Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Peroxisomal 2,4-dienoyl-CoA reductase SPS19

Gene

SPS19

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Auxiliary enzyme of beta-oxidation. Participates in the degradation of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in peroxisome. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA. Dispensable for growth and sporulation on solid acetate and oleate media, but is essential for these processes to occur on petroselineate.

Catalytic activityi

Trans-2,3-didehydroacyl-CoA + NADP+ = trans,trans-2,3,4,5-tetradehydroacyl-CoA + NADPH.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi29 – 5325NADPBy similarityAdd
BLAST

GO - Molecular functioni

  • 2,4-dienoyl-CoA reductase (NADPH) activity Source: SGD

GO - Biological processi

  • ascospore formation Source: SGD
  • fatty acid catabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Sporulation

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciMetaCyc:YNL202W-MONOMER.
YEAST:YNL202W-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisomal 2,4-dienoyl-CoA reductase SPS19 (EC:1.3.1.34)
Alternative name(s):
Sporulation-specific protein SPX19
Gene namesi
Name:SPS19
Synonyms:SPX19
Ordered Locus Names:YNL202W
ORF Names:N1362
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL202W.
SGDiS000005146. SPS19.

Subcellular locationi

GO - Cellular componenti

  • peroxisomal matrix Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 292291Peroxisomal 2,4-dienoyl-CoA reductase SPS19PRO_0000054565Add
BLAST

Proteomic databases

MaxQBiP32573.
PaxDbiP32573.
PeptideAtlasiP32573.

Expressioni

Developmental stagei

Sequentially activated during the process of meiosis and spore formation.

Inductioni

By oleate. Transcription is regulated by the transcription factors PIP2, OAF1 and ADR1. Weakly induced during sporulation in diploid cells.3 Publications

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi35632. 5 interactions.
DIPiDIP-4294N.
MINTiMINT-516231.

Structurei

3D structure databases

ProteinModelPortaliP32573.
SMRiP32573. Positions 19-269.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi290 – 2923Microbody targeting signalSequence Analysis

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1028.
GeneTreeiENSGT00760000118868.
InParanoidiP32573.
KOiK13237.
OMAiINGACIT.
OrthoDBiEOG7CZKH4.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PRINTSiPR00081. GDHRDH.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P32573-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNTANTLDGK FVTEGSWRPD LFKGKVAFVT GGAGTICRVQ TEALVLLGCK
60 70 80 90 100
AAIVGRDQER TEQAAKGISQ LAKDKDAVLA IANVDVRNFE QVENAVKKTV
110 120 130 140 150
EKFGKIDFVI AGAAGNFVCD FANLSPNAFK SVVDIDLLGS FNTAKACLKE
160 170 180 190 200
LKKSKGSILF VSATFHYYGV PFQGHVGAAK AGIDALAKNL AVELGPLGIR
210 220 230 240 250
SNCIAPGAID NTEGLKRLAG KKYKEKALAK IPLQRLGSTR DIAESTVYIF
260 270 280 290
SPAASYVTGT VLVVDGGMWH LGTYFGHELY PEALIKSMTS KL
Length:292
Mass (Da):31,109
Last modified:January 23, 2007 - v4
Checksum:iC82D520B1F5969A8
GO

Sequence cautioni

The sequence AAA62403.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAT93138.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA55506.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA96103.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78898 Genomic DNA. Translation: CAA55506.1. Different initiation.
Z71479 Genomic DNA. Translation: CAA96103.1. Different initiation.
AY693119 Genomic DNA. Translation: AAT93138.1. Different initiation.
M90351 Genomic DNA. Translation: AAA62403.1. Different initiation.
BK006947 Genomic DNA. Translation: DAA10352.1.
PIRiS50729.
RefSeqiNP_014197.2. NM_001183040.1.

Genome annotation databases

EnsemblFungiiYNL202W; YNL202W; YNL202W.
GeneIDi855518.
KEGGisce:YNL202W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78898 Genomic DNA. Translation: CAA55506.1. Different initiation.
Z71479 Genomic DNA. Translation: CAA96103.1. Different initiation.
AY693119 Genomic DNA. Translation: AAT93138.1. Different initiation.
M90351 Genomic DNA. Translation: AAA62403.1. Different initiation.
BK006947 Genomic DNA. Translation: DAA10352.1.
PIRiS50729.
RefSeqiNP_014197.2. NM_001183040.1.

3D structure databases

ProteinModelPortaliP32573.
SMRiP32573. Positions 19-269.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35632. 5 interactions.
DIPiDIP-4294N.
MINTiMINT-516231.

Proteomic databases

MaxQBiP32573.
PaxDbiP32573.
PeptideAtlasiP32573.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL202W; YNL202W; YNL202W.
GeneIDi855518.
KEGGisce:YNL202W.

Organism-specific databases

EuPathDBiFungiDB:YNL202W.
SGDiS000005146. SPS19.

Phylogenomic databases

eggNOGiCOG1028.
GeneTreeiENSGT00760000118868.
InParanoidiP32573.
KOiK13237.
OMAiINGACIT.
OrthoDBiEOG7CZKH4.

Enzyme and pathway databases

BioCyciMetaCyc:YNL202W-MONOMER.
YEAST:YNL202W-MONOMER.

Miscellaneous databases

NextBioi979547.
PROiP32573.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PRINTSiPR00081. GDHRDH.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A 21.7 kb DNA segment on the left arm of yeast chromosome XIV carries WHI3, GCR2, SPX18, SPX19, an homologue to the heat shock gene SSB1 and 8 new open reading frames of unknown function."
    Jonniaux J.-L., Coster F., Purnelle B., Goffeau A.
    Yeast 10:1639-1645(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "Identification of a sporulation-specific promoter regulating divergent transcription of two novel sporulation genes in Saccharomyces cerevisiae."
    Coe J.G., Murray L.E., Dawes I.W.
    Mol. Gen. Genet. 244:661-672(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-260.
    Strain: ATCC 28684 / S14.
  6. "The Saccharomyces cerevisiae peroxisomal 2,4-dienoyl-CoA reductase is encoded by the oleate-inducible gene SPS19."
    Gurvitz A., Rottensteiner H., Kilpelaeinen S.H., Hartig A., Hiltunen J.K., Binder M., Dawes I.W., Hamilton B.
    J. Biol. Chem. 272:22140-22147(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-13, ENZYME ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, INDUCTION.
  7. "Regulation of the yeast SPS19 gene encoding peroxisomal 2,4-dienoyl-CoA reductase by the transcription factors Pip2p and Oaf1p: beta-oxidation is dispensable for Saccharomyces cerevisiae sporulation in acetate medium."
    Gurvitz A., Rottensteiner H., Hiltunen J.K., Binder M., Dawes I.W., Ruis H., Hamilton B.
    Mol. Microbiol. 26:675-685(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  8. "Adr1p-dependent regulation of the oleic acid-inducible yeast gene SPS19 encoding the peroxisomal beta-oxidation auxiliary enzyme 2,4-dienoyl-CoA reductase."
    Gurvitz A., Wabnegger L., Rottensteiner H., Dawes I.W., Hartig A., Ruis H., Hamilton B.
    Mol. Cell Biol. Res. Commun. 4:81-89(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  9. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSPS19_YEAST
AccessioniPrimary (citable) accession number: P32573
Secondary accession number(s): D6W0Y6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 122 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.