ECHM_BOVIN
ID ECHM_BOVIN Reviewed; 290 AA.
AC Q58DM8; Q2TBV2; Q4PS76;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Enoyl-CoA hydratase, mitochondrial;
DE Short=mECH;
DE Short=mECH1;
DE EC=4.2.1.17 {ECO:0000250|UniProtKB:P30084};
DE EC=5.3.3.8 {ECO:0000250|UniProtKB:P14604};
DE AltName: Full=Enoyl-CoA hydratase 1;
DE Short=ECHS1;
DE AltName: Full=Short-chain enoyl-CoA hydratase;
DE Short=SCEH;
DE Flags: Precursor;
GN Name=ECHS1;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA Ferretti L., Uboldi C., Del Vecchio I., Eggen A., Brunner R., Iannuzzi L.;
RT "Comparative mapping of the bovine SPRN locus.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts unsaturated trans-2-enoyl-CoA species ((2E)-enoyl-
CC CoA) to the corresponding 3(S)-3-hydroxyacyl-CoA species through
CC addition of a water molecule to the double bond. Catalyzes the
CC hydration of medium- and short-chained fatty enoyl-CoA thioesters from
CC 4 carbons long (C4) up to C16 (By similarity). Has high substrate
CC specificity for crotonyl-CoA ((2E)-butenoyl-CoA) and moderate
CC specificity for acryloyl-CoA, 3-methylcrotonyl-CoA (3-methyl-(2E)-
CC butenoyl-CoA) and methacrylyl-CoA ((2E)-2-methylpropenoyl-CoA). Can
CC bind tiglyl-CoA (2-methylcrotonoyl-CoA), but hydrates only a small
CC amount of this substrate (By similarity). Plays a key role in the beta-
CC oxidation spiral of short- and medium-chain fatty acid oxidation. At a
CC lower rate than the hydratase reaction, catalyzes the isomerase
CC reaction of trans-3-enoyl-CoA species (such as (3E)-hexenoyl-CoA) to
CC trans-2-enoyl-CoA species (such as (2E)-hexenoyl-CoA), which are
CC subsequently hydrated to 3(S)-3-hydroxyacyl-CoA species (such as (3S)-
CC hydroxyhexanoyl-CoA) (By similarity). {ECO:0000250|UniProtKB:P14604,
CC ECO:0000250|UniProtKB:P30084}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O;
CC Xref=Rhea:RHEA:16105, ChEBI:CHEBI:15377, ChEBI:CHEBI:57318,
CC ChEBI:CHEBI:58856; EC=4.2.1.17;
CC Evidence={ECO:0000250|UniProtKB:P30084};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16107;
CC Evidence={ECO:0000250|UniProtKB:P30084};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3E)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA;
CC Xref=Rhea:RHEA:45228, ChEBI:CHEBI:58521, ChEBI:CHEBI:85097;
CC EC=5.3.3.8; Evidence={ECO:0000250|UniProtKB:P14604};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45229;
CC Evidence={ECO:0000250|UniProtKB:P14604};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3E)-hexenoyl-CoA = (2E)-hexenoyl-CoA; Xref=Rhea:RHEA:45736,
CC ChEBI:CHEBI:62077, ChEBI:CHEBI:84790;
CC Evidence={ECO:0000250|UniProtKB:P14604};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45737;
CC Evidence={ECO:0000250|UniProtKB:P14604};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-3-hydroxybutanoyl-CoA = (2E)-butenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:26558, ChEBI:CHEBI:15377, ChEBI:CHEBI:57316,
CC ChEBI:CHEBI:57332; Evidence={ECO:0000250|UniProtKB:P30084};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:26560;
CC Evidence={ECO:0000250|UniProtKB:P30084};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxyisovaleryl-CoA = 3-methyl-(2E)-butenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:31079, ChEBI:CHEBI:15377, ChEBI:CHEBI:57344,
CC ChEBI:CHEBI:62555; Evidence={ECO:0000250|UniProtKB:P30084};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31081;
CC Evidence={ECO:0000250|UniProtKB:P30084};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxypropanoyl-CoA = acryloyl-CoA + H2O;
CC Xref=Rhea:RHEA:26518, ChEBI:CHEBI:15377, ChEBI:CHEBI:57367,
CC ChEBI:CHEBI:58528; Evidence={ECO:0000250|UniProtKB:P30084};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:26520;
CC Evidence={ECO:0000250|UniProtKB:P30084};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxybutanoyl-CoA = (2E)-butenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:45584, ChEBI:CHEBI:15377, ChEBI:CHEBI:57332,
CC ChEBI:CHEBI:78611; Evidence={ECO:0000250|UniProtKB:P30084};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:45586;
CC Evidence={ECO:0000250|UniProtKB:P30084};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-2-methylpropenoyl-CoA + H2O = (S)-3-hydroxyisobutanoyl-
CC CoA; Xref=Rhea:RHEA:31175, ChEBI:CHEBI:15377, ChEBI:CHEBI:62500,
CC ChEBI:CHEBI:62611; Evidence={ECO:0000250|UniProtKB:P30084};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31176;
CC Evidence={ECO:0000250|UniProtKB:P30084};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxyhexanoyl-CoA = (2E)-hexenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:30547, ChEBI:CHEBI:15377, ChEBI:CHEBI:62075,
CC ChEBI:CHEBI:62077; Evidence={ECO:0000250|UniProtKB:P14604};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:30549;
CC Evidence={ECO:0000250|UniProtKB:P14604};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxydecanoyl-CoA = (2E)-decenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:31191, ChEBI:CHEBI:15377, ChEBI:CHEBI:61406,
CC ChEBI:CHEBI:62616; Evidence={ECO:0000250|UniProtKB:P14604};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31193;
CC Evidence={ECO:0000250|UniProtKB:P14604};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000250|UniProtKB:P30084}.
