ID   ECI1_YEAST              Reviewed;         280 AA.
AC   Q05871; D6VYS8;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 168.
DE   RecName: Full=3,2-trans-enoyl-CoA isomerase;
DE            EC=5.3.3.8;
DE   AltName: Full=Delta(3),Delta(2)-enoyl-CoA isomerase;
DE            Short=D3,D2-enoyl-CoA isomerase;
DE   AltName: Full=Dodecenoyl-CoA isomerase;
GN   Name=ECI1; OrderedLocusNames=YLR284C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP   INDUCTION.
RX   PubMed=9837886; DOI=10.1074/jbc.273.50.33184;
RA   Geisbrecht B.V., Zhu D., Schulz K., Nau K., Morrell J.C., Geraghty M.T.,
RA   Schulz H., Erdmann R., Gould S.J.;
RT   "Molecular characterization of Saccharomyces cerevisiae Delta3, Delta2-
RT   enoyl-CoA isomerase.";
RL   J. Biol. Chem. 273:33184-33191(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH DCI1.
RX   PubMed=10381339; DOI=10.1006/bbrc.1999.0860;
RA   Geisbrecht B.V., Schulz K., Nau K., Geraghty M.T., Schulz H., Erdmann R.,
RA   Gould S.J.;
RT   "Preliminary characterization of Yor180Cp: identification of a novel
RT   peroxisomal protein of Saccharomyces cerevisiae involved in fatty acid
RT   metabolism.";
RL   Biochem. Biophys. Res. Commun. 260:28-34(1999).
RN   [5]
RP   CRYSTALLIZATION, AND SUBUNIT.
RX   PubMed=10944342; DOI=10.1107/s0907444900006533;
RA   Mursula A.M., van Aalten D.M., Modis Y., Hiltunen J.K., Wierenga R.K.;
RT   "Crystallization and X-ray diffraction analysis of peroxisomal Delta3-
RT   Delta2-enoyl-CoA isomerase from Saccharomyces cerevisiae.";
RL   Acta Crystallogr. D 56:1020-1023(2000).
RN   [6]
RP   SUBCELLULAR LOCATION, AND DOMAIN.
RX   PubMed=11302517; DOI=10.1078/0171-9335-00144;
RA   Yang X., Purdue P.E., Lazarow P.B.;
RT   "Eci1p uses a PTS1 to enter peroxisomes: either its own or that of a
RT   partner, Dci1p.";
RL   Eur. J. Cell Biol. 80:126-138(2001).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS), MUTAGENESIS OF GLU-158, AND
RP   SUBUNIT.
RX   PubMed=11399063; DOI=10.1006/jmbi.2001.4671;
RA   Mursula A.M., van Aalten D.M., Hiltunen J.K., Wierenga R.K.;
RT   "The crystal structure of delta(3)-delta(2)-enoyl-CoA isomerase.";
RL   J. Mol. Biol. 309:845-853(2001).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND SUBUNIT.
RX   PubMed=14741345; DOI=10.1016/s0014-5793(03)01450-9;
RA   Mursula A.M., Hiltunen J.K., Wierenga R.K.;
RT   "Structural studies on delta(3)-delta(2)-enoyl-CoA isomerase: the variable
RT   mode of assembly of the trimeric disks of the crotonase superfamily.";
RL   FEBS Lett. 557:81-87(2004).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 1-268 IN COMPLEX WITH SUBSTRATE
RP   ANALOGS, AND ACTIVE SITE.
RX   PubMed=26527136; DOI=10.1107/s139900471501559x;
RA   Onwukwe G.U., Koski M.K., Pihko P., Schmitz W., Wierenga R.K.;
RT   "Structures of yeast peroxisomal (3),(2)-enoyl-CoA isomerase complexed with
RT   acyl-CoA substrate analogues: the importance of hydrogen-bond networks for
RT   the reactivity of the catalytic base and the oxyanion hole.";
RL   Acta Crystallogr. D 71:2178-2191(2015).
CC   -!- FUNCTION: Essential for the beta oxidation of unsaturated fatty acids.
CC       {ECO:0000269|PubMed:9837886}.
