ENO1_ARATH
ID ENO1_ARATH Reviewed; 477 AA.
AC Q9C9C4;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Enolase 1, chloroplastic;
DE EC=4.2.1.11;
DE AltName: Full=2-phospho-D-glycerate hydro-lyase 1;
DE AltName: Full=2-phosphoglycerate dehydratase 1;
DE Flags: Precursor;
GN Name=ENO1; OrderedLocusNames=At1g74030; ORFNames=F2P9.10;
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=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 [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 CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION
RP PHENOTYPE, AND BIOPHYSICOCHEMICAL PROPERTIES.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476, AND IDENTIFICATION BY
RP 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).
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:19223001};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.082 mM for 2-PGA (at pH 8) {ECO:0000269|PubMed:19223001};
CC KM=0.149 mM for 2-PGA (at pH 7) {ECO:0000269|PubMed:19223001};
CC KM=0.180 mM for PEP (at pH 8) {ECO:0000269|PubMed:19223001};
CC KM=0.534 mM for PEP (at pH 7) {ECO:0000269|PubMed:19223001};
CC KM=1.281 mM for 3-PGA (at pH 8) {ECO:0000269|PubMed:19223001};
CC KM=0.390 mM for 3-PGA (at pH 7) {ECO:0000269|PubMed:19223001};
CC pH dependence:
CC Optimum pH is 7.5-8.5 for the forward reaction (PEP formation) and
CC 6.0-7.5 for the reverse reaction (2-PGA formation).
CC {ECO:0000269|PubMed:19223001};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in young roots, young siliques,
CC and shoot apex. Lowly expressed in young leaves, stems and cotyledons.
CC {ECO:0000269|PubMed:19223001}.
CC -!- DISRUPTION PHENOTYPE: Distorted trichomes and reduced numbers of root
CC hairs. {ECO:0000269|PubMed:19223001}.
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
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DR EMBL; AC016662; AAG52510.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35539.1; -; Genomic_DNA.
DR EMBL; AY034978; AAK59483.1; -; mRNA.
DR EMBL; AY062968; AAL33814.1; -; mRNA.
DR PIR; B96768; B96768.
DR RefSeq; NP_177543.1; NM_106062.4.
DR AlphaFoldDB; Q9C9C4; -.
DR SMR; Q9C9C4; -.
DR BioGRID; 28960; 1.
DR IntAct; Q9C9C4; 1.
DR STRING; 3702.AT1G74030.1; -.
DR iPTMnet; Q9C9C4; -.
DR MetOSite; Q9C9C4; -.
DR PaxDb; Q9C9C4; -.
DR PRIDE; Q9C9C4; -.
DR ProteomicsDB; 220505; -.
DR EnsemblPlants; AT1G74030.1; AT1G74030.1; AT1G74030.
DR GeneID; 843741; -.
DR Gramene; AT1G74030.1; AT1G74030.1; AT1G74030.
DR KEGG; ath:AT1G74030; -.
DR Araport; AT1G74030; -.
DR TAIR; locus:2031476; AT1G74030.
DR eggNOG; KOG2670; Eukaryota.
DR HOGENOM; CLU_031223_2_1_1; -.
DR InParanoid; Q9C9C4; -.
DR OMA; EFMIIPV; -.
DR OrthoDB; 773373at2759; -.
DR PhylomeDB; Q9C9C4; -.
DR BioCyc; ARA:AT1G74030-MON; -.
DR UniPathway; UPA00109; UER00187.
DR PRO; PR:Q9C9C4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C9C4; baseline and differential.
DR Genevisible; Q9C9C4; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; 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; IDA:TAIR.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR GO; GO:0010090; P:trichome morphogenesis; 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 Chloroplast; Glycolysis; Lyase; Magnesium; Metal-binding; Phosphoprotein;
KW Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..41
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 42..477
FT /note="Enolase 1, chloroplastic"
FT /id="PRO_0000399510"
FT ACT_SITE 255
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 390
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 290
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 365
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 365
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 417..420
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 441
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 476
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
SQ SEQUENCE 477 AA; 51474 MW; 450D57056C64E43E CRC64;
MALTTKPHHL QRSFLSPSRV SGERYLESAP SCLRFRRSGV QCSVVAKECR VKGVKARQII
DSRGNPTVEV DLITDDLYRS AVPSGASTGI YEALELRDGD KSVYGGKGVL QAIKNINELV
APKLIGVDVR NQADVDALML ELDGTPNKSK LGANAILGVS LSVCRAGAGA KGVPLYKHIQ
ETSGTKELVM PVPAFNVING GSHAGNSLAM QEFMILPVGA TSFSEAFQMG SEVYHTLKGI
IKTKYGQDAC NVGDEGGFAP NVQDNREGLV LLIDAIEKAG YTGKIKIGMD VAASEFFMKD
GRYDLNFKKQ PNDGAHVLSA ESLADLYREF IKDFPIVSIE DPFDQDDWSS WASLQSSVDI
QLVGDDLLVT NPKRIAEAIK KQSCNALLLK VNQIGTVTES IQAALDSKAA GWGVMVSHRS
GETEDNFIAD LSVGLASGQI KTGAPCRSER LSKYNQLLRI EEELGNVRYA GEAFRSP
