FABD_YEAST
ID FABD_YEAST Reviewed; 360 AA.
AC Q12283; D6W2S6;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Malonyl CoA-acyl carrier protein transacylase, mitochondrial;
DE Short=MCT;
DE EC=2.3.1.39;
DE AltName: Full=Malonyl-CoA:ACP transferase;
DE Flags: Precursor;
GN Name=MCT1; OrderedLocusNames=YOR221C; ORFNames=YOR50-11;
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=8840505;
RX DOI=10.1002/(sici)1097-0061(199607)12:9<877::aid-yea969>3.0.co;2-s;
RA Galisson F., Dujon B.;
RT "Sequence and analysis of a 33 kb fragment from the right arm of chromosome
RT XV of the yeast Saccharomyces cerevisiae.";
RL Yeast 12:877-885(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 FUNCTION.
RX PubMed=9388293; DOI=10.1007/s002940050292;
RA Schneider R., Brors B., Buerger F., Camrath S., Weiss H.;
RT "Two genes of the putative mitochondrial fatty acid synthase in the genome
RT of Saccharomyces cerevisiae.";
RL Curr. Genet. 32:384-388(1997).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
CC -!- FUNCTION: Involved in biosynthesis of fatty acids in mitochondria.
CC {ECO:0000250, ECO:0000269|PubMed:9388293}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP];
CC Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449; EC=2.3.1.39;
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:16823961}.
CC -!- MISCELLANEOUS: Present with 1360 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the FabD family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA63184.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA99439.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X92441; CAA63184.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z75129; CAA99439.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BK006948; DAA10992.1; -; Genomic_DNA.
DR PIR; S60948; S60948.
DR RefSeq; NP_014864.4; NM_001183640.3.
DR AlphaFoldDB; Q12283; -.
DR SMR; Q12283; -.
DR BioGRID; 34615; 302.
DR DIP; DIP-4125N; -.
DR IntAct; Q12283; 5.
DR STRING; 4932.YOR221C; -.
DR MaxQB; Q12283; -.
DR PaxDb; Q12283; -.
DR PRIDE; Q12283; -.
DR EnsemblFungi; YOR221C_mRNA; YOR221C; YOR221C.
DR GeneID; 854396; -.
DR KEGG; sce:YOR221C; -.
DR SGD; S000005747; MCT1.
DR VEuPathDB; FungiDB:YOR221C; -.
DR eggNOG; KOG2926; Eukaryota.
DR HOGENOM; CLU_832050_0_0_1; -.
DR InParanoid; Q12283; -.
DR OMA; LRPIQEP; -.
DR BioCyc; MetaCyc:YOR221C-MON; -.
DR BioCyc; YEAST:YOR221C-MON; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q12283; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12283; protein.
DR GO; GO:0005739; C:mitochondrion; IMP:SGD.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IMP:SGD.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0006631; P:fatty acid metabolic process; IMP:SGD.
DR Gene3D; 3.40.366.10; -; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR SUPFAM; SSF52151; SSF52151; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Mitochondrion; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 25..360
FT /note="Malonyl CoA-acyl carrier protein transacylase,
FT mitochondrial"
FT /id="PRO_0000257811"
FT ACT_SITE 105
FT /evidence="ECO:0000250"
FT ACT_SITE 235
FT /evidence="ECO:0000250"
SQ SEQUENCE 360 AA; 40707 MW; F27DC450F367F240 CRC64;
MKLLTFPGQG TSISISILKA IIRNKSREFQ TILSQNGKES NDLLQYIFQN PSSPGSIAVC
SNLFYQLYQI LSNPSDPQDQ APKNMTKIDS PDKKDNEQCY LLGHSLGELT CLSVNSLFSL
KDLFDIANFR NKLMVTSTEK YLVAHNINRS NKFEMWALSS PRATDLPQEV QKLLNSPNLL
SSSQNTISVA NANSVKQCVV TGLVDDLESL RTELNLRFPR LRITELTNPY NIPFHNSTVL
RPVQEPLYDY IWDILKKNGT HTLMELNHPI IANLDGNISY YIHHALDRFV KCSSRTVQFT
MCYDTINSGT PVEIDKSICF GPGNVIYNLI RRNCPQVDTI EYTSLATIDA YHKAAEENKD
