ECHM_PONAB
ID ECHM_PONAB Reviewed; 290 AA.
AC Q5R646;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts unsaturated trans-2-enoyl-CoA species ((2E)-enoyl-
CC CoA) to the corresponding (3S)-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; CR860650; CAH92770.1; -; mRNA.
DR RefSeq; NP_001126615.1; NM_001133143.1.
DR AlphaFoldDB; Q5R646; -.
DR SMR; Q5R646; -.
DR STRING; 9601.ENSPPYP00000003261; -.
DR GeneID; 100173612; -.
DR KEGG; pon:100173612; -.
DR CTD; 1892; -.
DR eggNOG; KOG1680; Eukaryota.
DR InParanoid; Q5R646; -.
DR OrthoDB; 1221604at2759; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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; Phosphoprotein; 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_0000007413"
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 46
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30084"
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 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30084"
FT MOD_RES 115
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BH95"
FT MOD_RES 115
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BH95"
FT MOD_RES 118
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P30084"
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"
SQ SEQUENCE 290 AA; 31428 MW; 53636860E6592104 CRC64;
MATLRVLLSC VRGPLRPPVR CPAWRPFASG ANFEYIIAEK RGKNNTVGLI QLNRPKALNA
LCDGLIDELN QALKIFEEDP AVGAIVLTGG DKAFAAGADI KEMQNLSFQD CYSSKFLKHW
DHLTQIKKPV IAAVNGYAFG GGCELAMMCD IIYAGEKAQF AQPEILIGTI PGAGGTQRLT
RTVGKSLAME MVLTGDRISA QDAKQAGLVS KICPVETLVE EAIQCAEKIA SNSKIIAAMA
KESVNAAFEM TLAEGSKLEK KLFYSTFATN DRKEGMTAFV EKRKANFKDQ
