G6PD2_ARATH
ID G6PD2_ARATH Reviewed; 596 AA.
AC Q9FY99; Q43728; Q8VZD6;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase 2, chloroplastic {ECO:0000305};
DE Short=AtG6PD2 {ECO:0000303|PubMed:15634201};
DE Short=G6PDH2 {ECO:0000305};
DE EC=1.1.1.49 {ECO:0000269|PubMed:15634201};
DE Flags: Precursor;
GN Name=G6PD2 {ECO:0000303|PubMed:15634201};
GN OrderedLocusNames=At5g13110 {ECO:0000312|Araport:AT5G13110};
GN ORFNames=T19L5_70 {ECO:0000312|EMBL:CAC05439.1};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 NUCLEOTIDE SEQUENCE [MRNA] OF 105-596.
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 Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-60, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER SER-59, 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=12 uM for NADP {ECO:0000269|PubMed:15634201};
CC pH dependence:
CC Optimum pH is 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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:21309870}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, buds, flowers
CC and 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=CAC05439.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL391711; CAC05439.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91851.1; -; Genomic_DNA.
DR EMBL; AY065042; AAL57678.1; -; mRNA.
DR EMBL; X84229; CAA59011.1; -; mRNA.
DR PIR; S71245; S71245.
DR RefSeq; NP_196815.2; NM_121314.4.
DR AlphaFoldDB; Q9FY99; -.
DR SMR; Q9FY99; -.
DR BioGRID; 16428; 2.
DR IntAct; Q9FY99; 1.
DR STRING; 3702.AT5G13110.1; -.
DR iPTMnet; Q9FY99; -.
DR PaxDb; Q9FY99; -.
DR PRIDE; Q9FY99; -.
DR ProteomicsDB; 228959; -.
DR EnsemblPlants; AT5G13110.1; AT5G13110.1; AT5G13110.
DR GeneID; 831150; -.
DR Gramene; AT5G13110.1; AT5G13110.1; AT5G13110.
DR KEGG; ath:AT5G13110; -.
DR Araport; AT5G13110; -.
DR TAIR; locus:2179887; AT5G13110.
DR eggNOG; KOG0563; Eukaryota.
DR HOGENOM; CLU_013524_5_0_1; -.
DR InParanoid; Q9FY99; -.
DR OMA; NARWEGV; -.
DR OrthoDB; 383995at2759; -.
DR PhylomeDB; Q9FY99; -.
DR BRENDA; 1.1.1.49; 399.
DR UniPathway; UPA00115; UER00408.
DR PRO; PR:Q9FY99; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FY99; baseline and differential.
DR Genevisible; Q9FY99; AT.
DR GO; GO:0009507; C:chloroplast; ISS:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
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..59
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 60..596
FT /note="Glucose-6-phosphate 1-dehydrogenase 2,
FT chloroplastic"
FT /id="PRO_0000010436"
FT ACT_SITE 345
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P11411"
FT BINDING 116..123
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 150
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 253
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 253
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 283..287
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 321
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 340
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 441
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 446
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 482
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT MOD_RES 60
FT /note="N-acetylvaline"
FT /evidence="ECO:0007744|PubMed:22223895"
FT DISULFID 168..176
FT /note="Redox modulation"
FT /evidence="ECO:0000250|UniProtKB:Q43839"
FT CONFLICT 145
FT /note="I -> V (in Ref. 4; CAA59011)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="H -> I (in Ref. 4; CAA59011)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="T -> I (in Ref. 4; CAA59011)"
FT /evidence="ECO:0000305"
FT CONFLICT 489
FT /note="L -> F (in Ref. 4; CAA59011)"
FT /evidence="ECO:0000305"
FT CONFLICT 542
FT /note="D -> G (in Ref. 3; AAL57678)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 596 AA; 67160 MW; BDD89BEB49EF6E3B CRC64;
MAALSSSVTT RSYHSGYLAS FSPVNGDRHR SLSFLSASPQ GLNPLDLCVR FQRKSGRASV
FMQDGAIVTN SNSSESKTSL KGLKDEVLSA LSQEAAKVGV ESDGQSQSTV SITVVGASGD
LAKKKIFPAL FALYYEGCLP EHFTIFGYSR SKMTDVELRN MVSKTLTCRI DKRANCGEKM
EEFLKRCFYH SGQYDSQEHF TELDKKLKEH EAGRISNRLF YLSIPPNIFV DAVKCASTSA
SSVNGWTRVI VEKPFGRDSE TSAALTKSLK QYLEEDQIFR IDHYLGKELV ENLSVLRFSN
LIFEPLWSRQ YIRNVQFIFS EDFGTEGRGG YFDNYGIIRD IMQNHLLQIL ALFAMETPVS
LDAEDIRNEK VKVLRSMRPI RVEDVVIGQY KSHTKGGVTY PAYTDDKTVP KGSLTPTFAA
AALFIDNARW DGVPFLMKAG KALHTRSAEI RVQFRHVPGN LYNRNTGSDL DQATNELVIR
VQPDEAIYLK INNKVPGLGM RLDRSNLNLL YSARYSKEIP DAYERLLLDA IEGERRLFIR
SDELDAAWSL FTPLLKEIEE KKRIPEYYPY GSRGPVGAHY LAAKHKVQWG DVSIDQ
