ENOB_CHICK
ID ENOB_CHICK Reviewed; 434 AA.
AC P07322;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Beta-enolase;
DE EC=4.2.1.11 {ECO:0000250|UniProtKB:P15429};
DE AltName: Full=2-phospho-D-glycerate hydro-lyase;
DE AltName: Full=Phosphopyruvate hydratase;
GN Name=ENO3;
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 STRAIN=White leghorn; TISSUE=Muscle;
RX PubMed=7629021; DOI=10.1093/oxfordjournals.jbchem.a124743;
RA Tanaka M., Maeda K., Nakashima K.;
RT "Chicken alpha-enolase but not beta-enolase has a Src-dependent tyrosine-
RT phosphorylation site: cDNA cloning and nucleotide sequence analysis.";
RL J. Biochem. 117:554-559(1995).
RN [2]
RP PROTEIN SEQUENCE OF 2-434.
RX PubMed=3539098; DOI=10.1042/bj2360115;
RA Russell G.A., Dunbar B., Fothergill-Gilmore L.A.;
RT "The complete amino acid sequence of chicken skeletal-muscle enolase.";
RL Biochem. J. 236:115-126(1986).
RN [3]
RP ACETYLATION AT SER-2.
RX PubMed=2898218; DOI=10.1016/0003-2697(88)90277-1;
RA Gibson B.W., Daley D.J., Williams D.H.;
RT "Structural elucidation of N-terminal post-translational modifications by
RT mass spectrometry: application to chicken enolase and the alpha- and beta-
RT subunits of bovine mitochondrial F1-ATPase.";
RL Anal. Biochem. 169:217-226(1988).
CC -!- FUNCTION: Glycolytic enzyme that catalyzes the conversion of 2-
CC phosphoglycerate to phosphoenolpyruvate.
CC {ECO:0000250|UniProtKB:P15429}.
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:P15429};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10165;
CC Evidence={ECO:0000250|UniProtKB:P15429};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Mg(2+) is required for catalysis and for stabilizing the dimer.;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5. {ECO:0000250|UniProtKB:P15429}.
CC -!- SUBUNIT: Homodimer. Interacts with PNKD (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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; D37901; BAA07133.1; -; mRNA.
DR PIR; A23850; A23850.
DR PIR; JC4187; JC4187.
DR RefSeq; NP_990450.1; NM_205119.1.
DR AlphaFoldDB; P07322; -.
DR SMR; P07322; -.
DR Allergome; 11939; Gal d 9.
DR Allergome; 11940; Gal d 9.0101.
DR iPTMnet; P07322; -.
DR PRIDE; P07322; -.
DR GeneID; 396016; -.
DR CTD; 2027; -.
DR VEuPathDB; HostDB:geneid_396017; -.
DR InParanoid; P07322; -.
DR PhylomeDB; P07322; -.
DR Reactome; R-GGA-352875; Gluconeogenesis.
DR Reactome; R-GGA-352882; Glycolysis.
DR UniPathway; UPA00109; UER00187.
DR PRO; PR:P07322; -.
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 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Glycolysis; Lyase;
KW Magnesium; Metal-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2898218,
FT ECO:0000269|PubMed:3539098"
FT CHAIN 2..434
FT /note="Beta-enolase"
FT /id="PRO_0000134111"
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"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:2898218"
FT CONFLICT 17
FT /note="E -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="P -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="M -> V (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 119..120
FT /note="CK -> SH (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="G -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="H -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 266..267
FT /note="HT -> DP (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="Y -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="F -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="T -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="G -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="K -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 394..395
FT /note="KT -> EQ (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 434 AA; 47196 MW; 892D1BE4B6342F44 CRC64;
MSIQKIHARE ILDSRGEPTV EVDLHTAKGH FRAAVPSGAS TGIHEALEPR DGDKKRFLGK
GVLKAVEHIN KTIGPALIEK KISVVEQEKI DKVMIEMDGT ENKSKFGANA ILGVSLAVCK
AGAAEKGVPL YRHIADLAGN TELILPVPAF NVINGGSHAG NKLAMQEFMV LPVGAASFHD
AMRVGAEVYH SLKGVIKAKY GKDATNVGGE GGFAPNILDN HEALELLKAA IAQAGYTDKV
VIGMDVAASE FCRDGRYHLD FKSPPHTKRY ITGEQLGEIY RGFIKDYPVV SIEDPFDQDD
WEAWKRFVFH VDIQVVGDDL TVTNPKRIAH GAEQHACNCL LLKVNQIGSV TESIQACKLA
QSHGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEALGDK
AKFAGRKFRN PKAK
