ID DCI1_YEAST Reviewed; 271 AA. AC Q08558; D6W2N6; DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 146. DE RecName: Full=Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase {ECO:0000303|PubMed:10455114}; DE EC=5.3.3.21 {ECO:0000269|PubMed:10455114}; DE AltName: Full=Peroxisomal di-isomerase DCI1 {ECO:0000303|PubMed:10455114}; GN Name=DCI1 {ECO:0000303|PubMed:10455114}; Synonyms=ECI2, EHD2; GN OrderedLocusNames=YOR180C; 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 [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169874; RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."; RL Nature 387:98-102(1997). RN [2] 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 [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [4] RP INDUCTION. RX PubMed=9774671; DOI=10.1128/mcb.18.11.6560; RA Karpichev I.V., Small G.M.; RT "Global regulatory functions of Oaf1p and Pip2p (Oaf2p), transcription RT factors that regulate genes encoding peroxisomal proteins in Saccharomyces RT cerevisiae."; RL Mol. Cell. Biol. 18:6560-6570(1998). RN [5] RP SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH ECI1. 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 [6] RP INDUCTION, SUBCELLULAR LOCATION, FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=10455114; DOI=10.1074/jbc.274.35.24514; RA Gurvitz A., Mursula A.M., Yagi A.I., Hartig A., Ruis H., Rottensteiner H., RA Hiltunen J.K.; RT "Alternatives to the isomerase-dependent pathway for the beta-oxidation of RT oleic acid are dispensable in Saccharomyces cerevisiae. Identification of RT YOR180c/DCI1 encoding peroxisomal delta(3,5)-delta(2,4)-dienoyl-CoA RT isomerase."; RL J. Biol. Chem. 274:24514-24521(1999). RN [7] RP INDUCTION, SUBCELLULAR LOCATION, AND DOMAIN. RX PubMed=10639339; DOI=10.1242/jcs.113.3.533; RA Karpichev I.V., Small G.M.; RT "Evidence for a novel pathway for the targeting of a Saccharomyces RT cerevisiae peroxisomal protein belonging to the isomerase/hydratase RT family."; RL J. Cell Sci. 113:533-544(2000). RN [8] RP FUNCTION, 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 [9] RP INDUCTION. RX PubMed=12429834; DOI=10.1091/mbc.e01-12-0149; RA Palkova Z., Devaux F., Icicova M., Minarikova L., Le Crom S., Jacq C.; RT "Ammonia pulses and metabolic oscillations guide yeast colony RT development."; RL Mol. Biol. Cell 13:3901-3914(2002). CC -!- FUNCTION: Peroxisomal di-isomerase that is involved in fatty acid CC metabolism enzyme by converting 3,5-dienoyl-CoAs to the corresponding CC 2,4-dienoyl-CoAs (PubMed:10381339, PubMed:10455114). Required for ECI1 CC to be locazed to the peroxisome (PubMed:10381339, PubMed:11302517). CC {ECO:0000269|PubMed:10381339, ECO:0000269|PubMed:10455114, CC ECO:0000269|PubMed:11302517}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a (3E,5Z)-dienoyl-CoA = a (2E,4E)-(5,6-saturated)-dienoyl-CoA; CC Xref=Rhea:RHEA:45240, ChEBI:CHEBI:85110, ChEBI:CHEBI:85111; CC EC=5.3.3.21; Evidence={ECO:0000269|PubMed:10455114}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45241; CC Evidence={ECO:0000269|PubMed:10455114}; CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation. CC {ECO:0000269|PubMed:10455114}. CC -!- SUBUNIT: Interacts with ECI1. {ECO:0000269|PubMed:10381339}. CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:10381339, CC ECO:0000269|PubMed:10455114, ECO:0000269|PubMed:10639339}. CC -!- INDUCTION: By oleate, through the binding of the OAF1-PIP2 CC transcriptional activator complex to its promoter ORE element. CC Expression is also induced during ammonia pulses in yeast colonies, at CC the beginning of detectable ammonia production. CC {ECO:0000269|PubMed:10455114, ECO:0000269|PubMed:10639339, CC ECO:0000269|PubMed:12429834, ECO:0000269|PubMed:9774671}. CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z75088; CAA99389.1; -; Genomic_DNA. DR EMBL; AY558432; AAS56758.1; -; Genomic_DNA. DR EMBL; BK006948; DAA10952.1; -; Genomic_DNA. DR PIR; S67072; S67072. DR RefSeq; NP_014823.3; NM_001183599.3. DR AlphaFoldDB; Q08558; -. DR SMR; Q08558; -. DR BioGRID; 34575; 70. DR DIP; DIP-4132N; -. DR IntAct; Q08558; 2. DR MINT; Q08558; -. DR STRING; 4932.YOR180C; -. DR PaxDb; 4932-YOR180C; -. DR PeptideAtlas; Q08558; -. DR EnsemblFungi; YOR180C_mRNA; YOR180C; YOR180C. DR GeneID; 854352; -. DR KEGG; sce:YOR180C; -. DR AGR; SGD:S000005706; -. DR SGD; S000005706; DCI1. DR VEuPathDB; FungiDB:YOR180C; -. DR eggNOG; KOG0016; Eukaryota. DR GeneTree; ENSGT00940000173631; -. DR HOGENOM; CLU_009834_6_2_1; -. DR InParanoid; Q08558; -. DR OMA; GMARCRI; -. DR OrthoDB; 553487at2759; -. DR BioCyc; MetaCyc:YOR180C-MONOMER; -. DR BioCyc; YEAST:YOR180C-MONOMER; -. DR UniPathway; UPA00659; -. DR BioGRID-ORCS; 854352; 0 hits in 10 CRISPR screens. DR PRO; PR:Q08558; -. DR Proteomes; UP000002311; Chromosome XV. DR RNAct; Q08558; Protein. DR GO; GO:0005737; C:cytoplasm; HDA:SGD. DR GO; GO:0005782; C:peroxisomal matrix; IDA:SGD. DR GO; GO:0004165; F:delta(3)-delta(2)-enoyl-CoA isomerase activity; IDA:SGD. DR GO; GO:0051750; F:delta(3,5)-delta(2,4)-dienoyl-CoA isomerase activity; IEA:RHEA. DR GO; GO:0006635; P:fatty acid beta-oxidation; IMP: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 Fatty acid metabolism; Isomerase; Lipid metabolism; Peroxisome; KW Reference proteome. FT CHAIN 1..271 FT /note="Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase" FT /id="PRO_0000232996" FT MOTIF 269..271 FT /note="Peroxisome targeting signal (PTS1)" FT /evidence="ECO:0000269|PubMed:10639339, FT ECO:0000269|PubMed:11302517" FT ACT_SITE 152 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000250|UniProtKB:Q05871" FT BINDING 62..66 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q05871" FT BINDING 120 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q05871" SQ SEQUENCE 271 AA; 30058 MW; 0AA0BF3A981F733F CRC64; MSSRVCYHIN GPFFIIKLID PKHLNSLTFE DFVYIALLLH KANDIDSVLF TVLQSSGKYF SSGGKFSAVN KLNDGDVTSE VEKVSKLVSA ISSPNIFVAN AFAIHKKVLV CCLNGPAIGL SASLVALCDI VYSQNDSVFL LFPFSNLGFV AEVGTSVTLT QKLGINSANE HMIFSTPVLF KELIGTIITK NYQLTNTETF NEKVLQDIKQ NLEGLYPKSV LGMKELLHSE MKQKLIKAQA METNGTLPFW ASGEPFKRFK QLQEGNRRHK L //