ENO2_ARATH
ID ENO2_ARATH Reviewed; 444 AA.
AC P25696; Q8RWM8; Q8VYG4; Q940N0;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Bifunctional enolase 2/transcriptional activator;
DE EC=4.2.1.11 {ECO:0000269|PubMed:12032082};
DE AltName: Full=2-phospho-D-glycerate hydro-lyase 2;
DE AltName: Full=2-phosphoglycerate dehydratase 2 {ECO:0000303|PubMed:20028841};
DE AltName: Full=LOW EXPRESSION OF OSMOTICALLY RESPONSIVE GENES 1;
GN Name=ENO2; Synonyms=LOS2; OrderedLocusNames=At2g36530; ORFNames=F1O11.16;
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 [GENOMIC DNA].
RX PubMed=1841726; DOI=10.1105/tpc.3.7.719;
RA van der Straeten D., Rodrigues-Pousada R.A., Goodman H.M., van Montagu M.;
RT "Plant enolase: gene structure, expression, and evolution.";
RL Plant Cell 3:719-735(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF GLY-326.
RX PubMed=12032082; DOI=10.1093/emboj/21.11.2692;
RA Lee H., Guo Y., Ohta M., Xiong L., Stevenson B., Zhu J.K.;
RT "LOS2, a genetic locus required for cold-responsive gene transcription
RT encodes a bi-functional enolase.";
RL EMBO J. 21:2692-2702(2002).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=12953116; DOI=10.1105/tpc.012500;
RA Giege P., Heazlewood J.L., Roessner-Tunali U., Millar A.H., Fernie A.R.,
RA Leaver C.J., Sweetlove L.J.;
RT "Enzymes of glycolysis are functionally associated with the mitochondrion
RT in Arabidopsis cells.";
RL Plant Cell 15:2140-2151(2003).
RN [7]
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 [8]
RP FUNCTION.
RX PubMed=20028841; DOI=10.1105/tpc.109.069211;
RA Barkla B.J., Vera-Estrella R., Hernandez-Coronado M., Pantoja O.;
RT "Quantitative proteomics of the tonoplast reveals a role for glycolytic
RT enzymes in salt tolerance.";
RL Plant Cell 21:4044-4058(2009).
CC -!- FUNCTION: Multifunctional enzyme that acts as an enolase involved in
CC the metabolism and as a positive regulator of cold-responsive gene
CC transcription (PubMed:12032082). Binds to the cis-element the gene
CC promoter of STZ/ZAT10, a zinc finger transcriptional repressor
CC (PubMed:12032082). {ECO:0000269|PubMed:12032082,
CC ECO:0000269|PubMed:20028841}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289,
CC ChEBI:CHEBI:58702; EC=4.2.1.11;
CC Evidence={ECO:0000269|PubMed:12032082};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10165;
CC Evidence={ECO:0000269|PubMed:12032082};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Mg(2+) is required for catalysis and for stabilizing the dimer.;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5. {ECO:0000269|PubMed:12032082}.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12032082,
CC ECO:0000269|PubMed:12953116}. Nucleus {ECO:0000269|PubMed:12032082}.
CC Mitochondrion outer membrane {ECO:0000269|PubMed:12953116}. Note=Found
CC in circular or rod-shaped bodies that colocalizes with mitochondrion
CC marker. {ECO:0000269|PubMed:12953116}.
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
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DR EMBL; X58107; CAA41114.1; -; Genomic_DNA.
DR EMBL; AC006919; AAD24635.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09265.1; -; Genomic_DNA.
DR EMBL; AF424603; AAL11597.1; -; mRNA.
DR EMBL; AY054253; AAL06912.1; -; mRNA.
DR EMBL; AY072095; AAL59917.1; -; mRNA.
DR EMBL; AY092986; AAM12985.1; -; mRNA.
DR EMBL; AY150418; AAN12963.1; -; mRNA.
DR PIR; JQ1187; JQ1187.
DR RefSeq; NP_181192.1; NM_129209.4.
DR AlphaFoldDB; P25696; -.
DR SMR; P25696; -.
DR BioGRID; 3570; 5.
DR IntAct; P25696; 1.
DR STRING; 3702.AT2G36530.1; -.
DR iPTMnet; P25696; -.
