ID SPS19_YEAST Reviewed; 292 AA. AC P32573; D6W0Y6; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 27-MAR-2024, entry version 172. DE RecName: Full=Peroxisomal 2,4-dienoyl-CoA reductase SPS19 [(3E)-enoyl-CoA-producing]; DE EC=1.3.1.124 {ECO:0000269|PubMed:9268358}; DE AltName: Full=Sporulation-specific protein SPX19; GN Name=SPS19; Synonyms=SPX19; OrderedLocusNames=YNL202W; ORFNames=N1362; 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]. RC STRAIN=ATCC 96604 / S288c / FY1679; RX PubMed=7725799; DOI=10.1002/yea.320101213; RA Jonniaux J.-L., Coster F., Purnelle B., Goffeau A.; RT "A 21.7 kb DNA segment on the left arm of yeast chromosome XIV carries RT WHI3, GCR2, SPX18, SPX19, an homologue to the heat shock gene SSB1 and 8 RT new open reading frames of unknown function."; RL Yeast 10:1639-1645(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169873; RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F., RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its RT evolutionary implications."; RL Nature 387:93-98(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 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 [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-260. RC STRAIN=ATCC 28684 / S14; RX PubMed=7969036; DOI=10.1007/bf00282757; RA Coe J.G., Murray L.E., Dawes I.W.; RT "Identification of a sporulation-specific promoter regulating divergent RT transcription of two novel sporulation genes in Saccharomyces cerevisiae."; RL Mol. Gen. Genet. 244:661-672(1994). RN [6] RP PROTEIN SEQUENCE OF 2-13, ENZYME ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, RP AND INDUCTION. RX PubMed=9268358; DOI=10.1074/jbc.272.35.22140; RA Gurvitz A., Rottensteiner H., Kilpelaeinen S.H., Hartig A., Hiltunen J.K., RA Binder M., Dawes I.W., Hamilton B.; RT "The Saccharomyces cerevisiae peroxisomal 2,4-dienoyl-CoA reductase is RT encoded by the oleate-inducible gene SPS19."; RL J. Biol. Chem. 272:22140-22147(1997). RN [7] RP INDUCTION. RX PubMed=9427398; DOI=10.1046/j.1365-2958.1997.5931969.x; RA Gurvitz A., Rottensteiner H., Hiltunen J.K., Binder M., Dawes I.W., RA Ruis H., Hamilton B.; RT "Regulation of the yeast SPS19 gene encoding peroxisomal 2,4-dienoyl-CoA RT reductase by the transcription factors Pip2p and Oaf1p: beta-oxidation is RT dispensable for Saccharomyces cerevisiae sporulation in acetate medium."; RL Mol. Microbiol. 26:675-685(1997). RN [8] RP INDUCTION. RX PubMed=11170837; DOI=10.1006/mcbr.2000.0261; RA Gurvitz A., Wabnegger L., Rottensteiner H., Dawes I.W., Hartig A., Ruis H., RA Hamilton B.; RT "Adr1p-dependent regulation of the oleic acid-inducible yeast gene SPS19 RT encoding the peroxisomal beta-oxidation auxiliary enzyme 2,4-dienoyl-CoA RT reductase."; RL Mol. Cell Biol. Res. Commun. 4:81-89(2000). RN [9] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-188, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22106047; DOI=10.1002/pmic.201100166; RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.; RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae."; RL Proteomics 12:236-240(2012). CC -!- FUNCTION: Auxiliary enzyme of beta-oxidation. Participates in the CC degradation of unsaturated fatty enoyl-CoA esters having double bonds CC in both even- and odd-numbered positions in peroxisome. Catalyzes the CC NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA. CC Dispensable for growth and sporulation on solid acetate and oleate CC media, but is essential for these processes to occur on petroselineate. CC -!- CATALYTIC ACTIVITY: CC Reaction=a (2E,4Z)-dienoyl-CoA + H(+) + NADPH = a 4,5-saturated-(3E)- CC enoyl-CoA + NADP(+); Xref=Rhea:RHEA:61892, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:85099, CC ChEBI:CHEBI:85493; EC=1.3.1.124; CC Evidence={ECO:0000269|PubMed:9268358}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a (2E,4E)-dienoyl-CoA + H(+) + NADPH = a 4,5-saturated-(3E)- CC enoyl-CoA + NADP(+); Xref=Rhea:RHEA:45912, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:85101, CC ChEBI:CHEBI:85493; EC=1.3.1.124; CC Evidence={ECO:0000269|PubMed:9268358}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9268358}. CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:9268358}. CC -!