ID   ECH1_PONAB              Reviewed;         328 AA.
AC   Q5RFG0;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 79.
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;
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=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:Q62651}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q62651}.
CC       Peroxisome {ECO:0000250|UniProtKB:Q62651}.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; CR857198; CAH89497.1; -; mRNA.
DR   RefSeq; NP_001124647.1; NM_001131175.1.
DR   AlphaFoldDB; Q5RFG0; -.
DR   SMR; Q5RFG0; -.
DR   STRING; 9601.ENSPPYP00000011133; -.
DR   GeneID; 100171488; -.
DR   KEGG; pon:100171488; -.
DR   CTD; 1891; -.
DR   eggNOG; KOG1681; Eukaryota.
DR   InParanoid; Q5RFG0; -.
DR   OrthoDB; 1094098at2759; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Acetylation; Fatty acid metabolism; Isomerase; Lipid metabolism;
KW   Mitochondrion; Peroxisome; Phosphoprotein; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..26
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..328
FT                   /note="Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase,
FT                   mitochondrial"
FT                   /id="PRO_0000042945"
FT   MOTIF           326..328
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255"
FT   BINDING         116..120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P42126"
FT   BINDING         174
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P42126"
FT   SITE            197
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:P42126"
FT   SITE            205
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q62651"
FT   MOD_RES         231
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O35459"
FT   MOD_RES         268
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13011"
FT   MOD_RES         327
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13011"
SQ   SEQUENCE   328 AA;  35786 MW;  62E0C53808F8E054 CRC64;
     MAAGIVASRR LRDLLTRRLT ASNYPGLSIS LRLTGSPAQE EASGVALGEA PDHSYESLRV
     TSAQKHVLHV QLNRPNKRNA MNKVFWREMV ECFNKISRDA DCRAVVISGA GKMFTAGVDL
     MDMASDILQP KGDDVARISW YLRDIITRYQ ETFNVIEKCP KPVIAAVHGG CIGGGVDLVT
     ACDIRYCAQD AFFQVKEVDV GLAADVGTLQ RLPKVIGNQS LVNELAFTAR KMMADEALGS
     GLVSRVFPDK EVMLDAALAL AAEISSKSPV AVQSTKVNLL YSRDHSVAES LNYVASWNMS
     MLQTQDLMKS VQAATENKEL KSVTFSKL