ID   G6PD6_ARATH             Reviewed;         515 AA.
AC   Q9FJI5; Q9SUJ9;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   04-NOV-2008, entry version 58.
DE   RecName: Full=Glucose-6-phosphate 1-dehydrogenase, cytoplasmic isoform 2;
DE            EC=1.1.1.49;
DE   AltName: Full=G6PDH6;
DE            Short=G6PD6;
GN   Name=ACG12; OrderedLocusNames=At5g40760; ORFNames=K1B16.1, MNF13.6;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=99364543; PubMed=10437832; DOI=10.1023/A:1006257230779;
RA   Wendt U.K., Hauschild R., Lange C., Pietersma M., Wenderoth I.,
RA   von Schaewen A.;
RT   "Evidence for functional convergence of redox regulation in G6PDH
RT   isoforms of cyanobacteria and higher plants.";
RL   Plant Mol. Biol. 40:487-494(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=99087489; PubMed=9872454; DOI=10.1093/dnares/5.5.297;
RA   Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VII.
RT   Sequence features of the regions of 1,013,767 bp covered by sixteen
RT   physically assigned P1 and TAC clones.";
RL   DNA Res. 5:297-308(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
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.
CC   -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate + NADP(+) = D-glucono-
CC       1,5-lactone 6-phosphate + NADPH.
CC   -!- ENZYME REGULATION: Regulated by metabolites.
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: Cytoplasm.
CC   -!- MISCELLANEOUS: There are 6 glucose-6-phosphate 1-dehydrogenase
CC       genes in A.thaliana.
CC   -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase
CC       family.
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DR   EMBL; AJ010971; CAB52675.1; -; mRNA.
DR   EMBL; AB015470; BAB08837.1; -; Genomic_DNA.
DR   EMBL; AB009052; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BT004633; AAO42879.1; -; mRNA.
DR   PIR; T52610; T52610.
DR   RefSeq; NP_198892.1; -.
DR   UniGene; At.23901; -.
DR   HSSP; P11413; 1QKI.
DR   GeneID; 834076; -.
DR   GenomeReviews; BA000015_GR; AT5G40760.
DR   KEGG; ath:AT5G40760; -.
DR   NMPDR; fig|3702.1.peg.25780; -.
DR   TAIR; At5g40760; -.
DR   ArrayExpress; Q9FJI5; -.
DR   GermOnline; AT5G40760; Arabidopsis thaliana.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Complete proteome; Cytoplasm;
KW   Glucose metabolism; NADP; Oxidoreductase.
FT   CHAIN         1    515       Glucose-6-phosphate 1-dehydrogenase,
FT                                cytoplasmic isoform 2.
FT                                /FTId=PRO_0000068098.
FT   BINDING      40     40       NADP (By similarity).
FT   BINDING      73     73       NADP (By similarity).
FT   BINDING     212    212       Substrate (By similarity).
FT   BINDING     216    216       Substrate (By similarity).
FT   CONFLICT    361    361       A -> S (in Ref. 1; CAB52675).
SQ   SEQUENCE   515 AA;  59116 MW;  E8F7B88A52825C14 CRC64;
     MGSGQWHVEK RSTFRNDSFV REYGIVPETG CLSIIVLGAS GDLAKKKTFP ALFNLYRQGF
     LNPDEVHIFG YARTKISDEE LRDRIRGYLV DEKNAEQAEA LSKFLQLIKY VSGPYDAEEG
     FQRLDKAISE HEISKNSTEG SSRRLFYLAL PPSVYPSVCK MIKTCCMNKS DLGGWTRIVV
     EKPFGKDLES AEQLSSQIGE LFDESQIYRI DHYLGKELVQ NMLVLRFANR FFLPLWNRDN
     IENVQIVFRE DFGTEGRGGY FDEYGIIRDI IQNHLLQVLC LVAMEKPISL KPEHIRDEKV
     KVLQSVVPIS DDEVVLGQYE GYRDDDTVPN DSNTPTFATT ILRIHNERWE GVPFILKAGK
     ALNSRKAEIR IQFKDVPGDI FRCQKQGRNE FVIRLQPSEA MYMKLTVKQP GLDMNTVQSE
     LDLSYGQRYQ GVAIPEAYER LILDTIKGDQ QHFVRRDELK VAWEIFTPLL HRIDKGEVKS
     IPYKPGSRGP KEADQLLEKA GYLQTHGYIW IPPTL
//