G6PD1_ARATH
ID G6PD1_ARATH Reviewed; 576 AA.
AC Q43727; O65577; Q9FFM5;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase 1, chloroplastic {ECO:0000305};
DE Short=AtG6PD1 {ECO:0000303|PubMed:15634201};
DE Short=G6PDH1 {ECO:0000305};
DE EC=1.1.1.49 {ECO:0000269|PubMed:15634201};
DE Flags: Precursor;
GN Name=G6PD1 {ECO:0000303|PubMed:15634201}; Synonyms=APG1 {ECO:0000305};
GN OrderedLocusNames=At5g35790 {ECO:0000312|Araport:AT5G35790};
GN ORFNames=MIK22.2 {ECO:0000312|EMBL:BAB09918.1}, MWP19.3 {ECO:0000305};
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 [MRNA].
RX 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 isoforms
RT 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 PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-576.
RC STRAIN=cv. Columbia;
RA Fink A., Greppin H., Tacchini P.;
RT "Nucleotide sequence of a cDNA encoding the glucose-6-phosphate
RT dehydrogenase from Arabidopsis thaliana.";
RL (er) Plant Gene Register PGR95-021(1995).
RN [7]
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 [8]
RP INTERACTION WITH G6PD2; G6PD3 AND G6PD4, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF CYS-149; CYS-157 AND LYS-565.
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).
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=4.3 uM for NADP {ECO:0000269|PubMed:15634201};
CC pH dependence:
CC Optimum pH is 8.0. {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 G6PD2, G6PD3
CC and G6PD4 (PubMed:21309870). {ECO:0000250|UniProtKB:P11411,
CC ECO:0000269|PubMed:21309870}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:21309870}. Peroxisome
CC {ECO:0000269|PubMed:21309870}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems, buds, flowers and
CC siliques. {ECO:0000269|PubMed:15634201}.
CC -!- DEVELOPMENTAL STAGE: Increase of activity in the apex linked to the
CC early stages of the transition from vegetative to reproductive growth.
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 -!- SEQUENCE CAUTION:
CC Sequence=CAA59012.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ001359; CAA04696.1; -; mRNA.
DR EMBL; AB005236; BAB09918.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94018.1; -; Genomic_DNA.
DR EMBL; AY099561; AAM20413.1; -; mRNA.
DR EMBL; BT002133; AAN72144.1; -; mRNA.
DR EMBL; AY086213; AAM64291.1; -; mRNA.
DR EMBL; X84230; CAA59012.1; ALT_FRAME; mRNA.
DR RefSeq; NP_198428.1; NM_122970.6.
DR AlphaFoldDB; Q43727; -.
DR SMR; Q43727; -.
DR BioGRID; 18812; 5.
DR IntAct; Q43727; 1.
DR STRING; 3702.AT5G35790.1; -.
DR PaxDb; Q43727; -.
DR PRIDE; Q43727; -.
DR ProteomicsDB; 248600; -.
DR EnsemblPlants; AT5G35790.1; AT5G35790.1; AT5G35790.
DR GeneID; 833559; -.
DR Gramene; AT5G35790.1; AT5G35790.1; AT5G35790.
DR KEGG; ath:AT5G35790; -.
DR Araport; AT5G35790; -.
DR TAIR; locus:2165154; AT5G35790.
DR eggNOG; KOG0563; Eukaryota.
DR HOGENOM; CLU_013524_2_3_1; -.
DR InParanoid; Q43727; -.
DR OMA; PDEGIQM; -.
DR OrthoDB; 383995at2759; -.
DR PhylomeDB; Q43727; -.
DR BRENDA; 1.1.1.49; 399.
DR UniPathway; UPA00115; UER00408.
DR PRO; PR:Q43727; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q43727; baseline and differential.
DR Genevisible; Q43727; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005777; C:peroxisome; 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 PIRSF; PIRSF000110; G6PD; 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 Carbohydrate metabolism; Chloroplast; Disulfide bond; Glucose metabolism;
KW NADP; Oxidoreductase; Peroxisome; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..50
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 51..576
FT /note="Glucose-6-phosphate 1-dehydrogenase 1,
FT chloroplastic"
FT /id="PRO_0000010435"
FT ACT_SITE 326
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P11411"
FT BINDING 97..104
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 131
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 234
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 264..268
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 302
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 321
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 422
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 427
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 463
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT DISULFID 149..157
FT /note="Redox modulation"
FT /evidence="ECO:0000250|UniProtKB:Q43839"
FT MUTAGEN 149
FT /note="C->S: No effect on the interaction with G6PD4."
FT /evidence="ECO:0000269|PubMed:21309870"
FT MUTAGEN 157
FT /note="C->S: No effect on the interaction with G6PD4."
FT /evidence="ECO:0000269|PubMed:21309870"
FT MUTAGEN 565
FT /note="K->E: Abolishes targeting to peroxisome."
FT /evidence="ECO:0000269|PubMed:21309870"
FT CONFLICT 110
FT /note="A -> D (in Ref. 6; CAA59012)"
FT /evidence="ECO:0000305"
FT CONFLICT 205..213
FT /note="IPPNIFVDV -> STPKLLVDE (in Ref. 1; CAA04696)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="Q -> E (in Ref. 6; CAA59012)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="G -> A (in Ref. 6; CAA59012)"
FT /evidence="ECO:0000305"
FT CONFLICT 485..486
FT /note="RS -> PR (in Ref. 1; CAA04696)"
FT /evidence="ECO:0000305"
FT CONFLICT 514
FT /note="G -> A (in Ref. 1; CAA04696)"
FT /evidence="ECO:0000305"
FT CONFLICT 530
FT /note="D -> E (in Ref. 1; CAA04696)"
FT /evidence="ECO:0000305"
FT CONFLICT 539
FT /note="L -> R (in Ref. 1; CAA04696)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 576 AA; 65428 MW; 6559FFCCF76F44DF CRC64;
MATHSMIIPS PSSSSSSLAT AASPFKETLP LFSRSLTFPR KSLFSQVRLR FFAEKHSQLD
TSNGCATNFA SLQDSGDQLT EEHVTKGEST LSITVVGASG DLAKKKIFPA LFALFYEGCL
PQDFSVFGYA RTKLTHEELR DMISSTLTCR IDQREKCGDK MEQFLKRCFY HSGQYNSEED
FAELNKKLKE KEAGKISNRL YYLSIPPNIF VDVVRCASLR ASSENGWTRV IVEKPFGRDS
ESSGELTRCL KQYLTEEQIF RIDHYLGKEL VENLSVLRFS NLVFEPLWSR NYIRNVQLIF
SEDFGTEGRG GYFDQYGIIR DIMQNHLLQI LALFAMETPV SLDAEDIRSE KVKVLRSMKP
LRLEDVVVGQ YKGHNKGGKT YPGYTDDPTV PNHSLTPTFA AAAMFINNAR WDGVPFLMKA
GKALHTRGAE IRVQFRHVPG NLYKKSFATN LDNATNELVI RVQPDEGIYL RINNKVPGLG
MRLDRSDLNL LYRSRYPREI PDAYERLLLD AIEGERRLFI RSDELDAAWD LFTPALKELE
EKKIIPELYP YGSRGPVGAH YLASKYNVRW GDLGEA
