ID   CACM_YEAST              Reviewed;         687 AA.
AC   P80235; D6VPN4;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 2.
DT   27-MAR-2024, entry version 190.
DE   RecName: Full=Putative mitochondrial carnitine O-acetyltransferase;
DE            EC=2.3.1.7;
GN   Name=YAT1; OrderedLocusNames=YAR035W;
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=DL-1;
RX   PubMed=8262985; DOI=10.1016/s0021-9258(19)74266-5;
RA   Schmalix W.A., Bandlow W.;
RT   "The ethanol-inducible YAT1 gene from yeast encodes a presumptive
RT   mitochondrial outer carnitine acetyltransferase.";
RL   J. Biol. Chem. 268:27428-27439(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RA   Bussey H., Keng T., Storms R.K., Vo D., Zhong W., Fortin N., Barton A.B.,
RA   Kaback D.B., Clark M.W.;
RT   "Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of the 52
RT   Kbp CDC15-FLO1-PHO11-YAR074 region.";
RL   Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA   Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA   Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA   Storms R.K.;
RT   "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
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).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 76625 / YPH499;
RX   PubMed=17761666; DOI=10.1074/mcp.m700098-mcp200;
RA   Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,
RA   van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
RT   "Profiling phosphoproteins of yeast mitochondria reveals a role of
RT   phosphorylation in assembly of the ATP synthase.";
RL   Mol. Cell. Proteomics 6:1896-1906(2007).
CC   -!- FUNCTION: Involved in the transfer of acetyl-CoA into mitochondria. May
CC       also be involved in the metabolism of acetate and of ethanol.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-carnitine + acetyl-CoA = CoA + O-acetyl-(R)-carnitine;
CC         Xref=Rhea:RHEA:21136, ChEBI:CHEBI:16347, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:57589; EC=2.3.1.7;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane
CC       protein; Intermembrane side.
CC   -!- INDUCTION: By ethanol and by acetate. Repressed by glucose, and to a
CC       lesser extent, by galactose. Derepressed by glycerol.
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase 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; X74553; CAA52647.1; -; Genomic_DNA.
DR   EMBL; L28920; AAC09495.1; -; Genomic_DNA.
DR   EMBL; BK006935; DAA07004.1; -; Genomic_DNA.
DR   PIR; S53485; S53485.
DR   RefSeq; NP_009420.1; NM_001178226.1.
DR   AlphaFoldDB; P80235; -.
DR   SMR; P80235; -.
DR   BioGRID; 31811; 42.
DR   DIP; DIP-3795N; -.
DR   IntAct; P80235; 11.
DR   MINT; P80235; -.
DR   STRING; 4932.YAR035W; -.
DR   iPTMnet; P80235; -.
DR   PaxDb; 4932-YAR035W; -.
DR   PeptideAtlas; P80235; -.
DR   EnsemblFungi; YAR035W_mRNA; YAR035W; YAR035W.
DR   GeneID; 851285; -.
DR   KEGG; sce:YAR035W; -.
DR   AGR; SGD:S000000080; -.
DR   SGD; S000000080; YAT1.
DR   VEuPathDB; FungiDB:YAR035W; -.
DR   eggNOG; KOG3719; Eukaryota.
DR   GeneTree; ENSGT01060000248556; -.
DR   HOGENOM; CLU_013513_4_0_1; -.
DR   InParanoid; P80235; -.
DR   OMA; HILVMRR; -.
DR   OrthoDB; 1429709at2759; -.
DR   BioCyc; YEAST:YAR035W-MONOMER; -.
DR   BioGRID-ORCS; 851285; 10 hits in 10 CRISPR screens.
DR   PRO; PR:P80235; -.
DR   Proteomes; UP000002311; Chromosome I.
DR   RNAct; P80235; Protein.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0004092; F:carnitine O-acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:0004095; F:carnitine O-palmitoyltransferase activity; ISS:SGD.
DR   GO; GO:0009437; P:carnitine metabolic process; IMP:SGD.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 3.30.559.70; Choline/Carnitine o-acyltransferase, domain 2; 1.
DR   InterPro; IPR000542; Carn_acyl_trans.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR039551; Cho/carn_acyl_trans.
DR   InterPro; IPR042231; Cho/carn_acyl_trans_2.
DR   PANTHER; PTHR22589; CARNITINE O-ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR22589:SF29; MITOCHONDRIAL CARNITINE O-ACETYLTRANSFERASE-RELATED; 1.
DR   Pfam; PF00755; Carn_acyltransf; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   PROSITE; PS00439; ACYLTRANSF_C_1; 1.
DR   PROSITE; PS00440; ACYLTRANSF_C_2; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Fatty acid metabolism; Lipid metabolism; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW   Reference proteome; Transferase; Transport.
FT   CHAIN           1..687
FT                   /note="Putative mitochondrial carnitine O-
FT                   acetyltransferase"
FT                   /id="PRO_0000210175"
FT   ACT_SITE        346
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         446..459
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         481
FT                   /ligand="(R)-carnitine"
FT                   /ligand_id="ChEBI:CHEBI:16347"
FT                   /evidence="ECO:0000250"
FT   BINDING         494
FT                   /ligand="(R)-carnitine"
FT                   /ligand_id="ChEBI:CHEBI:16347"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         517
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17761666"
FT   CONFLICT        25
FT                   /note="P -> T (in Ref. 1; CAA52647)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        392
FT                   /note="S -> SS (in Ref. 1; CAA52647)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        595..596
FT                   /note="SF -> AS (in Ref. 1; CAA52647)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        653
FT                   /note="A -> T (in Ref. 1; CAA52647)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        660
FT                   /note="T -> A (in Ref. 1; CAA52647)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   687 AA;  77766 MW;  F00B628893B8BB39 CRC64;
     MPNLKRLPIP PLQDTLNRYL ARVEPLQDER QNRRTRRTVL SAENLDALNT LHERLLEYDA
     RLAESNPESS YIEQFWYDAY LLYDATVVLN VNPYFQLQDD PTIKDTPETA AQGPYGAHTV
     QVRRAARLTT SILKFIRQIR HGTLRTDTVR GKTPLSMDQY ERLFGSSRIP PGPGEPSCHL
     QTDATSHHVV AMYRGQFYWF DVLDTRNEPI FATPEQLEWN LYSIIMDAES AGSGSAPFGV
     FTTESRRVWS NIRDYLFHAD DCTNWRNLKL IDSALFVVCL DDVAFAADQQ DELTRSMLCG
     TSTINLDPHQ HQPPLNVQTG TCLNRWYDKL QLIVTKNGKA GINFEHTGVD GHTVLRLATD
     IYTDSILSFA RGVTKNVVDI FSDDDGKPSS SSLASAAHSA NLITIPRKLE WRTDNFLQSS
     LHFAETRISD LISQYEFVNL DFSNYGASHI KTVFKCSPDA FVQQVFQVAY FALYGRFETV
     YEPAMTKAFQ NGRTEAIRSV TGQSKLFVKS LLDQDASDAT KIQLLHDACT AHSQITRECS
     QGLGQDRHLY ALYCLWNQWY KDKLELPPIF RDKSWTTMQN NVLSTSNCGN PCLKSFGFGP
     VTANGFGIGY IIRDHSVSVV VSSRHRQTAR FASLMEKSLL EIDRIFKRQQ ARAAKPAART
     TASANTKSED MKYLLSGYDY FDVSVSG
//