- DEVELOPMENTAL STAGE: Sequentially activated during the process of CC meiosis and spore formation. CC -!- INDUCTION: By oleate. Transcription is regulated by the transcription CC factors PIP2, OAF1 and ADR1. Weakly induced during sporulation in CC diploid cells. {ECO:0000269|PubMed:11170837, CC ECO:0000269|PubMed:9268358, ECO:0000269|PubMed:9427398}. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) CC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA62403.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAT93138.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=CAA55506.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=CAA96103.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; X78898; CAA55506.1; ALT_INIT; Genomic_DNA. DR EMBL; Z71479; CAA96103.1; ALT_INIT; Genomic_DNA. DR EMBL; AY693119; AAT93138.1; ALT_INIT; Genomic_DNA. DR EMBL; M90351; AAA62403.1; ALT_INIT; Genomic_DNA. DR EMBL; BK006947; DAA10352.1; -; Genomic_DNA. DR PIR; S50729; S50729. DR RefSeq; NP_014197.2; NM_001183040.1. DR AlphaFoldDB; P32573; -. DR SMR; P32573; -. DR BioGRID; 35632; 52. DR DIP; DIP-4294N; -. DR IntAct; P32573; 1. DR STRING; 4932.YNL202W; -. DR iPTMnet; P32573; -. DR MaxQB; P32573; -. DR PaxDb; 4932-YNL202W; -. DR PeptideAtlas; P32573; -. DR EnsemblFungi; YNL202W_mRNA; YNL202W; YNL202W. DR GeneID; 855518; -. DR KEGG; sce:YNL202W; -. DR AGR; SGD:S000005146; -. DR SGD; S000005146; SPS19. DR VEuPathDB; FungiDB:YNL202W; -. DR eggNOG; KOG0725; Eukaryota. DR GeneTree; ENSGT00940000153801; -. DR HOGENOM; CLU_010194_1_2_1; -. DR InParanoid; P32573; -. DR OMA; GNHAYSA; -. DR OrthoDB; 2092693at2759; -. DR BioCyc; MetaCyc:YNL202W-MONOMER; -. DR BioCyc; YEAST:YNL202W-MONOMER; -. DR BRENDA; 1.3.1.124; 984. DR Reactome; R-SCE-390247; Beta-oxidation of very long chain fatty acids. DR Reactome; R-SCE-9033241; Peroxisomal protein import. DR BioGRID-ORCS; 855518; 3 hits in 10 CRISPR screens. DR PRO; PR:P32573; -. DR Proteomes; UP000002311; Chromosome XIV. DR RNAct; P32573; Protein. DR GO; GO:0005782; C:peroxisomal matrix; IDA:SGD. DR GO; GO:0005777; C:peroxisome; IBA:GO_Central. DR GO; GO:0008670; F:2,4-dienoyl-CoA reductase (NADPH) activity; IDA:SGD. DR GO; GO:0030437; P:ascospore formation; IMP:SGD. DR GO; GO:0009062; P:fatty acid catabolic process; IDA:SGD. DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central. DR CDD; cd05369; TER_DECR_SDR_a; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR045017; DECR2-like. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR002347; SDR_fam. DR PANTHER; PTHR43296; PEROXISOMAL 2,4-DIENOYL-COA REDUCTASE; 1. DR PANTHER; PTHR43296:SF2; PEROXISOMAL 2,4-DIENOYL-COA REDUCTASE [(3E)-ENOYL-COA-PRODUCING]; 1. DR Pfam; PF13561; adh_short_C2; 1. DR PRINTS; PR00081; GDHRDH. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Isopeptide bond; NADP; Oxidoreductase; KW Peroxisome; Reference proteome; Sporulation; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:9268358" FT CHAIN 2..292 FT /note="Peroxisomal 2,4-dienoyl-CoA reductase SPS19 [(3E)- FT enoyl-CoA-producing]" FT /id="PRO_0000054565" FT MOTIF 290..292 FT /note="Microbody targeting signal" FT /evidence="ECO:0000255" FT ACT_SITE 162 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:O93868" FT ACT_SITE 180 FT /note="Lowers pKa of active site Tyr" FT /evidence="ECO:0000250|UniProtKB:O93868" FT BINDING 36 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:L0E2Z4" FT BINDING 85 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:L0E2Z4" FT BINDING 145 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:L0E2Z4" FT BINDING 180 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:O93868" FT BINDING 209 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:O93868" FT CROSSLNK 188 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0007744|PubMed:22106047" SQ SEQUENCE 292 AA; 31109 MW; C82D520B1F5969A8 CRC64; MNTANTLDGK FVTEGSWRPD LFKGKVAFVT GGAGTICRVQ TEALVLLGCK AAIVGRDQER TEQAAKGISQ LAKDKDAVLA IANVDVRNFE QVENAVKKTV EKFGKIDFVI AGAAGNFVCD FANLSPNAFK SVVDIDLLGS FNTAKACLKE LKKSKGSILF VSATFHYYGV PFQGHVGAAK AGIDALAKNL AVELGPLGIR SNCIAPGAID NTEGLKRLAG KKYKEKALAK IPLQRLGSTR DIAESTVYIF SPAASYVTGT VLVVDGGMWH LGTYFGHELY PEALIKSMTS KL //