ID   G6PD3_ARATH             Reviewed;         599 AA.
AC   Q8L743; O48695; Q53YG8;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2002, sequence version 2.
DT   25-NOV-2008, entry version 60.
DE   RecName: Full=Glucose-6-phosphate 1-dehydrogenase 3, chloroplastic;
DE            Short=G6PDH3;
DE            Short=G6PD3;
DE            EC=1.1.1.49;
DE   Flags: Precursor;
GN   OrderedLocusNames=At1g24280; ORFNames=F3I6.22;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=21016719; PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
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. 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   -!- 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; AC002396; AAC00588.1; -; Genomic_DNA.
DR   EMBL; AY139768; AAM98087.1; -; mRNA.
DR   EMBL; BT003032; AAO23597.1; -; mRNA.
DR   PIR; T00659; T00659.
DR   RefSeq; NP_173838.1; -.
DR   UniGene; At.41453; -.
DR   HSSP; P11413; 1QKI.
DR   GeneID; 839044; -.
DR   GenomeReviews; CT485782_GR; AT1G24280.
DR   KEGG; ath:AT1G24280; -.
DR   NMPDR; fig|3702.1.peg.2822; -.
DR   TAIR; At1g24280; -.
DR   ArrayExpress; Q8L743; -.
DR   GermOnline; AT1G24280; Arabidopsis thaliana.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
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   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; Complete proteome;
KW   Glucose metabolism; NADP; Oxidoreductase; Plastid; Transit peptide.
FT   TRANSIT       1     57       Chloroplast (Potential).
FT   CHAIN        58    599       Glucose-6-phosphate 1-dehydrogenase 3,
FT                                chloroplastic.
FT                                /FTId=PRO_0000010437.
FT   COMPBIAS     78     81       Poly-Ser.
FT   COMPBIAS    422    425       Poly-Ala.
FT   ACT_SITE    348    348       Proton acceptor (By similarity).
FT   BINDING     121    121       NADP (By similarity).
FT   BINDING     153    153       NADP (By similarity).
FT   BINDING     286    286       Substrate (By similarity).
FT   BINDING     290    290       Substrate (By similarity).
FT   DISULFID    171    179       Redox modulation (By similarity).
FT   CONFLICT     79     79       S -> N (in Ref. 2; AAM98087/AAO23597).
SQ   SEQUENCE   599 AA;  67358 MW;  AC0964649C5DB49F CRC64;
     MSSLSCPTYR SRTSSSSPFL SNHHHSSLIN VVDPRRSLSF HYASPQGLNL AELCVVRSQR
     RSVQSSVVVQ DGSVATESSS SEEAKDVGVL TIPSLEADKV VAESDGGEQL STVSITVVGA
     SGDLAKKKIF PALFALYYEG CLPEHFTIFG YARSKMTDAE LRVMVSKTLT CRIDKRANCG
     EKMEEFLKRC FYHSGQYDSQ EHFVALDEKL KEHEGGRLSN RLFYLSIPPN IFVDAVKCAS
     SSASSVNGWT RVIVEKPFGR DSKTSAALTK SLKQYLEEDQ IFRIDHYLGK ELVENLSVLR
     FSNLIFEPLW SRQYIRNVQF IFSEDFGTEG RGGYFDNYGI IRDIMQNHLL QILALFAMET
     PVSLDAEDIR NEKVKVLRSM RPIKLEDVVI GQYKSHSIGG VTYPSYTDDK TVPKGSLTPT
     FAAAALFIDN ARWDGVPFLM KAGKALNTRS AEIRVQFRHV PGNLYNRNSG TDRDQTTNEL
     VIRVQPDEAI YLKINNKVPG LGMRLDQSNL NLLYSARYSK EIPDAYERLL LDAIEGERRL
     FIRSDELDAA WALFTPLLKE IEEKKTTPEF YPYGSRGPVG AHYLAAKHKV QWGDLSLDQ
//