ECI1_YEAST
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 03-AUG-2022, entry version 160.
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; 23.
DR DIP; DIP-1692N; -.
DR IntAct; Q05871; 4.
DR MINT; Q05871; -.
DR STRING; 4932.YLR284C; -.
DR MaxQB; Q05871; -.
DR PaxDb; Q05871; -.
DR PRIDE; Q05871; -.
DR EnsemblFungi; YLR284C_mRNA; YLR284C; YLR284C.
DR GeneID; 850990; -.
DR KEGG; sce:YLR284C; -.
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; LGTHLNQ; -.
DR BioCyc; MetaCyc:YLR284C-MON; -.
DR BioCyc; YEAST:YLR284C-MON; -.
DR BRENDA; 5.3.3.8; 984.
DR UniPathway; UPA00659; -.
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 InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF52096; SSF52096; 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
