PGKY3_ARATH
ID PGKY3_ARATH Reviewed; 401 AA.
AC Q9SAJ4; C0Z3A6; Q56ZW1; Q8LFV7;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Phosphoglycerate kinase 3, cytosolic {ECO:0000303|PubMed:24930633};
DE EC=2.7.2.3 {ECO:0000305};
GN Name=PGK3 {ECO:0000303|PubMed:24930633};
GN OrderedLocusNames=At1g79550 {ECO:0000312|Araport:AT1G79550};
GN ORFNames=T8K14.3 {ECO:0000312|EMBL:AAD30221.1};
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 [MRNA] (ISOFORM 1).
RA Shih M.-C.;
RT "Structure and regulation of nuclear genes encoding chloroplast and
RT cytosolic phosphoglycerate kinase in Arabidopsis thaliana.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [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] (ISOFORM 1).
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] (ISOFORM 2).
RC STRAIN=cv. Columbia; TISSUE=Root;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 271-401 (ISOFORM 1/2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP INDUCTION BY GLUCOSE-HEXOKINASE.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=16199612; DOI=10.1105/tpc.105.036806;
RA Chivasa S., Ndimba B.K., Simon W.J., Lindsey K., Slabas A.R.;
RT "Extracellular ATP functions as an endogenous external metabolite
RT regulating plant cell viability.";
RL Plant Cell 17:3019-3034(2005).
RN [9]
RP INDUCTION BY HEAT STRESS.
RC STRAIN=cv. Columbia;
RX PubMed=17085506; DOI=10.1104/pp.106.091322;
RA Charng Y.-Y., Liu H.-C., Liu N.-Y., Chi W.-T., Wang C.-N., Chang S.-H.,
RA Wang T.-T.;
RT "A heat-inducible transcription factor, HsfA2, is required for extension of
RT acquired thermotolerance in Arabidopsis.";
RL Plant Physiol. 143:251-262(2007).
RN [10]
RP INDUCTION BY HEAT STRESS.
RX PubMed=18055584; DOI=10.1104/pp.107.112060;
RA Larkindale J., Vierling E.;
RT "Core genome responses involved in acclimation to high temperature.";
RL Plant Physiol. 146:748-761(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [12]
RP DEVELOPMENTAL STAGE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=cv. Columbia;
RX PubMed=20118269; DOI=10.1104/pp.109.152413;
RA Hajduch M., Hearne L.B., Miernyk J.A., Casteel J.E., Joshi T.,
RA Agrawal G.K., Song Z., Zhou M., Xu D., Thelen J.J.;
RT "Systems analysis of seed filling in Arabidopsis: using general linear
RT modeling to assess concordance of transcript and protein expression.";
RL Plant Physiol. 152:2078-2087(2010).
RN [13]
RP INDUCTION BY 3OC8-HSL TREATMENT.
RX PubMed=22995300; DOI=10.1016/j.bbrc.2012.09.044;
RA Miao C., Liu F., Zhao Q., Jia Z., Song S.;
RT "A proteomic analysis of Arabidopsis thaliana seedling responses to 3-oxo-
RT octanoyl-homoserine lactone, a bacterial quorum-sensing signal.";
RL Biochem. Biophys. Res. Commun. 427:293-298(2012).
RN [14]
RP REGULATION BY LIGHT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=24884362; DOI=10.1186/1471-2164-15-320;
RA Oelze M.-L., Muthuramalingam M., Vogel M.O., Dietz K.-J.;
RT "The link between transcript regulation and de novo protein synthesis in
RT the retrograde high light acclimation response of Arabidopsis thaliana.";
RL BMC Genomics 15:320-320(2014).
RN [15]
RP TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=24930633; DOI=10.1111/tpj.12586;
RA Ouibrahim L., Mazier M., Estevan J., Pagny G., Decroocq V., Desbiez C.,
RA Moretti A., Gallois J.L., Caranta C.;
RT "Cloning of the Arabidopsis rwm1 gene for resistance to Watermelon mosaic
RT virus points to a new function for natural virus resistance genes.";
RL Plant J. 79:705-716(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl
CC phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3;
CC Evidence={ECO:0000305};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 2/5. {ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P00560}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00560}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SAJ4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SAJ4-2; Sequence=VSP_058567;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and inflorescence.
CC {ECO:0000269|PubMed:24930633}.
CC -!- DEVELOPMENTAL STAGE: Accumulates in developing seeds 5 days after
CC flowering (DAF). {ECO:0000269|PubMed:20118269}.
CC -!- INDUCTION: Repressed by glucose-hexokinase treatment (PubMed:16199612).
CC Induced by heat stress (e.g. 37 degrees Celsius) (PubMed:17085506,
CC PubMed:18055584). Accumulates in response to 3-oxo-octanoyl-homoserine
CC lactone treatment (3OC8-HSL), a bacterial quorum-sensing signal
CC (PubMed:22995300). Regulated by light (PubMed:24884362).
