ENO_CAEEL
ID ENO_CAEEL Reviewed; 434 AA.
AC Q27527; Q6A4N1; Q8I4F9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Enolase;
DE EC=4.2.1.11 {ECO:0000250|UniProtKB:P06733};
DE AltName: Full=2-phospho-D-glycerate hydro-lyase;
DE AltName: Full=2-phosphoglycerate dehydratase;
GN Name=enol-1 {ECO:0000312|WormBase:T21B10.2a};
GN ORFNames=T21B10.2 {ECO:0000312|WormBase:T21B10.2a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP PROTEIN SEQUENCE OF 2-11 (ISOFORM A).
RC STRAIN=Bristol N2;
RX PubMed=9150941; DOI=10.1002/elps.1150180337;
RA Bini L., Heid H., Liberatori S., Geier G., Pallini V., Zwilling R.;
RT "Two-dimensional gel electrophoresis of Caenorhabditis elegans homogenates
RT and identification of protein spots by microsequencing.";
RL Electrophoresis 18:557-562(1997).
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:P06733};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P00924};
CC Note=Mg(2+) is required for catalysis and for stabilizing the dimer.
CC {ECO:0000250|UniProtKB:P00924};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5. {ECO:0000250|UniProtKB:P06733}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P00924}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00924}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:T21B10.2a};
CC IsoId=Q27527-1; Sequence=Displayed;
CC Name=c {ECO:0000312|WormBase:T21B10.2c};
CC IsoId=Q27527-3; Sequence=VSP_020148;
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
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 EMBL; BX284602; CAA92692.1; -; Genomic_DNA.
DR EMBL; BX284602; CAH10783.1; -; Genomic_DNA.
DR PIR; T25040; T25040.
DR RefSeq; NP_001022349.1; NM_001027178.2. [Q27527-3]
DR RefSeq; NP_495900.1; NM_063499.5. [Q27527-1]
DR AlphaFoldDB; Q27527; -.
DR SMR; Q27527; -.
DR BioGRID; 39750; 56.
DR IntAct; Q27527; 1.
DR STRING; 6239.T21B10.2c.1; -.
DR World-2DPAGE; 0020:Q27527; -.
DR EPD; Q27527; -.
DR PaxDb; Q27527; -.
DR PeptideAtlas; Q27527; -.
DR PRIDE; Q27527; -.
DR EnsemblMetazoa; T21B10.2a.1; T21B10.2a.1; WBGene00011884. [Q27527-1]
DR EnsemblMetazoa; T21B10.2a.2; T21B10.2a.2; WBGene00011884. [Q27527-1]
DR EnsemblMetazoa; T21B10.2c.1; T21B10.2c.1; WBGene00011884. [Q27527-3]
DR GeneID; 174423; -.
DR KEGG; cel:CELE_T21B10.2; -.
DR UCSC; T21B10.2c.1; c. elegans. [Q27527-1]
DR CTD; 174423; -.
DR WormBase; T21B10.2a; CE03684; WBGene00011884; enol-1. [Q27527-1]
DR WormBase; T21B10.2c; CE36954; WBGene00011884; enol-1. [Q27527-3]
DR eggNOG; KOG2670; Eukaryota.
DR GeneTree; ENSGT00950000182805; -.
DR HOGENOM; CLU_031223_0_0_1; -.
DR InParanoid; Q27527; -.
DR OMA; EFMIIPV; -.
DR OrthoDB; 773373at2759; -.
DR PhylomeDB; Q27527; -.
DR Reactome; R-CEL-70171; Glycolysis.
DR Reactome; R-CEL-70263; Gluconeogenesis.
DR UniPathway; UPA00109; UER00187.
DR PRO; PR:Q27527; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00011884; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:WormBase.
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 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 Alternative splicing; Cytoplasm; Direct protein sequencing; Glycolysis;
KW Lyase; Magnesium; Metal-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9150941"
FT CHAIN 2..434
FT /note="Enolase"
FT /id="PRO_0000134079"
FT ACT_SITE 210
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P00924"
FT ACT_SITE 344
FT /note="Proton acceptor"
FT /evidence="ECO:0000305"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00924"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00924"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00924"
FT BINDING 294
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00924"
FT BINDING 294
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00924"
FT BINDING 319
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00924"
FT BINDING 319
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00924"
FT BINDING 371..374
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00924"
FT BINDING 395
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00924"
FT VAR_SEQ 1..2
FT /note="MP -> MFVPFTSAAHSLTSLIRGGGQPSKSNLSGQRMP (in isoform
FT c)"
FT /evidence="ECO:0000305"
FT /id="VSP_020148"
SQ SEQUENCE 434 AA; 46617 MW; DB45F18B26799F68 CRC64;
MPITKIHARQ IYDSRGNPTV EVDLFTEKGV FRAAVPSGAS TGVHEALELR DGDKAVHLGK
GVLKAVSNIN EKIAPALIAK GFDVTAQKDI DDFMMALDGS ENKGNLGANA ILGVSLAVAK
AGAVHKGLPL YKYIAELAGT GKVVLPVPAF NVINGGSHAG NKLAMQEFMI LPVGASSFAE
AMRMGSEVYH HLKAEIKKRY GLDATAVGDE GGFAPNIQDN KEGLDLLNTA IDKAGYTGKI
SIGMDVAASE FFKDGKYDLD FKNPASDSSK WLSGEQLTEL YQSFIKEYPV VSIEDAFDQD
DWDNWGKFHG ATSIQLVGDD LTVTNPKRIQ TAIDKKSCNC LLLKVNQIGS VTESIEAAKL
SRANGWGVMV SHRSGETEDT FIADLVVGLA TGQIKTGAPC RSERLAKYNQ LLRIEEELGA
DAVYAGHNFR NPQV