CC -!- SUBUNIT: Homohexamer; dimer of trimers. {ECO:0000250|UniProtKB:P14604}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P14604}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000305}.
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DR EMBL; DQ058610; AAY83884.1; -; mRNA.
DR EMBL; DQ058603; AAY83878.1; -; Genomic_DNA.
DR EMBL; BT021569; AAX46416.1; -; mRNA.
DR EMBL; BC109605; AAI09606.1; -; mRNA.
DR RefSeq; NP_001020377.2; NM_001025206.2.
DR AlphaFoldDB; Q58DM8; -.
DR SMR; Q58DM8; -.
DR STRING; 9913.ENSBTAP00000042386; -.
DR PaxDb; Q58DM8; -.
DR PeptideAtlas; Q58DM8; -.
DR PRIDE; Q58DM8; -.
DR Ensembl; ENSBTAT00000044947; ENSBTAP00000042386; ENSBTAG00000017710.
DR GeneID; 281748; -.
DR KEGG; bta:281748; -.
DR CTD; 1892; -.
DR VEuPathDB; HostDB:ENSBTAG00000017710; -.
DR VGNC; VGNC:28308; ECHS1.
DR eggNOG; KOG1680; Eukaryota.
DR GeneTree; ENSGT00940000157609; -.
DR HOGENOM; CLU_009834_7_6_1; -.
DR InParanoid; Q58DM8; -.
DR OMA; IFKQTDA; -.
DR OrthoDB; 1221604at2759; -.
DR TreeFam; TF314497; -.
DR BioCyc; MetaCyc:MON-11697; -.
DR SABIO-RK; Q58DM8; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000009136; Chromosome 26.
DR Bgee; ENSBTAG00000017710; Expressed in liver and 105 other tissues.
DR ExpressionAtlas; Q58DM8; baseline.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0043956; F:3-hydroxypropionyl-CoA dehydratase activity; IEA:RHEA.
DR GO; GO:0120092; F:crotonyl-CoA hydratase activity; IEA:RHEA.
DR GO; GO:0004165; F:delta(3)-delta(2)-enoyl-CoA isomerase activity; IEA:RHEA.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; ISS:UniProtKB.
DR GO; GO:0006635; P:fatty acid beta-oxidation; ISS:UniProtKB.
DR Gene3D; 1.10.12.10; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR014748; Enoyl-CoA_hydra_C.
DR Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF52096; SSF52096; 1.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Fatty acid metabolism; Isomerase; Lipid metabolism; Lyase;
KW Mitochondrion; Reference proteome; Transit peptide.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 28..290
FT /note="Enoyl-CoA hydratase, mitochondrial"
FT /id="PRO_0000007410"
FT BINDING 98..101
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 164
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT MOD_RES 101
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BH95"
FT MOD_RES 101
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BH95"
FT MOD_RES 204
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BH95"
FT MOD_RES 211
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BH95"
FT CONFLICT 198
FT /note="I -> N (in Ref. 3; AAI09606)"
FT /evidence="ECO:0000305"
FT CONFLICT 269..277
FT /note="TEDRKEGMA -> PKTGRKAWP (in Ref. 1; AAY83884)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 290 AA; 31243 MW; 30CAD9F7314AD50F CRC64;
MAALRALLPR VRAPLRPWLF CPVQRSFASS AAFEYIITAK KGRNSNVGLI QLNRPKALNA
LCNGLIVELN QALQAFEEDP AVGAIVLTGG EKVFAAGADI KEMQSLTFQN CYSGGFLSHW
DQLTRVKKPV IAAVNGYALG GGCELAMMCD IIYAGEKAQF GQPEILIGTI PGAGGTQRLT
RAVGKSLAME MVLTGDRISA QDAKQAGLVS KIFPVETVVE EAIQCAEKIA SNSKIVTAMA
KESVNAAFEM TLAEGVKLEK KLFYSTFATE DRKEGMAAFV EKRKANFKDQ
