ID   FABD_SCHPO              Reviewed;         318 AA.
AC   O13698;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 128.
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; ORFNames=SPAC11G7.05c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Involved in biosynthesis of fatty acids in mitochondria.
CC       {ECO:0000250}.
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:16823372}.
CC   -!- SIMILARITY: Belongs to the FabD family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB16210.1; -; Genomic_DNA.
DR   PIR; T37548; T37548.
DR   RefSeq; NP_594399.1; NM_001019822.2.
DR   AlphaFoldDB; O13698; -.
DR   SMR; O13698; -.
DR   BioGRID; 278158; 1.
DR   STRING; 284812.O13698; -.
DR   MaxQB; O13698; -.
DR   PaxDb; 4896-SPAC11G7-05c-1; -.
DR   EnsemblFungi; SPAC11G7.05c.1; SPAC11G7.05c.1:pep; SPAC11G7.05c.
DR   GeneID; 2541662; -.
DR   KEGG; spo:SPAC11G7.05c; -.
DR   PomBase; SPAC11G7.05c; mct1.
DR   VEuPathDB; FungiDB:SPAC11G7.05c; -.
DR   eggNOG; KOG2926; Eukaryota.
DR   HOGENOM; CLU_030558_0_1_1; -.
DR   InParanoid; O13698; -.
DR   OMA; LNKTQFT; -.
DR   PhylomeDB; O13698; -.
DR   Reactome; R-SPO-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR   UniPathway; UPA00094; -.
DR   PRO; PR:O13698; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR   GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR   Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   PANTHER; PTHR42681; MALONYL-COA-ACYL CARRIER PROTEIN TRANSACYLASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42681:SF1; MALONYL-COA-ACYL CARRIER PROTEIN TRANSACYLASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; Mitochondrion; Reference proteome;
KW   Transferase; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..318
FT                   /note="Malonyl CoA-acyl carrier protein transacylase,
FT                   mitochondrial"
FT                   /id="PRO_0000314111"
SQ   SEQUENCE   318 AA;  35602 MW;  C719BA7786333EE0 CRC64;
     MSAILFPGQG VDWKTWMQPY LENNIVQNTL KEAENVTEIE IRKYIVEAEA KSNLRQPITT
     IAQPAILACS IALLRAFPPF TKKFRFYVGH SLGEYSAFVA SQTLSFSSAL KLVQARAKAM
     SYASALCQNP TSMLAITLTS RFPTDNFLNT VYSAVQKYRL IDIANVNSDR QIVLSGDKKE
     LESITSTLSE LVRSLGKLRS NWLDVSGAFH SRYMLPARDS LKNALGETEF NISPELCYTD
     SGKRFLPIIS NVTAELYPAD EEDIRRQLLL QCFRPVLFKN CLKTVKSKYG ANLFYAYGPG
     TTMQSIAKQN GISTKSRP
//