ID   ENO_POPEU               Reviewed;          26 AA.
AC   P84541;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Enolase;
DE            EC=4.2.1.11;
DE   AltName: Full=2-phospho-D-glycerate hydro-lyase;
DE   AltName: Full=2-phosphoglycerate dehydratase;
DE   Flags: Fragments;
OS   Populus euphratica (Euphrates poplar).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX   NCBI_TaxID=75702;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Leaf;
RX   PubMed=16740589; DOI=10.1093/aob/mcl106;
RA   Ferreira S., Hjernoe K., Larsen M., Wingsle G., Larsen P., Fey S.,
RA   Roepstorff P., Pais M.S.;
RT   "Proteome profiling of Populus euphratica Oliv. upon heat stress.";
RL   Ann. Bot. 98:361-377(2006).
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:0000250|UniProtKB:P42895};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q42971};
CC       Note=Mg(2+) is required for catalysis and for stabilizing the dimer.
CC       {ECO:0000250|UniProtKB:Q42971};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 4/5.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P42895}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the enolase family. {ECO:0000255}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P84541; -.
DR   UniPathway; UPA00109; UER00187.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR029017; Enolase-like_N.
DR   SUPFAM; SSF54826; SSF54826; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Glycolysis; Lyase; Magnesium;
KW   Metal-binding.
FT   CHAIN           <1..>26
FT                   /note="Enolase"
FT                   /id="PRO_0000134077"
FT   NON_CONS        18..19
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         26
SQ   SEQUENCE   26 AA;  2751 MW;  C17438AD1FF8A6A2 CRC64;
     AAVPSGASTG VYEALELRFR APVEPY