PTE1_YEAST
ID PTE1_YEAST Reviewed; 349 AA.
AC P41903; D6VWJ4;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Peroxisomal acyl-coenzyme A thioester hydrolase 1;
DE EC=3.1.2.2 {ECO:0000269|PubMed:10092594};
DE AltName: Full=Peroxisomal long-chain acyl-CoA thioesterase 1;
GN Name=TES1; Synonyms=PTE1; OrderedLocusNames=YJR019C; ORFNames=J1456;
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=DH484;
RA Hani J., Stumpf G., Domdey H.;
RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=10092594; DOI=10.1074/jbc.274.14.9216;
RA Jones J.M., Nau K., Geraghty M.T., Erdmann R., Gould S.J.;
RT "Identification of peroxisomal acyl-CoA thioesterases in yeast and
RT humans.";
RL J. Biol. Chem. 274:9216-9223(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [4]
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).
CC -!- FUNCTION: Acyl-coenzyme A (acyl-CoA) thioesterases are a group of
CC enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty
CC acid and coenzyme A (CoASH), providing the potential to regulate
CC intracellular levels of acyl-CoAs, free fatty acids and CoASH.
CC Contributes to growth on fatty acids. {ECO:0000269|PubMed:10092594}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2;
CC Evidence={ECO:0000269|PubMed:10092594};
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:10092594}.
CC -!- INDUCTION: Up-regulated by oleic acid. {ECO:0000269|PubMed:10092594}.
CC -!- SIMILARITY: Belongs to the C/M/P thioester hydrolase family.
CC {ECO:0000305}.
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DR EMBL; X85972; CAA59960.1; -; Genomic_DNA.
DR EMBL; X87611; CAA60943.1; -; Genomic_DNA.
DR EMBL; AF124265; AAD27617.1; -; Genomic_DNA.
DR EMBL; Z49519; CAA89543.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08810.1; -; Genomic_DNA.
DR PIR; S52763; S52763.
DR RefSeq; NP_012553.3; NM_001181677.3.
DR PDB; 1TBU; X-ray; 2.20 A; A/B/C/D=1-118.
DR PDBsum; 1TBU; -.
DR AlphaFoldDB; P41903; -.
DR SMR; P41903; -.
DR BioGRID; 33774; 52.
DR DIP; DIP-4480N; -.
DR IntAct; P41903; 6.
DR MINT; P41903; -.
DR STRING; 4932.YJR019C; -.
DR iPTMnet; P41903; -.
DR MaxQB; P41903; -.
DR PaxDb; P41903; -.
DR PRIDE; P41903; -.
DR EnsemblFungi; YJR019C_mRNA; YJR019C; YJR019C.
DR GeneID; 853477; -.
DR KEGG; sce:YJR019C; -.
DR SGD; S000003780; TES1.
DR VEuPathDB; FungiDB:YJR019C; -.
DR eggNOG; KOG3016; Eukaryota.
DR GeneTree; ENSGT00390000004207; -.
DR HOGENOM; CLU_032690_2_0_1; -.
DR InParanoid; P41903; -.
DR OMA; SQVWFRT; -.
DR BioCyc; MetaCyc:YJR019C-MON; -.
DR BioCyc; YEAST:YJR019C-MON; -.
DR BRENDA; 3.1.2.2; 984.
DR BRENDA; 3.1.2.20; 984.
DR Reactome; R-SCE-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-SCE-2046106; alpha-linolenic acid (ALA) metabolism.
DR Reactome; R-SCE-389887; Beta-oxidation of pristanoyl-CoA.
DR Reactome; R-SCE-390247; Beta-oxidation of very long chain fatty acids.
DR Reactome; R-SCE-9033241; Peroxisomal protein import.
DR EvolutionaryTrace; P41903; -.
DR PRO; PR:P41903; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P41903; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005782; C:peroxisomal matrix; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IDA:SGD.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IDA:SGD.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IBA:GO_Central.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IMP:SGD.
DR GO; GO:0009062; P:fatty acid catabolic process; IBA:GO_Central.
DR GO; GO:0019395; P:fatty acid oxidation; IMP:SGD.
DR Gene3D; 2.40.160.210; -; 1.
DR InterPro; IPR042171; Acyl-CoA_hotdog.
DR InterPro; IPR003703; Acyl_CoA_thio.
DR InterPro; IPR025652; Acyl_CoA_thio_II_dom.
DR InterPro; IPR029069; HotDog_dom_sf.
DR PANTHER; PTHR11066; PTHR11066; 1.
DR Pfam; PF02551; Acyl_CoA_thio; 2.
DR SUPFAM; SSF54637; SSF54637; 2.
DR TIGRFAMs; TIGR00189; tesB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Peroxisome; Reference proteome; Serine esterase.
FT CHAIN 1..349
FT /note="Peroxisomal acyl-coenzyme A thioester hydrolase 1"
FT /id="PRO_0000202158"
FT MOTIF 347..349
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 259
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 282
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 333
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:1TBU"
FT STRAND 21..29
FT /evidence="ECO:0007829|PDB:1TBU"
FT HELIX 42..54
FT /evidence="ECO:0007829|PDB:1TBU"
FT STRAND 62..70
FT /evidence="ECO:0007829|PDB:1TBU"
FT STRAND 81..89
FT /evidence="ECO:0007829|PDB:1TBU"
FT STRAND 91..102
FT /evidence="ECO:0007829|PDB:1TBU"
FT STRAND 105..115
FT /evidence="ECO:0007829|PDB:1TBU"
SQ SEQUENCE 349 AA; 40260 MW; F1B5A51C9A46783E CRC64;
MSASKMAMSN LEKILELVPL SPTSFVTKYL PAAPVGSKGT FGGTLVSQSL LASLHTVPLN
FFPTSLHSYF IKGGDPRTKI TYHVQNLRNG RNFIHKQVSA YQHDKLIFTS MILFAVQRSK
EHDSLQHWET IPGLQGKQPD PHRYEEATSL FQKEVLDPQK LSRYASLSDR FQDATSMSKY
VDAFQYGVME YQFPKDMFYS ARHTDELDYF VKVRPPITTV EHAGDESSLH KHHPYRIPKS
ITPENDARYN YVAFAYLSDS YLLLTIPYFH NLPLYCHSFS VSLDHTIYFH QLPHVNNWIY
LKISNPRSHW DKHLVQGKYF DTQSGRIMAS VSQEGYVVYG SERDIRAKF
