ECI1_RAT
ID ECI1_RAT Reviewed; 289 AA.
AC P23965;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Enoyl-CoA delta isomerase 1, mitochondrial {ECO:0000305};
DE Short=MECI {ECO:0000303|PubMed:11781327};
DE EC=5.3.3.8 {ECO:0000269|PubMed:11781327, ECO:0000269|PubMed:8218206};
DE AltName: Full=3,2-trans-enoyl-CoA isomerase {ECO:0000303|PubMed:8218206};
DE AltName: Full=Delta(3),Delta(2)-enoyl-CoA isomerase {ECO:0000303|PubMed:11781327};
DE Short=D3,D2-enoyl-CoA isomerase {ECO:0000303|PubMed:11781327};
DE AltName: Full=Dodecenoyl-CoA isomerase;
DE Flags: Precursor;
GN Name=Eci1 {ECO:0000312|RGD:61892}; Synonyms=Dci;
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], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=1958319; DOI=10.1515/bchm3.1991.372.2.613;
RA Mueller-Newen G., Stoffel W.;
RT "Mitochondrial 3-2trans-Enoyl-CoA isomerase. Purification, cloning,
RT expression, and mitochondrial import of the key enzyme of unsaturated fatty
RT acid beta-oxidation.";
RL Biol. Chem. Hoppe-Seyler 372:613-624(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=2040594; DOI=10.1016/s0021-9258(18)99081-2;
RA Palosaari P.M., Vihinen M., Maentsaelae P.I., Alexson S.E.,
RA Pihlajaniemi T., Hiltunen J.K.;
RT "Amino acid sequence similarities of the mitochondrial short chain delta 3,
RT delta 2-enoyl-CoA isomerase and peroxisomal multifunctional delta 3, delta
RT 2-enoyl-CoA isomerase, 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA
RT dehydrogenase enzyme in rat liver. The proposed occurrence of isomerization
RT and hydration in the same catalytic domain of the multifunctional enzyme.";
RL J. Biol. Chem. 266:10750-10753(1991).
RN [3]
RP MUTAGENESIS OF GLU-165, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8218206; DOI=10.1021/bi00093a018;
RA Mueller-Newen G., Stoffel W.;
RT "Site-directed mutagenesis of putative active-site amino acid residues of
RT 3,2-trans-enoyl-CoA isomerase, conserved within the low-homology
RT isomerase/hydratase enzyme family.";
RL Biochemistry 32:11405-11412(1993).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11781327; DOI=10.1074/jbc.m112228200;
RA Zhang D., Yu W., Geisbrecht B.V., Gould S.J., Sprecher H., Schulz H.;
RT "Functional characterization of delta3,delta2-enoyl-CoA isomerases from rat
RT liver.";
RL J. Biol. Chem. 277:9127-9132(2002).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 29-289, AND SUBUNIT.
RX PubMed=15883186; DOI=10.1110/ps.041303705;
RA Hubbard P.A., Yu W., Schulz H., Kim J.-J.P.;
RT "Domain swapping in the low-similarity isomerase/hydratase superfamily: the
RT crystal structure of rat mitochondrial delta3, delta2-enoyl-CoA
RT isomerase.";
RL Protein Sci. 14:1545-1555(2005).
CC -!- FUNCTION: Able to isomerize both 3-cis and 3-trans double bonds into
CC the 2-trans form in a range of enoyl-CoA species.
CC {ECO:0000269|PubMed:11781327, ECO:0000269|PubMed:8218206}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3Z)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA;
CC Xref=Rhea:RHEA:45900, ChEBI:CHEBI:85097, ChEBI:CHEBI:85489;
CC EC=5.3.3.8; Evidence={ECO:0000269|PubMed:8218206};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45901;
CC Evidence={ECO:0000305|PubMed:8218206};
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:0000269|PubMed:8218206};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45229;
CC Evidence={ECO:0000305|PubMed:8218206};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3Z)-octenoyl-CoA = (2E)-octenoyl-CoA; Xref=Rhea:RHEA:46044,
CC ChEBI:CHEBI:62242, ChEBI:CHEBI:85640;
CC Evidence={ECO:0000269|PubMed:11781327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46045;
CC Evidence={ECO:0000269|PubMed:11781327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-tetradecenoyl-CoA = (3Z)-tetradecenoyl-CoA;
CC Xref=Rhea:RHEA:29847, ChEBI:CHEBI:61405, ChEBI:CHEBI:61968;
CC Evidence={ECO:0000269|PubMed:11781327};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29849;
CC Evidence={ECO:0000269|PubMed:11781327};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=470 uM for (3Z)-hexenoyl-CoA {ECO:0000269|PubMed:11781327};
CC KM=190 uM for (3Z)-octenoyl-CoA {ECO:0000269|PubMed:11781327};
CC KM=48 uM for (3Z)-tetradecenoyl-CoA {ECO:0000269|PubMed:11781327};
CC KM=240 uM for (3E)-hexenoyl-CoA {ECO:0000269|PubMed:11781327};
CC KM=150 uM for (3E)-octenoyl-CoA {ECO:0000269|PubMed:11781327};
CC KM=57 uM for (3E)-tetradecenoyl-CoA {ECO:0000269|PubMed:11781327};
CC Note=kcat are 270 sec(-1), 25 sec(-1), 20 sec(-1), 200 sec(-1), 180
CC sec(-1) and 98 sec(-1) for (3Z)-hexenoyl-CoA, (3Z)-octenoyl-CoA,
CC (3Z)-tetradecenoyl-CoA, (3E)-hexenoyl-CoA, (3E)-octenoyl-CoA and
CC (3E)-tetradecenoyl-CoA, respectively. {ECO:0000269|PubMed:11781327};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000269|PubMed:11781327, ECO:0000269|PubMed:8218206}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:15883186}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:11781327}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000305}.
