ID E0I4M9_9BACL Unreviewed; 433 AA.
AC E0I4M9;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=[acyl-carrier-protein] S-malonyltransferase {ECO:0000256|ARBA:ARBA00013258};
DE EC=2.3.1.39 {ECO:0000256|ARBA:ARBA00013258};
GN ORFNames=PaecuDRAFT_0071 {ECO:0000313|EMBL:EFM12560.1};
OS Paenibacillus curdlanolyticus YK9.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=717606 {ECO:0000313|EMBL:EFM12560.1, ECO:0000313|Proteomes:UP000005387};
RN [1] {ECO:0000313|EMBL:EFM12560.1, ECO:0000313|Proteomes:UP000005387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YK9 {ECO:0000313|EMBL:EFM12560.1,
RC ECO:0000313|Proteomes:UP000005387};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Land M.L., Hauser L., Chang Y.-J., Jeffries C., Anderson I.J.,
RA Johnson E., Loganathan U., Mulhopadhyay B., Kyrpides N., Woyke T.J.;
RT "The draft genome of Paenibacillus curdlanolyticus YK9.";
RL Submitted (JUL-2010) 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};
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DR EMBL; AEDD01000001; EFM12560.1; -; Genomic_DNA.
DR RefSeq; WP_006036089.1; NZ_AEDD01000001.1.
DR AlphaFoldDB; E0I4M9; -.
DR STRING; 717606.PaecuDRAFT_0071; -.
DR eggNOG; COG0331; Bacteria.
DR OrthoDB; 9805460at2; -.
DR Proteomes; UP000005387; 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; 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 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 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Reference proteome {ECO:0000313|Proteomes:UP000005387};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 10..308
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
SQ SEQUENCE 433 AA; 47389 MW; 3E76CC84545B2ADE CRC64;
MKEMNRIALL FPGQGSQYVG MGKRLYDEYE VARETFEEAN DVLGFDLKGL CFHGDLSELS
QTENTQPALL TASVAAYRVY MEQIGIQPLL AAGHSLGEYS ALVCSGALTF AEALKIVRLR
GQYMQQASLA GIGKMASISQ YPLDEIEQLC HFASTSEQQV RIACYNSPSQ SVISGHASAV
QQVAAEAAKA GAKVIELNVS AAFHSSLMEE AEAKLKAELQ KYTFNKPNWP IISNVTGLPY
MESADVAELL TRQMVYPVLW NQSMDYLQKQ AIAVTIELGP KKVLTNLLKA SLHNGSSLQA
MALESKEEVE MIKQALHKSG ASKPAGEKEI PGLAVIASCI AAAVSTKNRN WDSQAYQTGV
AQPYREVKRM YELLESNKQE PSAEQIQLAI RMLQTVLETK KAPVEQQQAM MAKIKERAAL
FGAREVKEAV GVC
//
