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Database: UniProt
Entry: E3H859_ILYPC
LinkDB: E3H859_ILYPC
Original site: E3H859_ILYPC 
ID   E3H859_ILYPC            Unreviewed;       301 AA.
AC   E3H859;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=Malonyl CoA-acyl carrier protein transacylase {ECO:0000256|PIRNR:PIRNR000446};
DE            EC=2.3.1.39 {ECO:0000256|PIRNR:PIRNR000446};
GN   OrderedLocusNames=Ilyop_1510 {ECO:0000313|EMBL:ADO83290.1};
OS   Ilyobacter polytropus (strain ATCC 51220 / DSM 2926 / LMG 16218 / CuHBu1).
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC   Ilyobacter.
OX   NCBI_TaxID=572544 {ECO:0000313|EMBL:ADO83290.1, ECO:0000313|Proteomes:UP000006875};
RN   [1] {ECO:0000313|EMBL:ADO83290.1, ECO:0000313|Proteomes:UP000006875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51220 / DSM 2926 / LMG 16218 / CuHBu1
RC   {ECO:0000313|Proteomes:UP000006875};
RX   PubMed=21304735; DOI=10.4056/sigs.1273360;
RA   Sikorski J., Chertkov O., Lapidus A., Nolan M., Lucas S., Del Rio T.G.,
RA   Tice H., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Brambilla E., Yasawong M.,
RA   Rohde M., Pukall R., Spring S., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Ilyobacter polytropus type strain (CuHbu1).";
RL   Stand. Genomic Sci. 3:304-314(2010).
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         Evidence={ECO:0000256|ARBA:ARBA00000936,
CC         ECO:0000256|PIRNR:PIRNR000446};
CC   -!- SIMILARITY: Belongs to the fabD family.
CC       {ECO:0000256|PIRNR:PIRNR000446}.
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DR   EMBL; CP002281; ADO83290.1; -; Genomic_DNA.
DR   RefSeq; WP_013387957.1; NC_014632.1.
DR   AlphaFoldDB; E3H859; -.
DR   STRING; 572544.Ilyop_1510; -.
DR   KEGG; ipo:Ilyop_1510; -.
DR   eggNOG; COG0331; Bacteria.
DR   HOGENOM; CLU_030558_0_1_0; -.
DR   OrthoDB; 9805460at2; -.
DR   Proteomes; UP000006875; Chromosome.
DR   GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
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; IPR024925; Malonyl_CoA-ACP_transAc.
DR   InterPro; IPR004410; Malonyl_CoA-ACP_transAc_FabD.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   NCBIfam; TIGR00128; fabD; 1.
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   PIRSF; PIRSF000446; Mct; 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 {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|PIRNR:PIRNR000446};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006875};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000446}.
FT   DOMAIN          7..298
FT                   /note="Malonyl-CoA:ACP transacylase (MAT)"
FT                   /evidence="ECO:0000259|SMART:SM00827"
FT   ACT_SITE        91
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000446-1"
FT   ACT_SITE        198
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000446-1"
SQ   SEQUENCE   301 AA;  32643 MW;  93EDD98CCD2D06C4 CRC64;
     MSKIAFVFPG QGAQYVGMGK DLYENNEIAK KYFDEIFENM EIDLKRVMFE GPEEDLKQTK
     YTQPAIVAMS LVLAKLMEEK GIKADYVAGH SVGEYAALGS GGYLSLEDAV KLTAFRGDTM
     NTVSQEVNGT MAAIIGMEAA KIEEVLAGVD GVVEAVNFNE PGQTVIAGSV AAIEKACEAL
     KAAGARRALI LSVSGPFHSS LMKPAGEKLK AEVENYEFKT GTAKLVANTT AEVTTDAEEI
     KKELYDQTFG PVRWVETVEK LKSEGVEKIY EIGPGKVLKG LIRKIDKTLV VENIEKLEDL
     A
//
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