ECH1_RAT
ID ECH1_RAT Reviewed; 327 AA.
AC Q62651;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial {ECO:0000305};
DE EC=5.3.3.- {ECO:0000269|PubMed:11278886, ECO:0000269|PubMed:9417087};
DE Flags: Precursor;
GN Name=Ech1 {ECO:0000312|RGD:69353};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=7558027; DOI=10.1006/geno.1995.1077;
RA Fitzpatrick D.R., Germain-Lee E., Valle D.;
RT "Isolation and characterization of rat and human cDNAs encoding a novel
RT putative peroxisomal enoyl-CoA hydratase.";
RL Genomics 27:457-466(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 185-210 AND 219-229, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
RN [4]
RP CHARACTERIZATION, CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=9417087; DOI=10.1074/jbc.273.1.349;
RA Filppula S.A., Yagi A.I., Kilpeleainen S.H., Novikov D., Fitzpatrick D.R.,
RA Vihinen M., Valle D., Hiltunen J.K.;
RT "Delta3,5-delta2,4-dienoyl-CoA isomerase from rat liver. Molecular
RT characterization.";
RL J. Biol. Chem. 273:349-355(1998).
RN [5]
RP SUBCELLULAR LOCATION, FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF ASP-176; GLU-196 AND ASP-204.
RX PubMed=11278886; DOI=10.1074/jbc.m011315200;
RA Zhang D., Liang X., He X.Y., Alipui O.D., Yang S.Y., Schulz H.;
RT "Delta 3,5,delta 2,4-dienoyl-CoA isomerase is a multifunctional isomerase.
RT A structural and mechanistic study.";
RL J. Biol. Chem. 276:13622-13627(2001).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), SEQUENCE REVISION TO 164, AND
RP SUBUNIT.
RX PubMed=9739087; DOI=10.1016/s0969-2126(98)00098-7;
RA Modis Y., Filppula S.A., Novikov D.K., Norledge B., Hiltunen J.K.,
RA Wierenga R.K.;
RT "The crystal structure of dienoyl-CoA isomerase at 1.5 A resolution reveals
RT the importance of aspartate and glutamate sidechains for catalysis.";
RL Structure 6:957-970(1998).
CC -!- FUNCTION: Isomerization of 3-trans,5-cis-dienoyl-CoA to 2-trans,4-
CC trans-dienoyl-CoA. {ECO:0000269|PubMed:11278886}.
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:0000269|PubMed:11278886};
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:0000269|PubMed:9417087};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=30 uM for 3,5-octadienoyl-CoA {ECO:0000269|PubMed:11278886};
CC Vmax=2450 umol/min/mg enzyme towards 3,5-octadienoyl-CoA
CC {ECO:0000269|PubMed:11278886};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000269|PubMed:11278886, ECO:0000269|PubMed:9417087}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:9739087}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11278886,
CC ECO:0000269|PubMed:9417087}. Peroxisome {ECO:0000269|PubMed:11278886,
CC ECO:0000269|PubMed:9417087}.
CC -!- TISSUE SPECIFICITY: Expressed in heart and liver (at protein level).
CC {ECO:0000269|PubMed:11278886, ECO:0000269|PubMed:9417087}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000305}.
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DR EMBL; U08976; AAA82008.1; -; mRNA.
DR EMBL; BC062226; AAH62226.1; -; mRNA.
DR PIR; A57626; A57626.
DR RefSeq; NP_072116.1; NM_022594.1.
DR PDB; 1DCI; X-ray; 1.50 A; A/B/C=54-327.
DR PDBsum; 1DCI; -.
DR AlphaFoldDB; Q62651; -.
DR SMR; Q62651; -.
DR BioGRID; 249110; 1.
DR IntAct; Q62651; 1.
DR MINT; Q62651; -.
DR STRING; 10116.ENSRNOP00000027537; -.
DR SwissLipids; SLP:000001100; -.
DR iPTMnet; Q62651; -.
DR PhosphoSitePlus; Q62651; -.
DR jPOST; Q62651; -.
DR PaxDb; Q62651; -.
DR PRIDE; Q62651; -.
DR Ensembl; ENSRNOT00000096349; ENSRNOP00000085027; ENSRNOG00000020308.
DR GeneID; 64526; -.
DR KEGG; rno:64526; -.
DR UCSC; RGD:69353; rat.
DR CTD; 1891; -.
DR RGD; 69353; Ech1.
DR eggNOG; KOG1681; Eukaryota.
