CACM_YEAST
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 03-AUG-2022, entry version 183.
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}.
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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; 38.
DR DIP; DIP-3795N; -.
DR IntAct; P80235; 11.
DR MINT; P80235; -.
DR STRING; 4932.YAR035W; -.
DR iPTMnet; P80235; -.
DR PaxDb; P80235; -.
DR PRIDE; P80235; -.
DR EnsemblFungi; YAR035W_mRNA; YAR035W; YAR035W.
DR GeneID; 851285; -.
DR KEGG; sce:YAR035W; -.
DR SGD; S000000080; YAT1.
DR VEuPathDB; FungiDB:YAR035W; -.
DR eggNOG; KOG3719; Eukaryota.
DR GeneTree; ENSGT01050000244969; -.
DR HOGENOM; CLU_013513_4_0_1; -.
DR InParanoid; P80235; -.
DR OMA; HILVMRR; -.
DR BioCyc; YEAST:YAR035W-MON; -.
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; -; 1.
DR Gene3D; 3.30.559.70; -; 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; PTHR22589; 1.
DR Pfam; PF00755; Carn_acyltransf; 1.
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
