SPS19_YEAST
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 03-AUG-2022, entry version 165.
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; Evidence={ECO:0000305};
CC Sequence=AAT93138.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA55506.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA96103.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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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; 51.
DR DIP; DIP-4294N; -.
DR IntAct; P32573; 1.
DR STRING; 4932.YNL202W; -.
DR iPTMnet; P32573; -.
DR MaxQB; P32573; -.
DR PaxDb; P32573; -.
DR PRIDE; P32573; -.
DR EnsemblFungi; YNL202W_mRNA; YNL202W; YNL202W.
DR GeneID; 855518; -.
DR KEGG; sce:YNL202W; -.
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; GSICSAQ; -.
DR BioCyc; MetaCyc:YNL202W-MON; -.
DR BioCyc; YEAST:YNL202W-MON; -.
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 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:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
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 InterPro; IPR045017; DECR2-like.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43296; PTHR43296; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 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 BINDING 29..53
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
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
