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Database: UniProt
Entry: A0A024QD66_9BACI
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ID   A0A024QD66_9BACI        Unreviewed;       312 AA.
AC   A0A024QD66;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Malonyl CoA-acyl carrier protein transacylase {ECO:0000256|PIRNR:PIRNR000446};
DE            EC=2.3.1.39 {ECO:0000256|PIRNR:PIRNR000446};
GN   Name=fabD {ECO:0000313|EMBL:CDQ40150.1};
GN   ORFNames=BN990_02468 {ECO:0000313|EMBL:CDQ40150.1};
OS   Virgibacillus massiliensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX   NCBI_TaxID=1462526 {ECO:0000313|EMBL:CDQ40150.1, ECO:0000313|Proteomes:UP000028875};
RN   [1] {ECO:0000313|EMBL:CDQ40150.1, ECO:0000313|Proteomes:UP000028875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Vm-5 {ECO:0000313|EMBL:CDQ40150.1,
RC   ECO:0000313|Proteomes:UP000028875};
RA   Urmite Genomes U.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000028875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Vm-5 {ECO:0000313|Proteomes:UP000028875};
RA   Khelaifia S., Croce O., Lagier J.C., Raoult D.;
RT   "Draft genome sequence of Virgibacillus massiliensis Vm-5.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
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:CDQ40150.1}.
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DR   EMBL; CCDP010000001; CDQ40150.1; -; Genomic_DNA.
DR   RefSeq; WP_038244412.1; NZ_CCDP010000001.1.
DR   AlphaFoldDB; A0A024QD66; -.
DR   STRING; 1462526.BN990_02468; -.
DR   eggNOG; COG0331; Bacteria.
DR   OrthoDB; 9805460at2; -.
DR   Proteomes; UP000028875; 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:UP000028875};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000446}.
FT   DOMAIN          7..300
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        199
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000446-1"
SQ   SEQUENCE   312 AA;  34342 MW;  C4B5F9FDA3825842 CRC64;
     MKKVAFMFPG QGSQEVGMGK ELYETYPDMK QLFEEADRTL NTDLTKIMFE GPKERLTETE
     NAQPALLLMS VALHTLLLKH EVQPVMTVGH SLGEYSALVA AGAISLEEAL PLVSTRGKLM
     EQAFPKGQGT MAAVLGLDVE TIQAGLDEID DEIVDLANLN CPGQIVISGS VKGIEQATTI
     LKSKGAKRVM PLNVSGPFHS RLMKAANESF ANYLNEVSIK DATIPVYANV SASPVRESNE
     IKNLLIKQLY SPVRFEESIM NMMDHDMDAF VEVGNGKVLS GLVRKINRRT KTFAVQDTAS
     LEEFIAWYRE DI
//
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