ECHM_DICDI
ID ECHM_DICDI Reviewed; 277 AA.
AC Q1ZXF1;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Probable enoyl-CoA hydratase, mitochondrial {ECO:0000305};
DE EC=4.2.1.17 {ECO:0000250|UniProtKB:P30084};
DE AltName: Full=Enoyl-CoA hydratase 1;
DE AltName: Full=Short-chain enoyl-CoA hydratase;
DE Short=SCEH;
DE Flags: Precursor;
GN Name=echs1; ORFNames=DDB_G0285071;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Straight-chain enoyl-CoA thioesters from C4 up to at least
CC C16 are processed, although with decreasing catalytic rate.
CC {ECO:0000250|UniProtKB:P14604, 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 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O;
CC Xref=Rhea:RHEA:20724, ChEBI:CHEBI:15377, ChEBI:CHEBI:58521,
CC ChEBI:CHEBI:137480; EC=4.2.1.17;
CC Evidence={ECO:0000250|UniProtKB:P30084};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20726;
CC Evidence={ECO:0000250|UniProtKB:P30084};
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 -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC -!- SUBUNIT: Homohexamer; dimer of trimers. {ECO:0000250|UniProtKB:P14604}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P14604}.
CC -!- DOMAIN: The monomer is folded into a right-handed spiral of four turns,
CC followed by two small domains which are involved in trimerization.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000073; EAS66856.1; -; Genomic_DNA.
DR RefSeq; XP_001134539.1; XM_001134539.1.
DR AlphaFoldDB; Q1ZXF1; -.
DR SMR; Q1ZXF1; -.
DR STRING; 44689.DDB0232942; -.
DR PaxDb; Q1ZXF1; -.
DR EnsemblProtists; EAS66856; EAS66856; DDB_G0285071.
DR GeneID; 8624884; -.
DR KEGG; ddi:DDB_G0285071; -.
DR dictyBase; DDB_G0285071; echs1.
DR eggNOG; KOG1680; Eukaryota.
DR HOGENOM; CLU_009834_7_6_1; -.
DR InParanoid; Q1ZXF1; -.
DR OMA; IFKQTDA; -.
DR PhylomeDB; Q1ZXF1; -.
DR Reactome; R-DDI-70895; Branched-chain amino acid catabolism.
DR Reactome; R-DDI-77310; Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
DR Reactome; R-DDI-77346; Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
DR Reactome; R-DDI-77348; Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
DR Reactome; R-DDI-77350; Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
DR Reactome; R-DDI-77352; Beta oxidation of butanoyl-CoA to acetyl-CoA.
DR UniPathway; UPA00659; -.
DR PRO; PR:Q1ZXF1; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:dictyBase.
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:0004300; F:enoyl-CoA hydratase activity; IBA:GO_Central.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
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 3: Inferred from homology;
KW Fatty acid metabolism; Lipid metabolism; Lyase; Mitochondrion;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..42
FT /note="Mitochondrion"
FT CHAIN 43..277
FT /note="Probable enoyl-CoA hydratase, mitochondrial"
FT /id="PRO_0000331592"
FT BINDING 85..88
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 151
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 277 AA; 30187 MW; 69C207F4D78F792B CRC64;
MLKQVIKTVS SSQAPKKYFF KQFCTSTTEK KGRVGLVTLN RPKSLNALSD GLISEINSAV
KLFQEDKDVG SIIITGSEKA FAAGADIKEM EKVTLPDAYN NDLLAQWHDL TKIRKPIIAA
VNGYALGGGC ELAMMCDIII AGEKAVFGQP EIKLGTIPGC GGTQRLIRAI GKSKAMELVL
TGNNLTAVEA EKAGLVSKVV PVEELLTEAT KMAEKIASYS QLTVAMAKEA VNASYELTLQ
EGIRFERRMF HSTFGTHDQK EGMNAFVEKR TPTWHNK