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DR EMBL; X61184; CAA43488.1; -; mRNA.
DR EMBL; M61112; AAA41073.1; -; mRNA.
DR PIR; S17161; S17161.
DR PDB; 1XX4; X-ray; 2.20 A; A=29-289.
DR PDBsum; 1XX4; -.
DR AlphaFoldDB; P23965; -.
DR SMR; P23965; -.
DR IntAct; P23965; 1.
DR STRING; 10116.ENSRNOP00000011784; -.
DR SwissLipids; SLP:000001593; -.
DR iPTMnet; P23965; -.
DR PhosphoSitePlus; P23965; -.
DR jPOST; P23965; -.
DR PaxDb; P23965; -.
DR PRIDE; P23965; -.
DR UCSC; RGD:61892; rat.
DR RGD; 61892; Eci1.
DR eggNOG; KOG1683; Eukaryota.
DR InParanoid; P23965; -.
DR PhylomeDB; P23965; -.
DR BRENDA; 5.3.3.8; 5301.
DR Reactome; R-RNO-77288; mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
DR SABIO-RK; P23965; -.
DR UniPathway; UPA00659; -.
DR EvolutionaryTrace; P23965; -.
DR PRO; PR:P23965; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0004165; F:delta(3)-delta(2)-enoyl-CoA isomerase activity; IDA:UniProtKB.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IDA:RGD.
DR GO; GO:0016863; F:intramolecular oxidoreductase activity, transposing C=C bonds; IDA:UniProtKB.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IDA:UniProtKB.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
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 Reference proteome; Transit peptide.
FT TRANSIT 1..28
FT /note="Mitochondrion"
FT CHAIN 29..289
FT /note="Enoyl-CoA delta isomerase 1, mitochondrial"
FT /id="PRO_0000007422"
FT BINDING 93..97
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P42126"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P42126"
FT BINDING 164
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 MOD_RES 48
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P42125"
FT MOD_RES 48
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P42125"
FT MOD_RES 71
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P42125"
FT MOD_RES 76
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P42126"
FT MOD_RES 222
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P42125"
FT MOD_RES 222
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P42125"
FT MOD_RES 229
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P42125"
FT MOD_RES 229
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P42125"
FT MOD_RES 255
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P42125"
FT MOD_RES 255
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P42125"
FT MOD_RES 275
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P42125"
FT MOD_RES 283
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P42125"
FT MOD_RES 283
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P42125"
FT MUTAGEN 165
FT /note="E->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:8218206"
FT CONFLICT 1..8
FT /note="MALAAARR -> AGCCAC (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="D -> N (in Ref. 2; AAA41073)"
FT /evidence="ECO:0000305"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:1XX4"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:1XX4"
FT TURN 52..55
FT /evidence="ECO:0007829|PDB:1XX4"
FT HELIX 59..74
FT /evidence="ECO:0007829|PDB:1XX4"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:1XX4"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:1XX4"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:1XX4"
FT HELIX 105..123
FT /evidence="ECO:0007829|PDB:1XX4"
FT STRAND 126..133
FT /evidence="ECO:0007829|PDB:1XX4"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:1XX4"
FT HELIX 139..147
FT /evidence="ECO:0007829|PDB:1XX4"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:1XX4"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:1XX4"
FT HELIX 174..184
FT /evidence="ECO:0007829|PDB:1XX4"
FT HELIX 186..195
FT /evidence="ECO:0007829|PDB:1XX4"
FT HELIX 201..206
FT /evidence="ECO:0007829|PDB:1XX4"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:1XX4"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:1XX4"
FT HELIX 219..230
FT /evidence="ECO:0007829|PDB:1XX4"
FT HELIX 235..254
FT /evidence="ECO:0007829|PDB:1XX4"
FT HELIX 257..269
FT /evidence="ECO:0007829|PDB:1XX4"
FT HELIX 271..282
FT /evidence="ECO:0007829|PDB:1XX4"
SQ SEQUENCE 289 AA; 32254 MW; 79D2CED09DD8FDC6 CRC64;
MALAAARRVL LQAGSRLGRR GAVDGARRFS NKRVLVEKEG EAGIAVMKFK NPPVNSLSLE
FLTEFVISLE KLENDKSIRG VILTSERPGI FSAGLDLMEM YGRNPAHYAE YWKAVQELWL
RLYLSNLTLI SAINGASPAG GCLMALTCDY RIMADNSKYT IGLNESLLGI VAPFWLKDNY
VNTIGHRAAE RALQLGTLFP PAEALKVGLV DEVVPEDQVH SKARSVMAKW FTIPDHSRQL
TKSMMRKATA DNLIKQREAD IQNFTSFISR DSIQKSLHVY LEKLKQKKG
