ID A0A3Q1M0V5_BOVIN Unreviewed; 576 AA.
AC A0A3Q1M0V5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Beta-enolase {ECO:0000256|ARBA:ARBA00040232};
DE EC=4.2.1.11 {ECO:0000256|ARBA:ARBA00012058};
DE AltName: Full=2-phospho-D-glycerate hydro-lyase {ECO:0000256|ARBA:ARBA00031125};
DE AltName: Full=Enolase 3 {ECO:0000256|ARBA:ARBA00041942};
DE AltName: Full=Muscle-specific enolase {ECO:0000256|ARBA:ARBA00042698};
DE AltName: Full=Skeletal muscle enolase {ECO:0000256|ARBA:ARBA00042657};
GN Name=ENO3 {ECO:0000313|Ensembl:ENSBTAP00000063298.1,
GN ECO:0000313|VGNC:VGNC:28498};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000063298.1, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000063298.1, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000063298.1,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000063298.1}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000063298.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Glycolytic enzyme that catalyzes the conversion of 2-
CC phosphoglycerate to phosphoenolpyruvate. Appears to have a function in
CC striated muscle development and regeneration.
CC {ECO:0000256|ARBA:ARBA00037209}.
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:0000256|ARBA:ARBA00036172};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10165;
CC Evidence={ECO:0000256|ARBA:ARBA00036172};
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 AlphaFoldDB; A0A3Q1M0V5; -.
DR Ensembl; ENSBTAT00000072789.1; ENSBTAP00000063298.1; ENSBTAG00000005534.4.
DR VEuPathDB; HostDB:ENSBTAG00000005534; -.
DR VGNC; VGNC:28498; ENO3.
DR GeneTree; ENSGT00950000182805; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000005534; Expressed in biceps femoris and 106 other cell types or tissues.
DR ExpressionAtlas; A0A3Q1M0V5; 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:SF5; BETA-ENOLASE; 1.
DR PANTHER; PTHR11902; ENOLASE; 1.
DR Pfam; PF00113; Enolase_C; 1.
DR Pfam; PF03952; Enolase_N; 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:A0A3Q1M0V5};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136}.
FT DOMAIN 87..218
FT /note="Enolase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01193"
FT DOMAIN 226..505
FT /note="Enolase C-terminal TIM barrel"
FT /evidence="ECO:0000259|SMART:SM01192"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 576 AA; 62126 MW; 83EDC16DAB793FB2 CRC64;
MEGPAHVQPP FAPLPGQGPG HGLSPPSADR ARPQPSPSLR VQAGPVPRTV QASQYRDVDE
GLAGDGGPDG GRVLIAHDGC VLTAMAMQKI FAREILDSRG NPTVEVDLHT AKGRFRAAVP
SGASTGIYEA LELRDGDKSR YLGKGVLKAV EHINKTLGPA LLEKKLSVVD QEKVDKFMIE
LDGTENKSKF GANAILGVSL AVCKAGAAEK GVPLYRHIAD LAGNPELILP VPAFNVINGG
SHAGNKLAMQ EFMILPVGAS SFREAMRIGA EVYHHLKGVI KAKYGKDATN VGDEGGFAPN
ILENNEALEL LKTAIQAAGY PDKVVIGMDV AASEFYRNGK YDLDFKSPDD PARHISGEKL
GELYKNFIKN YPVVSIEDPF DQDDWATWTS FLSGVNIQIV GDDLTVTNPK RIAQAVEKKA
CNCLLLKVNQ IGSVTESIQA CKLAQSNGWG VMVSHRSGET EDTFIADLVV GLCTGQIKTG
APCRSERLAK YNQLMRYRGH SEPGHQELRA FGLEYHSPDH VCLPGLRRLL GTRLSLLDAS
SVTRRPSERL EAPGVHRTDL GLQALPPEIK HWCQPS
//
