ECH1_DICDI
ID ECH1_DICDI Reviewed; 293 AA.
AC Q54SS0;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial {ECO:0000305};
DE EC=5.3.3.- {ECO:0000250|UniProtKB:Q62651};
DE Flags: Precursor;
GN Name=ech1; ORFNames=DDB_G0282261;
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: Isomerization of 3-trans,5-cis-dienoyl-CoA to 2-trans,4-
CC trans-dienoyl-CoA. {ECO:0000250|UniProtKB:Q62651}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3E,5Z)-octadienoyl-CoA = (2E,4E)-octadienoyl-CoA;
CC Xref=Rhea:RHEA:45244, ChEBI:CHEBI:62243, ChEBI:CHEBI:85108;
CC Evidence={ECO:0000250|UniProtKB:Q62651};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3E,5Z,8Z,11Z,14Z)-eicosapentaenoyl-CoA = (2E,4E,8Z,11Z,14Z)-
CC eicosapentaenoyl-CoA; Xref=Rhea:RHEA:45224, ChEBI:CHEBI:85090,
CC ChEBI:CHEBI:85091; Evidence={ECO:0000250|UniProtKB:Q62651};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000250|UniProtKB:Q62651}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q62651}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000046; EAL66336.1; -; Genomic_DNA.
DR RefSeq; XP_640315.1; XM_635223.1.
DR AlphaFoldDB; Q54SS0; -.
DR SMR; Q54SS0; -.
DR STRING; 44689.DDB0267015; -.
DR PaxDb; Q54SS0; -.
DR EnsemblProtists; EAL66336; EAL66336; DDB_G0282261.
DR GeneID; 8623491; -.
DR KEGG; ddi:DDB_G0282261; -.
DR dictyBase; DDB_G0282261; ech1.
DR eggNOG; KOG1681; Eukaryota.
DR HOGENOM; CLU_009834_7_0_1; -.
DR InParanoid; Q54SS0; -.
DR OMA; QYVAHVE; -.
DR PhylomeDB; Q54SS0; -.
DR Reactome; R-DDI-9033241; Peroxisomal protein import.
DR UniPathway; UPA00659; -.
DR PRO; PR:Q54SS0; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; ISS:dictyBase.
DR GO; GO:0051750; F:delta(3,5)-delta(2,4)-dienoyl-CoA isomerase activity; ISS:dictyBase.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.12.10; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR045002; Ech1-like.
DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR014748; Enoyl-CoA_hydra_C.
DR PANTHER; PTHR43149; PTHR43149; 1.
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; Isomerase; Lipid metabolism; Mitochondrion;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..293
FT /note="Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase,
FT mitochondrial"
FT /id="PRO_0000331593"
FT BINDING 84..88
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P42126"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P42126"
FT SITE 165
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P42126"
FT SITE 173
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q62651"
SQ SEQUENCE 293 AA; 32522 MW; BB90E83EBD0A9B46 CRC64;
MEGSLFFTNA TPSTSILKIT DYKYLRLEKN DSTFVAELVL CRPKQYNSMD DDFYNEFISI
YDEIQNDSKI RCVILRGEGK GLTAGLNLGK IAPLITGDSE VSQSQNNLDL FKMIRRWQAS
LDKINKCSKP TIALIHGACI GGGVDMITAC DIRLCSSDAK FSIRETKLSI IADLGTLQRI
SKIVGSGFAR ELALTGKDID AKTAERFNLV NHVYPDHDTL LSEGRKLALS IAQNSPLVVQ
ATKLTLNHAD DHTIDEGLYR VALQNAAFLK SDDLNESATS FFEKRQPIFK CNL
