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Database: UniProt
Entry: U7ULB6_9FIRM
LinkDB: U7ULB6_9FIRM
Original site: U7ULB6_9FIRM 
ID   U7ULB6_9FIRM            Unreviewed;       313 AA.
AC   U7ULB6;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
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:ERT59659.1};
GN   ORFNames=HMPREF1250_0736 {ECO:0000313|EMBL:ERT59659.1};
OS   Megasphaera vaginalis.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Megasphaera.
OX   NCBI_TaxID=1111454 {ECO:0000313|EMBL:ERT59659.1, ECO:0000313|Proteomes:UP000017090};
RN   [1] {ECO:0000313|EMBL:ERT59659.1, ECO:0000313|Proteomes:UP000017090}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BV3C16-1 {ECO:0000313|EMBL:ERT59659.1,
RC   ECO:0000313|Proteomes:UP000017090};
RA   Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA   Methe B., Sutton G., Nelson K.E.;
RL   Submitted (SEP-2013) 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:ERT59659.1}.
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DR   EMBL; AWXA01000034; ERT59659.1; -; Genomic_DNA.
DR   RefSeq; WP_023053713.1; NZ_AWXA01000034.1.
DR   AlphaFoldDB; U7ULB6; -.
DR   STRING; 1111454.HMPREF1250_0736; -.
DR   PATRIC; fig|1111454.3.peg.1185; -.
DR   eggNOG; COG0331; Bacteria.
DR   OrthoDB; 9805460at2; -.
DR   Proteomes; UP000017090; 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:UP000017090};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000446}.
FT   DOMAIN          6..305
FT                   /note="Malonyl-CoA:ACP transacylase (MAT)"
FT                   /evidence="ECO:0000259|SMART:SM00827"
FT   ACT_SITE        90
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000446-1"
FT   ACT_SITE        200
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000446-1"
SQ   SEQUENCE   313 AA;  33322 MW;  8E4A30522F666BDC CRC64;
     MKTAFVFPGQ GAQKTGMLKD LYEAYPLVRE VFEEADDTLG FSLTQLCFEG PDEELMKTFN
     TQPAILTAST ACCRVLMQEG IRPDIVAGHS LGEYSALVAA GALSFADAVK TVRLRGQFMQ
     DAVPLGEGAM AAILGLDDDT IKEICHTVSL QGGAVQAVNF NCPGQTVIAG AAKAVETAAA
     ELKKAGAKRA VMLSVSAPFH STLMEPAAKR LAEVLEEITI NDAEIPVVAN VNGRVETAAA
     EIKQNLVAQA ASPVLWIDCT RTMRQCGADV FVEAGPGKTL CGFNKKIDKS IHSENVEDIP
     SLQKTLEFFQ GVR
//
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