarity).
FT   BINDING      95     95       NADP (By similarity).
FT   BINDING     127    127       NADP (By similarity).
FT   BINDING     260    260       Substrate (By similarity).
FT   BINDING     264    264       Substrate (By similarity).
FT   BINDING     423    423       Substrate (By similarity).
FT   DISULFID    145    153       Redox modulation (By similarity).
SQ   SEQUENCE   574 AA;  65180 MW;  D498DB32D25849AA CRC64;
     MEELVSCHHL PLLCLQSSVP PNGCLTFFQD SACQRCSHSE FSNGHPLNDV SLQNDVAVNP
     IVAKSIDPSA DLQLLPLLES VKEEPTLSII VVGASGDLAK KKIFPALFAL FYENCLPENF
     TVFGFSRTEM NDEELRTMIS KTLTCRIDQR ENCGEKMDHF LQRCFYHSGQ YNSEDDFSGL
     DCKLKEKEAG RLQNRLFYLS IPPNIFVDVV RCVSHRASSA SGWTRVIVEK PFGRDSDSSR
     ELTRSFKQYL SEDQIFRIDH YLGKELVENL SVLRFSNLVF EPLWSRNYIR NVQLIFSEDF
     GTEGRGGYFD NYGIIRDIMQ NHLLQILALF AMETPVSLDA EDIRNEKVKV LRSMKPLKLQ
     DVVVGQYKGH SKGNKSYSGY TDDPTVPNNS VTPTFAAAAL FIDNARWDGV PFLMKAGKAL
     HTKRAEIRVQ FRHVPGNLYK KTFGTDLDKA TNELVLRVQP DEAIYLKINN KVPGLGMRLD
     RTDLNLCYST RYRGEIPDAY ERLLLDAIEG ERRLFIRSDK LDAAWSLFTP LLKELEEKKV
     APELYPYGSR GPVGAHYLAA KHNVRWGDLS GEDS
//