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;
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;
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC   -!- SUBUNIT: Homohexamer, dimer of trimers. Interacts with DCI1.
CC       {ECO:0000269|PubMed:10381339, ECO:0000269|PubMed:10944342,
CC       ECO:0000269|PubMed:11399063, ECO:0000269|PubMed:14741345}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:10381339,
CC       ECO:0000269|PubMed:11302517, ECO:0000269|PubMed:9837886}. Note=This
CC       location is DCI1 dependent.
CC   -!- INDUCTION: By oleate. {ECO:0000269|PubMed:9837886}.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; AF090442; AAC83700.1; -; Genomic_DNA.
DR   EMBL; U17243; AAB67329.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09594.1; -; Genomic_DNA.
DR   PIR; S50369; S50369.
DR   RefSeq; NP_013386.1; NM_001182171.1.
DR   PDB; 1HNO; X-ray; 2.50 A; A=1-280.
DR   PDB; 1HNU; X-ray; 2.15 A; A=1-280.
DR   PDB; 1K39; X-ray; 3.29 A; A/B/C=1-280.
DR   PDB; 1PJH; X-ray; 2.10 A; A/B/C=1-280.
DR   PDB; 4ZDB; X-ray; 2.14 A; A/B/C=1-280.
DR   PDB; 4ZDC; X-ray; 2.13 A; A/B/C=1-280.
DR   PDB; 4ZDD; X-ray; 3.00 A; A=1-280.
DR   PDB; 4ZDE; X-ray; 2.10 A; A/B/C=1-280.
DR   PDB; 4ZDF; X-ray; 1.81 A; A/B=1-268.
DR   PDBsum; 1HNO; -.
DR   PDBsum; 1HNU; -.
DR   PDBsum; 1K39; -.
DR   PDBsum; 1PJH; -.
DR   PDBsum; 4ZDB; -.
DR   PDBsum; 4ZDC; -.
DR   PDBsum; 4ZDD; -.
DR   PDBsum; 4ZDE; -.
DR   PDBsum; 4ZDF; -.
DR   AlphaFoldDB; Q05871; -.
DR   SMR; Q05871; -.
DR   BioGRID; 31549; 26.
DR   DIP; DIP-1692N; -.
DR   IntAct; Q05871; 4.
DR   MINT; Q05871; -.
DR   STRING; 4932.YLR284C; -.
DR   MaxQB; Q05871; -.
DR   PaxDb; 4932-YLR284C; -.
DR   PeptideAtlas; Q05871; -.
DR   EnsemblFungi; YLR284C_mRNA; YLR284C; YLR284C.
DR   GeneID; 850990; -.
DR   KEGG; sce:YLR284C; -.
DR   AGR; SGD:S000004274; -.
DR   SGD; S000004274; ECI1.
DR   VEuPathDB; FungiDB:YLR284C; -.
DR   eggNOG; KOG0016; Eukaryota.
DR   GeneTree; ENSGT00940000173631; -.
DR   HOGENOM; CLU_009834_6_2_1; -.
DR   InParanoid; Q05871; -.
DR   OMA; DVAWCSE; -.
DR   OrthoDB; 553487at2759; -.
DR   BioCyc; MetaCyc:YLR284C-MONOMER; -.
DR   BioCyc; YEAST:YLR284C-MONOMER; -.
DR   BRENDA; 5.3.3.8; 984.
DR   Reactome; R-SCE-390247; Beta-oxidation of very long chain fatty acids.
DR   Reactome; R-SCE-9033241; Peroxisomal protein import.
DR   UniPathway; UPA00659; -.
DR   BioGRID-ORCS; 850990; 0 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; Q05871; -.
DR   PRO; PR:Q05871; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; Q05871; Protein.
DR   GO; GO:0005782; C:peroxisomal matrix; IBA:GO_Central.
DR   GO; GO:0005777; C:peroxisome; IDA:SGD.
DR   GO; GO:0004165; F:delta(3)-delta(2)-enoyl-CoA isomerase activity; IDA:SGD.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IDA:SGD.
DR   CDD; cd06558; crotonase-like; 1.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR   PANTHER; PTHR43684; -; 1.
DR   PANTHER; PTHR43684:SF1; ENOYL-COA DELTA ISOMERASE 2; 1.