DR GeneTree; ENSGT00940000159610; -.
DR HOGENOM; CLU_009834_7_0_1; -.
DR InParanoid; Q62651; -.
DR OMA; QYVAHVE; -.
DR OrthoDB; 1094098at2759; -.
DR PhylomeDB; Q62651; -.
DR TreeFam; TF314317; -.
DR BRENDA; 5.3.3.21; 5301.
DR Reactome; R-RNO-9033241; Peroxisomal protein import.
DR UniPathway; UPA00659; -.
DR EvolutionaryTrace; Q62651; -.
DR PRO; PR:Q62651; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020308; Expressed in heart and 19 other tissues.
DR Genevisible; Q62651; RN.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0051750; F:delta(3,5)-delta(2,4)-dienoyl-CoA isomerase activity; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing;
KW Fatty acid metabolism; Isomerase; Lipid metabolism; Mitochondrion;
KW Peroxisome; Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 34..327
FT /note="Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase,
FT mitochondrial"
FT /id="PRO_0000007419"
FT MOTIF 325..327
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 115..119
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P42126"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P42126"
FT SITE 196
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000305|PubMed:9417087"
FT SITE 204
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000305|PubMed:9417087"
FT MOD_RES 230
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:O35459"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13011"
FT MOD_RES 316
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:O35459"
FT MOD_RES 326
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13011"
FT MUTAGEN 176
FT /note="D->A,D: Strongly decreases dienoyl-CoA and trienoyl-
FT CoA isomerase activity."
FT /evidence="ECO:0000269|PubMed:11278886"
FT MUTAGEN 196
FT /note="E->D,Q: Strongly decreases dienoyl-CoA and trienoyl-
FT CoA isomerase activity."
FT /evidence="ECO:0000269|PubMed:11278886"
FT MUTAGEN 204
FT /note="D->A,N: Strongly decreases dienoyl-CoA and trienoyl-
FT CoA isomerase activity."
FT /evidence="ECO:0000269|PubMed:11278886"
FT CONFLICT 164
FT /note="A -> T (in Ref. 1; AAA82008)"
FT /evidence="ECO:0000305"
FT STRAND 55..63
FT /evidence="ECO:0007829|PDB:1DCI"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:1DCI"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:1DCI"
FT HELIX 82..96
FT /evidence="ECO:0007829|PDB:1DCI"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:1DCI"
FT HELIX 119..126
FT /evidence="ECO:0007829|PDB:1DCI"
FT HELIX 134..157
FT /evidence="ECO:0007829|PDB:1DCI"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:1DCI"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:1DCI"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:1DCI"
FT HELIX 173..178
FT /evidence="ECO:0007829|PDB:1DCI"
FT STRAND 181..187
FT /evidence="ECO:0007829|PDB:1DCI"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:1DCI"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:1DCI"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:1DCI"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:1DCI"
FT HELIX 218..227
FT /evidence="ECO:0007829|PDB:1DCI"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:1DCI"
FT HELIX 233..238
FT /evidence="ECO:0007829|PDB:1DCI"
FT STRAND 241..248
FT /evidence="ECO:0007829|PDB:1DCI"
FT HELIX 249..265
FT /evidence="ECO:0007829|PDB:1DCI"
FT HELIX 268..283
FT /evidence="ECO:0007829|PDB:1DCI"
FT HELIX 286..300
FT /evidence="ECO:0007829|PDB:1DCI"
FT HELIX 304..314
FT /evidence="ECO:0007829|PDB:1DCI"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:1DCI"
SQ SEQUENCE 327 AA; 36172 MW; 6FAE35D7D5F66BC2 CRC64;
MATAMTVSSK LLGLLMQQLR GTRQLYFNVS LRSLSSSAQE ASKRIPEEVS DHNYESIQVT
SAQKHVLHVQ LNRPEKRNAM NRAFWRELVE CFQKISKDSD CRAVVVSGAG KMFTSGIDLM
DMASDILQPP GDDVARIAWY LRDLISRYQK TFTVIEKCPK PVIAAIHGGC IGGGVDLISA
CDIRYCTQDA FFQVKEVDVG LAADVGTLQR LPKVIGNRSL VNELTFTARK MMADEALDSG
LVSRVFPDKD VMLNAAFALA ADISSKSPVA VQGSKINLIY SRDHSVDESL DYMATWNMSM
LQTQDIIKSV QAAMEKKDSK SITFSKL
