ENOG_CHICK
ID ENOG_CHICK Reviewed; 434 AA.
AC O57391;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Gamma-enolase;
DE EC=4.2.1.11;
DE AltName: Full=2-phospho-D-glycerate hydro-lyase;
DE AltName: Full=Neural enolase;
DE Short=NSE;
GN Name=ENO2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=9434147; DOI=10.1016/s0167-4781(97)00157-7;
RA Tanaka M., Taniguchi T., Ohkubo T., Nakashima K.;
RT "cDNA cloning and characterization of neuron-specific enolase from
RT chicken.";
RL Biochim. Biophys. Acta 1395:28-33(1998).
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.
CC -!- TISSUE SPECIFICITY: Expressed in the brain and, to much less but
CC significant extents, in the pituitary and adrenal glands.
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; AB004291; BAA24680.1; -; mRNA.
DR RefSeq; NP_990207.1; NM_204876.1.
DR AlphaFoldDB; O57391; -.
DR SMR; O57391; -.
DR BioGRID; 675967; 1.
DR IntAct; O57391; 1.
DR STRING; 9031.ENSGALP00000023398; -.
DR PaxDb; O57391; -.
DR PRIDE; O57391; -.
DR GeneID; 395689; -.
DR KEGG; gga:395689; -.
DR CTD; 2026; -.
DR VEuPathDB; HostDB:geneid_395689; -.
DR eggNOG; KOG2670; Eukaryota.
DR InParanoid; O57391; -.
DR OrthoDB; 773373at2759; -.
DR PhylomeDB; O57391; -.
DR Reactome; R-GGA-352875; Gluconeogenesis.
DR Reactome; R-GGA-352882; Glycolysis.
DR UniPathway; UPA00109; UER00187.
DR PRO; PR:O57391; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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 2: Evidence at transcript level;
KW Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..434
FT /note="Gamma-enolase"
FT /id="PRO_0000134115"
FT ACT_SITE 210
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 343
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 318
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 370..373
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 434 AA; 47308 MW; 359E32F78BACCE07 CRC64;
MAVERIHARE ILDSRGNPTV EVDLYTHKGM FRAAVPSGAS TGIYEALELR DNDKSRFLGK
GVLQAVDHIN STVAPAIVGS GLSVVDQEKI DNLMLEMDGT ENKSKFGANA ILGVSLAVCK
AGAAEKDVPL YRHIADLAGN SDLILPVPAF NVINGGSHAG NKLAMQEFMI LPVGAESFRD
AMRIGAEVYH NLKSVIKEKY GKDATNVGDE GGFAPNILEN SEALELLKEA IDKAGYTDKI
VIGMDVAASE FYRDGKYDLD FKSPDDPSRY ISADELGDLY QSFVRAYPVL SIEDPFDQDD
WEAWSKFTAN VGIQIVGDDL TVTNPKRIER AVEEKACNCL LLKVNQIGSV TEAIQACKLA
QENGWGVMVS HRSGETEDTF IADLVVALCT GQIKTGAPCR SERLAKYNQL MRIEEELGDE
ARFAGHNFRN PSVL
