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Database: UniProt
Entry: A0A0F2NKA2_9FIRM
LinkDB: A0A0F2NKA2_9FIRM
Original site: A0A0F2NKA2_9FIRM 
ID   A0A0F2NKA2_9FIRM        Unreviewed;       314 AA.
AC   A0A0F2NKA2;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
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=VR68_04905 {ECO:0000313|EMBL:KJS01606.1};
OS   Peptococcaceae bacterium BRH_c4a.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX   NCBI_TaxID=1629716 {ECO:0000313|EMBL:KJS01606.1, ECO:0000313|Proteomes:UP000033439};
RN   [1] {ECO:0000313|EMBL:KJS01606.1, ECO:0000313|Proteomes:UP000033439}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c4a {ECO:0000313|EMBL:KJS01606.1};
RA   Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (MAR-2015) 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:KJS01606.1}.
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DR   EMBL; LADN01000033; KJS01606.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F2NKA2; -.
DR   STRING; 1629716.VR68_04905; -.
DR   PATRIC; fig|1629716.3.peg.1630; -.
DR   Proteomes; UP000033439; 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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000446}.
FT   DOMAIN          7..306
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   314 AA;  33441 MW;  07B1F0AB0DE4275D CRC64;
     MAKRSFVFPG QGSQQVGMGR DMYEKYPAAR DIFDRANKAL GFDITALCFG GAEEELKKTV
     NAQPAILTVS VACLAVMRQM GLRPDTAAGH SLGEYTALVA AGALNFEDAV TLVRLRGQYM
     QEAVPLGEGG MVAVLGMETG KISDICSGLS GPDGVVEAVN LNCPGQVVIA GDTRSLEKAV
     EVLNERGARK CLPLSVSAPF HSSLMRSAGE KLEASLSRVK IKDPEIPVLS NVTADYHGKT
     AEIKDLLVKQ VSSPVRWEEC VRKMIGDGTG IFVEVGPGKV ISGLVRKIDR DVEVKNVEDS
     VSLEKILASF GEVS
//
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