CC {ECO:0000269|PubMed:16199612, ECO:0000269|PubMed:17085506,
CC ECO:0000269|PubMed:18055584, ECO:0000269|PubMed:22995300,
CC ECO:0000269|PubMed:24884362}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000305}.
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DR EMBL; AF247560; AAF70260.1; -; mRNA.
DR EMBL; AC007202; AAD30221.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36262.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36263.1; -; Genomic_DNA.
DR EMBL; AF348582; AAK15553.1; -; mRNA.
DR EMBL; AY062863; AAL32941.1; -; mRNA.
DR EMBL; BT008486; AAP37845.1; -; mRNA.
DR EMBL; AK319070; BAH57185.1; -; mRNA.
DR EMBL; AY084622; AAM61185.1; -; mRNA.
DR EMBL; AK220849; BAD94190.1; -; mRNA.
DR PIR; H96826; H96826.
DR RefSeq; NP_178073.1; NM_106603.3. [Q9SAJ4-1]
DR RefSeq; NP_849907.1; NM_179576.3. [Q9SAJ4-1]
DR AlphaFoldDB; Q9SAJ4; -.
DR SMR; Q9SAJ4; -.
DR STRING; 3702.AT1G79550.2; -.
DR iPTMnet; Q9SAJ4; -.
DR PaxDb; Q9SAJ4; -.
DR PRIDE; Q9SAJ4; -.
DR ProteomicsDB; 235098; -. [Q9SAJ4-1]
DR EnsemblPlants; AT1G79550.1; AT1G79550.1; AT1G79550. [Q9SAJ4-1]
DR EnsemblPlants; AT1G79550.2; AT1G79550.2; AT1G79550. [Q9SAJ4-1]
DR GeneID; 844293; -.
DR Gramene; AT1G79550.1; AT1G79550.1; AT1G79550. [Q9SAJ4-1]
DR Gramene; AT1G79550.2; AT1G79550.2; AT1G79550. [Q9SAJ4-1]
DR KEGG; ath:AT1G79550; -.
DR Araport; AT1G79550; -.
DR TAIR; locus:2206410; AT1G79550.
DR eggNOG; KOG1367; Eukaryota.
DR HOGENOM; CLU_025427_0_2_1; -.
DR InParanoid; Q9SAJ4; -.
DR OMA; DMIFDIG; -.
DR PhylomeDB; Q9SAJ4; -.
DR UniPathway; UPA00109; UER00185.
DR PRO; PR:Q9SAJ4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SAJ4; baseline and differential.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; ISS:TAIR.
DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IMP:TAIR.
DR GO; GO:0009749; P:response to glucose; IEP:UniProtKB.
DR GO; GO:0009408; P:response to heat; IEP:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IEP:UniProtKB.
DR GO; GO:0002237; P:response to molecule of bacterial origin; IEP:UniProtKB.
DR CDD; cd00318; Phosphoglycerate_kinase; 1.
DR Gene3D; 3.40.50.1260; -; 2.
DR HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR InterPro; IPR001576; Phosphoglycerate_kinase.
DR InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR InterPro; IPR036043; Phosphoglycerate_kinase_sf.
DR PANTHER; PTHR11406; PTHR11406; 1.
DR Pfam; PF00162; PGK; 1.
DR PIRSF; PIRSF000724; Pgk; 1.
DR PRINTS; PR00477; PHGLYCKINASE.
DR SUPFAM; SSF53748; SSF53748; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Glycolysis; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..401
FT /note="Phosphoglycerate kinase 3, cytosolic"
FT /id="PRO_0000437736"
FT BINDING 25..27
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07378"
FT BINDING 41
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07378"
FT BINDING 64..67
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07378"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07378"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07378"
FT BINDING 206
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P07378"
FT BINDING 321
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P07378"
FT BINDING 328
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P07378"
FT BINDING 357..360
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P07378"
FT VAR_SEQ 1..175
FT /note="Missing (in isoform 2)"
FT /id="VSP_058567"
FT CONFLICT 166
FT /note="F -> Y (in Ref. 6; AAM61185)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="L -> I (in Ref. 6; AAM61185)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 401 AA; 42132 MW; ECB96678A51EEBBF CRC64;
MATKRSVGTL KEADLKGKSV FVRVDLNVPL DDNSNITDDT RIRAAVPTIK YLMGNGSRVV
LCSHLGRPKG VTPKYSLKPL VPRLSELLGV EVVMANDSIG EEVQKLVAGL PEGGVLLLEN
VRFYAEEEKN DPEFAKKLAA LADVYVNDAF GTAHRAHAST EGVAKFLKPS VAGFLMQKEL
DYLVGAVANP KKPFAAIVGG SKVSTKIGVI ESLLNTVDIL LLGGGMIFTF YKAQGLSVGS
SLVEEDKLDL AKSLMEKAKA KGVSLLLPTD VVIADKFAPD ANSKIVPATA IPDGWMGLDI
GPDSIKTFSE ALDTTKTIIW NGPMGVFEFD KFAAGTEAVA KQLAELSGKG VTTIIGGGDS
VAAVEKVGLA DKMSHISTGG GASLELLEGK PLPGVLALDE A
