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Database: UniProt
Entry: A0A1P8B1N1_ARATH
LinkDB: A0A1P8B1N1_ARATH
Original site: A0A1P8B1N1_ARATH 
ID   A0A1P8B1N1_ARATH        Unreviewed;       433 AA.
AC   A0A1P8B1N1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=phosphopyruvate hydratase {ECO:0000256|ARBA:ARBA00012058};
DE            EC=4.2.1.11 {ECO:0000256|ARBA:ARBA00012058};
GN   Name=LOS2 {ECO:0000313|EMBL:ANM62807.1, ECO:0000313|TAIR:AT2G36530};
GN   Synonyms=cytosolic enolase {ECO:0000313|EMBL:ANM62807.1}, ENO2
GN   {ECO:0000313|EMBL:ANM62807.1}, ENOC {ECO:0000313|EMBL:ANM62807.1},
GN   ENOLASE 2 {ECO:0000313|EMBL:ANM62807.1};
GN   OrderedLocusNames=At2g36530 {ECO:0000313|Araport:AT2G36530,
GN   ECO:0000313|EMBL:ANM62807.1};
GN   ORFNames=F1O11.16 {ECO:0000313|EMBL:ANM62807.1}, F1O11_16
GN   {ECO:0000313|EMBL:ANM62807.1};
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 {ECO:0000313|EMBL:ANM62807.1, ECO:0000313|Proteomes:UP000006548};
RN   [1] {ECO:0000313|EMBL:ANM62807.1, ECO:0000313|Proteomes:UP000006548}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S., Shea T.P., Benito M.I., Town C.D.,
RA   Fujii C.Y., Mason T., Bowman C.L., Barnstead M., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee 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] {ECO:0007829|PubMed:19245862}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA   Jones A.M., 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   [3] {ECO:0000313|Proteomes:UP000006548}
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
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).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 4/5. {ECO:0000256|ARBA:ARBA00005031}.
CC   -!- SIMILARITY: Belongs to the enolase family.
CC       {ECO:0000256|ARBA:ARBA00009604}.
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DR   EMBL; CP002685; ANM62807.1; -; Genomic_DNA.
DR   RefSeq; NP_001324936.1; NM_001336601.1.
DR   AlphaFoldDB; A0A1P8B1N1; -.
DR   SMR; A0A1P8B1N1; -.
DR   EnsemblPlants; AT2G36530.2; AT2G36530.2; AT2G36530.
DR   GeneID; 818226; -.
DR   Gramene; AT2G36530.2; AT2G36530.2; AT2G36530.
DR   Araport; AT2G36530; -.
DR   TAIR; AT2G36530; LOS2.
DR   UniPathway; UPA00109; UER00187.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; A0A1P8B1N1; baseline and differential.
DR   GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03313; enolase; 1.
DR   Gene3D; 3.20.20.120; Enolase-like C-terminal domain; 1.
DR   Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 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   NCBIfam; TIGR01060; eno; 1.
DR   PANTHER; PTHR11902:SF59; BIFUNCTIONAL ENOLASE 2_TRANSCRIPTIONAL ACTIVATOR; 1.
DR   PANTHER; PTHR11902; ENOLASE; 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   SFLD; SFLDS00001; Enolase; 1.
DR   SMART; SM01192; Enolase_C; 1.
DR   SMART; SM01193; Enolase_N; 1.
DR   SUPFAM; SSF51604; Enolase C-terminal domain-like; 1.
DR   SUPFAM; SSF54826; Enolase N-terminal domain-like; 1.
DR   PROSITE; PS00164; ENOLASE; 1.
PE   1: Evidence at protein level;
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:A0A1P8B1N1,
KW   ECO:0007829|ProteomicsDB:A0A1P8B1N1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006548}.
FT   DOMAIN          6..128
FT                   /note="Enolase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01193"
FT   DOMAIN          136..429
FT                   /note="Enolase C-terminal TIM barrel"
FT                   /evidence="ECO:0000259|SMART:SM01192"
FT   ACT_SITE        204
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-1"
FT   ACT_SITE        341
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-1"
FT   BINDING         152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         289
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         316
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         368..371
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         392
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
SQ   SEQUENCE   433 AA;  46517 MW;  607D8C1808458F19 CRC64;
     MIGDLISAIW IVDIHTSNGI KVTAAVPSGA STGIYEALEL RDGGSDYLGK GVSKAVGNVN
     NIIGPALIGK DPTQQTAIDN FMVHELDGTQ NEWGWCKQKL GANAILAVSL AVCKAGAVVS
     GIPLYKHIAN LAGNPKIVLP VPAFNVINGG SHAGNKLAMQ EFMILPVGAA SFKEAMKMGV
     EVYHHLKSVI KKKYGQDATN VGDEGGFAPN IQENKEGLEL LKTAIEKAGY TGKVVIGMDV
     AASEFYSEDK TYDLNFKEEN NNGSQKISGD ALKDLYKSFV AEYPIVSIED PFDQDDWEHY
     AKMTTECGTE VQIVGDDLLV TNPKRVAKAI AEKSCNALLL KVNQIGSVTE SIEAVKMSKK
     AGWGVMTSHR SGETEDTFIA DLAVGLSTGQ IKTGAPCRSE RLAKYNQLLR IEEELGSEAI
     YAGVNFRKPV EPY
//
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