ENO3_ARATH
ID ENO3_ARATH Reviewed; 475 AA.
AC Q9ZW34;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Cytosolic enolase 3;
DE EC=4.2.1.11;
DE AltName: Full=2-phospho-D-glycerate hydro-lyase 3;
DE AltName: Full=2-phosphoglycerate dehydratase 3;
GN Name=ENO3; Synonyms=ENOC; OrderedLocusNames=At2g29560; ORFNames=F16P2.6;
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=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 [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 SUBCELLULAR LOCATION.
RX PubMed=19223001; DOI=10.1016/j.febslet.2009.02.017;
RA Prabhakar V., Lottgert T., Gigolashvili T., Bell K., Flugge U.I.,
RA Hausler R.E.;
RT "Molecular and functional characterization of the plastid-localized
RT Phosphoenolpyruvate enolase (ENO1) from Arabidopsis thaliana.";
RL FEBS Lett. 583:983-991(2009).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 -!- 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Mg(2+) is required for catalysis and for stabilizing the dimer.
CC {ECO:0000250};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19223001}. Nucleus
CC {ECO:0000269|PubMed:19223001}.
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
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DR EMBL; AC004561; AAC95183.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08273.1; -; Genomic_DNA.
DR EMBL; AY035128; AAK59633.1; -; mRNA.
DR EMBL; AY113918; AAM44966.1; -; mRNA.
DR PIR; G84697; G84697.
DR RefSeq; NP_180516.1; NM_128509.4.
DR AlphaFoldDB; Q9ZW34; -.
DR SMR; Q9ZW34; -.
DR STRING; 3702.AT2G29560.1; -.
DR iPTMnet; Q9ZW34; -.
DR MetOSite; Q9ZW34; -.
DR PaxDb; Q9ZW34; -.
DR PRIDE; Q9ZW34; -.
DR ProteomicsDB; 220421; -.
DR EnsemblPlants; AT2G29560.1; AT2G29560.1; AT2G29560.
DR GeneID; 817505; -.
DR Gramene; AT2G29560.1; AT2G29560.1; AT2G29560.
DR KEGG; ath:AT2G29560; -.
DR Araport; AT2G29560; -.
DR TAIR; locus:2043067; AT2G29560.
DR eggNOG; KOG2670; Eukaryota.
DR HOGENOM; CLU_031223_2_1_1; -.
DR InParanoid; Q9ZW34; -.
DR OMA; DFCIGTK; -.
DR OrthoDB; 773373at2759; -.
DR PhylomeDB; Q9ZW34; -.
DR BioCyc; ARA:AT2G29560-MON; -.
DR UniPathway; UPA00109; UER00187.
DR PRO; PR:Q9ZW34; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZW34; baseline and differential.
DR Genevisible; Q9ZW34; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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 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 Acetylation; Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding;
KW Nucleus; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..475
FT /note="Cytosolic enolase 3"
FT /id="PRO_0000399511"
FT ACT_SITE 252
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 386
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 287
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 336
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 336
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 361
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 361
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 413..416
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 437
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 475 AA; 51600 MW; DD09B5DC58A46B57 CRC64;
MSVQEYLDKH MLSRKIEDAV NAAVRAKTSD PVLFIANHLK KAVSSVITKV KARQILDSRG
IPTVEVDLHT NKGVFRASVP SGDSSGTYEA IELRDGDKGM YLGNSVAKAV KNINEKISEA
LIGMDPKLQG QIDQAMIDLD KTEKKSELGA NAILAVSIAA CKAGAAEKEV PLCKHLSDLS
GRANMVLPVP AFTVLSGGKH ASNTFAIQEI MILPIGASRF EEALQWGSET YHHLKAVISE
KNGGLGCNVG EDGGLAPDIS SLKEGLELVK EAINRTGYND KIKIAIDIAA TNFCLGTKYD
LDIKSPNKSG QNFKSAEDMI DMYKEICNDY PIVSIEDPFD KEDWEHTKYF SSLGICQVVG
DDLLMSNSKR VERAIQESSC NALLLKVNQI GTVTEAIEVV KMARDAQWGV VTSHRCGETE
DSFISDLSVG LATGVIKAGA PCRGERTMKY NQLLRIEEEL GDQAVYAGED WKLSL
