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Database: UniProt
Entry: W4EYY4_9BACL
LinkDB: W4EYY4_9BACL
Original site: W4EYY4_9BACL 
ID   W4EYY4_9BACL            Unreviewed;       320 AA.
AC   W4EYY4;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Malonyl CoA-acyl carrier protein transacylase {ECO:0000256|PIRNR:PIRNR000446};
DE            EC=2.3.1.39 {ECO:0000256|PIRNR:PIRNR000446};
GN   ORFNames=C176_10342 {ECO:0000313|EMBL:ETT85823.1};
OS   Viridibacillus arenosi FSL R5-213.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Viridibacillus.
OX   NCBI_TaxID=1227360 {ECO:0000313|EMBL:ETT85823.1, ECO:0000313|Proteomes:UP000019062};
RN   [1] {ECO:0000313|EMBL:ETT85823.1, ECO:0000313|Proteomes:UP000019062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL R5-213 {ECO:0000313|EMBL:ETT85823.1,
RC   ECO:0000313|Proteomes:UP000019062};
RX   PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA   Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA   den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT   "Genomic comparison of sporeforming bacilli isolated from milk.";
RL   BMC Genomics 15:26-26(2014).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ETT85823.1}.
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DR   EMBL; ASQA01000016; ETT85823.1; -; Genomic_DNA.
DR   RefSeq; WP_038183991.1; NZ_ASQA01000016.1.
DR   AlphaFoldDB; W4EYY4; -.
DR   PATRIC; fig|1227360.4.peg.2108; -.
DR   eggNOG; COG0331; Bacteria.
DR   Proteomes; UP000019062; Unassembled WGS sequence.
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:UP000019062};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000446}.
FT   DOMAIN          7..312
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        201
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000446-1"
SQ   SEQUENCE   320 AA;  34284 MW;  30CBBA572BC81878 CRC64;
     MTKIAFIFPG QGSQSVGMGA EFVAEHQECK AYYNKADELL GYSLSKLMLE GPAEDLTLTY
     NAQPALLTTS AMIADKLTKV GITPDYTAGH SLGEYTALVA SGVMSFQDGV QAVHSRGMFM
     NEAVPAGEGA MAAILGLDRD ALKAVTDEVS ASGEVVQLAN LNCPGQIVIS GTKTGVDKAS
     VKAKEAGAKR ALPLVVSGPF HSELMRPAAG KLQENLKQKA MQDAKIPVIS NVTAKPVTEQ
     NEIQQLLVEQ LYSPVLWEDS VRKMIDLGVD VFIECGPGKV LSGLVKKVDR QVKTYCVYDE
     ATFEQVVEAS KEWSHEEARG
//
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