G6PD3_ARATH
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 03-AUG-2022, entry version 152.
DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase 3, chloroplastic {ECO:0000305};
DE Short=AtG6PD3 {ECO:0000303|PubMed:15634201};
DE Short=G6PDH3 {ECO:0000305};
DE EC=1.1.1.49 {ECO:0000269|PubMed:15634201};
DE Flags: Precursor;
GN Name=G6PD3 {ECO:0000303|PubMed:15634201};
GN OrderedLocusNames=At1g24280 {ECO:0000312|Araport:AT1G24280};
GN ORFNames=F3I6.22 {ECO:0000312|EMBL:AAC00588.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., 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., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
RX PubMed=15634201; DOI=10.1111/j.1365-313x.2004.02293.x;
RA Wakao S., Benning C.;
RT "Genome-wide analysis of glucose-6-phosphate dehydrogenases in
RT Arabidopsis.";
RL Plant J. 41:243-256(2005).
RN [5]
RP INTERACTION WITH G6PD1, AND SUBCELLULAR LOCATION.
RX PubMed=21309870; DOI=10.1111/j.1365-313x.2011.04535.x;
RA Meyer T., Hoelscher C., Schwoeppe C., von Schaewen A.;
RT "Alternative targeting of Arabidopsis plastidic glucose-6-phosphate
RT dehydrogenase G6PD1 involves cysteine-dependent interaction with G6PD4 in
RT the cytosol.";
RL Plant J. 66:745-758(2011).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-67, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER SER-66, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Catalyzes the rate-limiting step of the oxidative pentose-
CC phosphate pathway, which represents a route for the dissimilation of
CC carbohydrates besides glycolysis (PubMed:15634201). The main function
CC of this enzyme is to provide reducing power (NADPH) and pentose
CC phosphates for fatty acid and nucleic acid synthesis which are involved
CC in membrane synthesis and cell division (PubMed:15634201).
CC {ECO:0000269|PubMed:15634201}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-
CC lactone + H(+) + NADPH; Xref=Rhea:RHEA:15841, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57955, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:61548; EC=1.1.1.49;
CC Evidence={ECO:0000269|PubMed:15634201};
CC -!- ACTIVITY REGULATION: Regulated by metabolites. Post-translationally
CC inactivated by cysteine-mediated redox modification via the ferredoxin-
CC thioredoxin system in the light and this avoids futile cycles with
CC photosynthetic CO2 fixation. {ECO:0000250|UniProtKB:Q43839}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=17 uM for NADP {ECO:0000269|PubMed:15634201};
CC pH dependence:
CC Optimum pH is 8.0-8.5. {ECO:0000269|PubMed:15634201};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC 1/3. {ECO:0000305}.
CC -!- SUBUNIT: Forms homodimer (By similarity). Interacts with G6PD1
CC (PubMed:21309870). {ECO:0000250|UniProtKB:P11411,
CC ECO:0000269|PubMed:21309870}.
CC -!- INTERACTION:
CC Q8L743; Q8S8E3: PYL6; NbExp=3; IntAct=EBI-2355237, EBI-2363192;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:21309870}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, flowers and siliques.
CC {ECO:0000269|PubMed:15634201}.
CC -!- MISCELLANEOUS: There are 6 glucose-6-phosphate 1-dehydrogenase genes in
CC A.thaliana. {ECO:0000303|PubMed:15634201}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC002396; AAC00588.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30511.1; -; Genomic_DNA.
DR EMBL; AY139768; AAM98087.1; -; mRNA.
DR EMBL; BT003032; AAO23597.1; -; mRNA.
DR PIR; T00659; T00659.
DR RefSeq; NP_173838.1; NM_102274.3.
DR AlphaFoldDB; Q8L743; -.
DR SMR; Q8L743; -.
DR BioGRID; 24282; 3.
DR IntAct; Q8L743; 2.
DR STRING; 3702.AT1G24280.1; -.
DR iPTMnet; Q8L743; -.
DR PaxDb; Q8L743; -.
DR PRIDE; Q8L743; -.
DR ProteomicsDB; 230021; -.
DR EnsemblPlants; AT1G24280.1; AT1G24280.1; AT1G24280.
DR GeneID; 839044; -.
DR Gramene; AT1G24280.1; AT1G24280.1; AT1G24280.
DR KEGG; ath:AT1G24280; -.
DR Araport; AT1G24280; -.
DR TAIR; locus:2032412; AT1G24280.
DR eggNOG; KOG0563; Eukaryota.
DR HOGENOM; CLU_013524_2_3_1; -.
DR InParanoid; Q8L743; -.
DR OMA; PEFYPYG; -.
DR OrthoDB; 383995at2759; -.
DR PhylomeDB; Q8L743; -.
DR BRENDA; 1.1.1.49; 399.
DR UniPathway; UPA00115; UER00408.
DR PRO; PR:Q8L743; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8L743; baseline and differential.
DR Genevisible; Q8L743; AT.
DR GO; GO:0009507; C:chloroplast; ISS:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IDA:TAIR.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IDA:TAIR.
DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IDA:TAIR.
DR HAMAP; MF_00966; G6PD; 1.
DR InterPro; IPR001282; G6P_DH.
DR InterPro; IPR019796; G6P_DH_AS.
DR InterPro; IPR022675; G6P_DH_C.
DR InterPro; IPR022674; G6P_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR23429; PTHR23429; 1.
DR Pfam; PF02781; G6PD_C; 1.
DR Pfam; PF00479; G6PD_N; 1.
DR PRINTS; PR00079; G6PDHDRGNASE.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00871; zwf; 1.
DR PROSITE; PS00069; G6P_DEHYDROGENASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Carbohydrate metabolism; Chloroplast; Disulfide bond;
KW Glucose metabolism; NADP; Oxidoreductase; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..66
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 67..599
FT /note="Glucose-6-phosphate 1-dehydrogenase 3,
FT chloroplastic"
FT /id="PRO_0000010437"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 348
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P11411"
FT BINDING 119..126
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 119..126
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 153
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 256
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 256
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 286..290
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 324
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 343
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 444
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 449
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 485
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT MOD_RES 67
FT /note="N-acetylvaline"
FT /evidence="ECO:0007744|PubMed:22223895"
FT DISULFID 171..179
FT /note="Redox modulation"
FT /evidence="ECO:0000250|UniProtKB:Q43839"
FT CONFLICT 79
FT /note="S -> N (in Ref. 3; AAM98087/AAO23597)"
FT /evidence="ECO:0000305"
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
