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Bifunctional enolase 2/transcriptional activator (EC 4 2 1 11) (2-phospho-D-glycerate hydro-lyase 2) (2-phosphoglycerate dehydratase 2) (LOW EXPRESSION OF OSMOTICALLY RESPONSIVE GENES 1)

 ENO2_ARATH              Reviewed;         444 AA.
P25696; Q8RWM8; Q8VYG4; Q940N0;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
01-MAY-1992, sequence version 1.
26-FEB-2020, entry version 160.
RecName: Full=Bifunctional enolase 2/transcriptional activator;
EC=4.2.1.11;
AltName: Full=2-phospho-D-glycerate hydro-lyase 2;
AltName: Full=2-phosphoglycerate dehydratase 2;
AltName: Full=LOW EXPRESSION OF OSMOTICALLY RESPONSIVE GENES 1;
Name=ENO2; Synonyms=LOS2; OrderedLocusNames=At2g36530; ORFNames=F1O11.16;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1841726; DOI=10.1105/tpc.3.7.719;
van der Straeten D., Rodrigues-Pousada R.A., Goodman H.M., van Montagu M.;
"Plant enolase: gene structure, expression, and evolution.";
Plant Cell 3:719-735(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
Nature 402:761-768(1999).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana reference
genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-326.
PubMed=12032082; DOI=10.1093/emboj/21.11.2692;
Lee H., Guo Y., Ohta M., Xiong L., Stevenson B., Zhu J.K.;
"LOS2, a genetic locus required for cold-responsive gene transcription
encodes a bi-functional enolase.";
EMBO J. 21:2692-2702(2002).
[6]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=12953116; DOI=10.1105/tpc.012500;
Giege P., Heazlewood J.L., Roessner-Tunali U., Millar A.H., Fernie A.R.,
Leaver C.J., Sweetlove L.J.;
"Enzymes of glycolysis are functionally associated with the mitochondrion
in Arabidopsis cells.";
Plant Cell 15:2140-2151(2003).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Columbia;
PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
Rathjen J.P., Peck S.C.;
"Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
thaliana.";
J. Proteomics 72:439-451(2009).
[8]
FUNCTION.
PubMed=20028841; DOI=10.1105/tpc.109.069211;
Barkla B.J., Vera-Estrella R., Hernandez-Coronado M., Pantoja O.;
"Quantitative proteomics of the tonoplast reveals a role for glycolytic
enzymes in salt tolerance.";
Plant Cell 21:4044-4058(2009).
-!- FUNCTION: Multifunctional enzyme that acts as an enolase involved in
the metabolism and as a positive regulator of cold-responsive gene
transcription. Binds to the cis-element the gene promoter of STZ/ZAT10,
a zinc finger transcriptional repressor. {ECO:0000269|PubMed:12032082,
ECO:0000269|PubMed:20028841}.
-!- CATALYTIC ACTIVITY:
Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate;
Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289,
ChEBI:CHEBI:58702; EC=4.2.1.11;
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Note=Mg(2+) is required for catalysis and for stabilizing the dimer.;
-!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
glyceraldehyde 3-phosphate: step 4/5.
-!- SUBUNIT: Homodimer.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12032082,
ECO:0000269|PubMed:12953116}. Nucleus {ECO:0000269|PubMed:12032082}.
Mitochondrion outer membrane {ECO:0000269|PubMed:12953116}. Note=Found
in circular or rod-shaped bodies that colocalizes with mitochondrion
marker. {ECO:0000269|PubMed:12953116}.
-!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
---------------------------------------------------------------------------
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EMBL; X58107; CAA41114.1; -; Genomic_DNA.
EMBL; AC006919; AAD24635.1; -; Genomic_DNA.
EMBL; CP002685; AEC09265.1; -; Genomic_DNA.
EMBL; AF424603; AAL11597.1; -; mRNA.
EMBL; AY054253; AAL06912.1; -; mRNA.
EMBL; AY072095; AAL59917.1; -; mRNA.
EMBL; AY092986; AAM12985.1; -; mRNA.
EMBL; AY150418; AAN12963.1; -; mRNA.
PIR; JQ1187; JQ1187.
RefSeq; NP_181192.1; NM_129209.4.
SMR; P25696; -.
BioGrid; 3570; 5.
IntAct; P25696; 1.
STRING; 3702.AT2G36530.1; -.
iPTMnet; P25696; -.
SwissPalm; P25696; -.
SWISS-2DPAGE; P25696; -.
PaxDb; P25696; -.
PRIDE; P25696; -.
EnsemblPlants; AT2G36530.1; AT2G36530.1; AT2G36530.