DR   Pfam; PF00378; ECH_1; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Fatty acid metabolism; Isomerase; Lipid metabolism;
KW   Peroxisome; Reference proteome.
FT   CHAIN           1..280
FT                   /note="3,2-trans-enoyl-CoA isomerase"
FT                   /id="PRO_0000109263"
FT   MOTIF           278..280
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        158
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000269|PubMed:26527136"
FT   BINDING         68..72
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:26527136,
FT                   ECO:0007744|PDB:4ZDB, ECO:0007744|PDB:4ZDC"
FT   BINDING         126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:26527136,
FT                   ECO:0007744|PDB:4ZDC"
FT   MUTAGEN         158
FT                   /note="E->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11399063"
FT   STRAND          11..16
FT                   /evidence="ECO:0007829|PDB:4ZDF"
FT   STRAND          19..24
FT                   /evidence="ECO:0007829|PDB:4ZDF"
FT   HELIX           27..29
FT                   /evidence="ECO:0007829|PDB:4ZDF"
FT   HELIX           35..50
FT                   /evidence="ECO:0007829|PDB:4ZDF"
FT   STRAND          56..60
FT                   /evidence="ECO:0007829|PDB:4ZDF"
FT   STRAND          65..67
FT                   /evidence="ECO:0007829|PDB:4ZDF"
FT   HELIX           73..75
FT                   /evidence="ECO:0007829|PDB:4ZDF"
FT   TURN            77..81
FT                   /evidence="ECO:0007829|PDB:1K39"
FT   STRAND          82..88
FT                   /evidence="ECO:0007829|PDB:4ZDB"
FT   HELIX           89..96
FT                   /evidence="ECO:0007829|PDB:4ZDF"
FT   HELIX           98..110
FT                   /evidence="ECO:0007829|PDB:4ZDF"
FT   STRAND          113..119
FT                   /evidence="ECO:0007829|PDB:4ZDF"
FT   HELIX           125..133
FT                   /evidence="ECO:0007829|PDB:4ZDF"
FT   STRAND          134..141
FT                   /evidence="ECO:0007829|PDB:4ZDF"
FT   STRAND          145..147
FT                   /evidence="ECO:0007829|PDB:4ZDF"
FT   HELIX           150..153
FT                   /evidence="ECO:0007829|PDB:4ZDF"
FT   HELIX           161..169
FT                   /evidence="ECO:0007829|PDB:4ZDF"
FT   HELIX           171..179
FT                   /evidence="ECO:0007829|PDB:4ZDF"
FT   HELIX           186..191
FT                   /evidence="ECO:0007829|PDB:4ZDF"
FT   STRAND          196..198
FT                   /evidence="ECO:0007829|PDB:4ZDF"
FT   HELIX           206..220
FT                   /evidence="ECO:0007829|PDB:4ZDF"
FT   TURN            221..223
FT                   /evidence="ECO:0007829|PDB:4ZDF"
FT   HELIX           226..237
FT                   /evidence="ECO:0007829|PDB:4ZDF"
FT   TURN            238..240
FT                   /evidence="ECO:0007829|PDB:4ZDF"
FT   HELIX           241..261
FT                   /evidence="ECO:0007829|PDB:4ZDF"
FT   TURN            263..266
FT                   /evidence="ECO:0007829|PDB:4ZDF"
SQ   SEQUENCE   280 AA;  31698 MW;  CDB72D157ABB845C CRC64;
     MSQEIRQNEK ISYRIEGPFF IIHLMNPDNL NALEGEDYIY LGELLELADR NRDVYFTIIQ
     SSGRFFSSGA DFKGIAKAQG DDTNKYPSET SKWVSNFVAR NVYVTDAFIK HSKVLICCLN
     GPAIGLSAAL VALCDIVYSI NDKVYLLYPF ANLGLITEGG TTVSLPLKFG TNTTYECLMF
     NKPFKYDIMC ENGFISKNFN MPSSNAEAFN AKVLEELREK VKGLYLPSCL GMKKLLKSNH
     IDAFNKANSV EVNESLKYWV DGEPLKRFRQ LGSKQRKHRL
//