ID A7GRI2_BACCN Unreviewed; 316 AA.
AC A7GRI2;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 91.
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=Bcer98_2504 {ECO:0000313|EMBL:ABS22740.1};
OS Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=315749 {ECO:0000313|EMBL:ABS22740.1, ECO:0000313|Proteomes:UP000002300};
RN [1] {ECO:0000313|EMBL:ABS22740.1, ECO:0000313|Proteomes:UP000002300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98
RC {ECO:0000313|Proteomes:UP000002300};
RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "Extending the Bacillus cereus group genomics to putative food-borne
RT pathogens of different toxicity.";
RL Chem. Biol. Interact. 171:236-249(2008).
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; CP000764; ABS22740.1; -; Genomic_DNA.
DR RefSeq; WP_012094946.1; NC_009674.1.
DR AlphaFoldDB; A7GRI2; -.
DR STRING; 315749.Bcer98_2504; -.
DR KEGG; bcy:Bcer98_2504; -.
DR eggNOG; COG0331; Bacteria.
DR HOGENOM; CLU_030558_0_1_9; -.
DR OrthoDB; 9805460at2; -.
DR Proteomes; UP000002300; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000446}.
FT DOMAIN 7..314
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 316 AA; 34221 MW; B9235F86D3E079A1 CRC64;
MGKLAFLFPG QGSQAVGMGK QLAENNKKVA EVFQKADQVL NEPLSQVIFE GPQEKLTLTT
NAQPALLTTS FAILTALNEY DITPDYVAGH SLGEYSALVA VEALTFEDAV YAVRKRGEYM
EEAVPGGEGA MAAILGADPN MLKQVTEEVT NEGHAVQIAN MNSVKQIVIS GTKQGVELAS
QKAKEKGAKR AIPLRVSGPF HSSLMKPAAE KFKSVLNEIA IQDAKIPVIA NVTADCMTNR
EEIQEKLIEQ LYSPVLWYPS MEYMIEQGVD TFIEIGPGKV LAGLMKAIDS SVKVYTVYDE
ETLKDTISSL RGENGC
//