GeneID; 818226; -.
Gramene; AT2G36530.1; AT2G36530.1; AT2G36530.
KEGG; ath:AT2G36530; -.
Araport; AT2G36530; -.
TAIR; locus:2044851; AT2G36530.
eggNOG; KOG2670; Eukaryota.
eggNOG; COG0148; LUCA.
HOGENOM; CLU_031223_0_0_1; -.
InParanoid; P25696; -.
KO; K01689; -.
OMA; TRYKGKA; -.
OrthoDB; 773373at2759; -.
PhylomeDB; P25696; -.
BioCyc; ARA:AT2G36530-MONOMER; -.
BioCyc; MetaCyc:AT2G36530-MONOMER; -.
UniPathway; UPA00109; UER00187.
PRO; PR:P25696; -.
Proteomes; UP000006548; Chromosome 2.
Proteomes; UP000007605; Chromosome 2, ARATH_2.
ExpressionAtlas; P25696; baseline and differential.
Genevisible; P25696; AT.
GO; GO:0048046; C:apoplast; IDA:TAIR.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0005737; C:cytoplasm; IDA:TAIR.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
GO; GO:0005740; C:mitochondrial envelope; IDA:TAIR.
GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:TAIR.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0005507; F:copper ion binding; IDA:TAIR.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0004634; F:phosphopyruvate hydratase activity; IDA:TAIR.
GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
GO; GO:0009409; P:response to cold; IMP:TAIR.
GO; GO:0009416; P:response to light stimulus; IMP:TAIR.
CDD; cd03313; enolase; 1.
Gene3D; 3.20.20.120; -; 1.
Gene3D; 3.30.390.10; -; 1.
HAMAP; MF_00318; Enolase; 1.
InterPro; IPR000941; Enolase.
InterPro; IPR036849; Enolase-like_C_sf.
InterPro; IPR029017; Enolase-like_N.
InterPro; IPR020810; Enolase_C.
InterPro; IPR020809; Enolase_CS.
InterPro; IPR020811; Enolase_N.
PANTHER; PTHR11902; PTHR11902; 1.
Pfam; PF00113; Enolase_C; 1.
Pfam; PF03952; Enolase_N; 1.
PIRSF; PIRSF001400; Enolase; 1.
PRINTS; PR00148; ENOLASE.
SFLD; SFLDG00178; enolase; 1.
SMART; SM01192; Enolase_C; 1.
SMART; SM01193; Enolase_N; 1.
SUPFAM; SSF51604; SSF51604; 1.
SUPFAM; SSF54826; SSF54826; 1.
TIGRFAMs; TIGR01060; eno; 1.
PROSITE; PS00164; ENOLASE; 1.
1: Evidence at protein level;
Cytoplasm; DNA-binding; Glycolysis; Lyase; Magnesium; Membrane;
Metal-binding; Mitochondrion; Mitochondrion outer membrane; Nucleus;
Reference proteome; Repressor; Transcription; Transcription regulation.
CHAIN 1..444
/note="Bifunctional enolase 2/transcriptional activator"
/id="PRO_0000134067"
REGION 379..382
/note="Substrate binding"
/evidence="ECO:0000250"
ACT_SITE 215
/note="Proton donor"
/evidence="ECO:0000250"
ACT_SITE 352
/note="Proton acceptor"
/evidence="ECO:0000250"
METAL 250
/note="Magnesium"
/evidence="ECO:0000250"
METAL 300
/note="Magnesium"
/evidence="ECO:0000250"
METAL 327
/note="Magnesium"
/evidence="ECO:0000250"
BINDING 163
/note="Substrate"
/evidence="ECO:0000250"
BINDING 172
/note="Substrate"
/evidence="ECO:0000250"
BINDING 300
/note="Substrate"
/evidence="ECO:0000250"
BINDING 327
/note="Substrate"
/evidence="ECO:0000250"
BINDING 403
/note="Substrate"
/evidence="ECO:0000250"
MUTAGEN 326
/note="G->S: Impairs cold-responsive gene transcription."
/evidence="ECO:0000269|PubMed:12032082"
CONFLICT 73
/note="I -> V (in Ref. 4; AAL06912)"
/evidence="ECO:0000305"
CONFLICT 160
/note="G -> D (in Ref. 4; AAM12985)"
/evidence="ECO:0000305"
CONFLICT 207
/note="Q -> H (in Ref. 4; AAL59917)"
/evidence="ECO:0000305"
CONFLICT 386
/note="E -> K (in Ref. 4; AAL06912)"
/evidence="ECO:0000305"
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


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