DR MetOSite; P25696; -.
DR SwissPalm; P25696; -.
DR SWISS-2DPAGE; P25696; -.
DR PaxDb; P25696; -.
DR PRIDE; P25696; -.
DR ProteomicsDB; 220458; -.
DR EnsemblPlants; AT2G36530.1; AT2G36530.1; AT2G36530.
DR GeneID; 818226; -.
DR Gramene; AT2G36530.1; AT2G36530.1; AT2G36530.
DR KEGG; ath:AT2G36530; -.
DR Araport; AT2G36530; -.
DR TAIR; locus:2044851; AT2G36530.
DR eggNOG; KOG2670; Eukaryota.
DR HOGENOM; CLU_031223_0_0_1; -.
DR InParanoid; P25696; -.
DR OMA; KHADNGI; -.
DR OrthoDB; 773373at2759; -.
DR PhylomeDB; P25696; -.
DR BioCyc; ARA:AT2G36530-MON; -.
DR BioCyc; MetaCyc:AT2G36530-MON; -.
DR UniPathway; UPA00109; UER00187.
DR PRO; PR:P25696; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P25696; baseline and differential.
DR Genevisible; P25696; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005740; C:mitochondrial envelope; IDA:TAIR.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IDA:TAIR.
DR GO; GO:0006096; P:glycolytic process; IDA:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0009409; P:response to cold; IMP:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IMP:TAIR.
DR CDD; cd03313; enolase; 1.
DR Gene3D; 3.20.20.120; -; 1.
DR Gene3D; 3.30.390.10; -; 1.
DR HAMAP; MF_00318; Enolase; 1.
DR InterPro; IPR000941; Enolase.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR020810; Enolase_C.
DR InterPro; IPR020809; Enolase_CS.
DR InterPro; IPR020811; Enolase_N.
DR PANTHER; PTHR11902; PTHR11902; 1.
DR Pfam; PF00113; Enolase_C; 1.
DR Pfam; PF03952; Enolase_N; 1.
DR PIRSF; PIRSF001400; Enolase; 1.
DR PRINTS; PR00148; ENOLASE.
DR SFLD; SFLDF00002; enolase; 1.
DR SMART; SM01192; Enolase_C; 1.
DR SMART; SM01193; Enolase_N; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
DR TIGRFAMs; TIGR01060; eno; 1.
DR PROSITE; PS00164; ENOLASE; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; DNA-binding; Glycolysis; Lyase; Magnesium; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion outer membrane; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..444
FT /note="Bifunctional enolase 2/transcriptional activator"
FT /id="PRO_0000134067"
FT ACT_SITE 215
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 352
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 327
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 327
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 379..382
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 403
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MUTAGEN 326
FT /note="G->S: Impairs cold-responsive gene transcription."
FT /evidence="ECO:0000269|PubMed:12032082"
FT CONFLICT 73
FT /note="I -> V (in Ref. 4; AAL06912)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="G -> D (in Ref. 4; AAM12985)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="Q -> H (in Ref. 4; AAL59917)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="E -> K (in Ref. 4; AAL06912)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 444 AA; 47719 MW; 4037C7E0390B6C2B CRC64;
MATITVVKAR QIFDSRGNPT VEVDIHTSNG IKVTAAVPSG ASTGIYEALE LRDGGSDYLG
KGVSKAVGNV NNIIGPALIG KDPTQQTAID NFMVHELDGT QNEWGWCKQK LGANAILAVS
LAVCKAGAVV SGIPLYKHIA NLAGNPKIVL PVPAFNVING GSHAGNKLAM QEFMILPVGA
ASFKEAMKMG VEVYHHLKSV IKKKYGQDAT NVGDEGGFAP NIQENKEGLE LLKTAIEKAG
YTGKVVIGMD VAASEFYSED KTYDLNFKEE NNNGSQKISG DALKDLYKSF VAEYPIVSIE
DPFDQDDWEH YAKMTTECGT EVQIVGDDLL VTNPKRVAKA IAEKSCNALL LKVNQIGSVT
ESIEAVKMSK KAGWGVMTSH RSGETEDTFI ADLAVGLSTG QIKTGAPCRS ERLAKYNQLL
RIEEELGSEA IYAGVNFRKP VEPY
