ID FABD_STAAW Reviewed; 308 AA. AC Q7A124; DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 99. DE RecName: Full=Malonyl CoA-acyl carrier protein transacylase; DE Short=MCT; DE EC=2.3.1.39; GN Name=fabD; OrderedLocusNames=MW1113; OS Staphylococcus aureus (strain MW2). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=196620; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MW2; RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5; RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y., RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.; RT "Genome and virulence determinants of high virulence community-acquired RT MRSA."; RL Lancet 359:1819-1827(2002). 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 -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC -!- SIMILARITY: Belongs to the FabD family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BA000033; BAB94978.1; -; Genomic_DNA. DR RefSeq; WP_000047343.1; NC_003923.1. DR AlphaFoldDB; Q7A124; -. DR SMR; Q7A124; -. DR KEGG; sam:MW1113; -. DR HOGENOM; CLU_030558_0_1_9; -. DR UniPathway; UPA00094; -. DR Proteomes; UP000000418; Chromosome. DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway. 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; Fatty acid biosynthesis; Fatty acid metabolism; KW Lipid biosynthesis; Lipid metabolism; Transferase. FT CHAIN 1..308 FT /note="Malonyl CoA-acyl carrier protein transacylase" FT /id="PRO_0000194225" FT ACT_SITE 89 FT /evidence="ECO:0000250" FT ACT_SITE 199 FT /evidence="ECO:0000250" SQ SEQUENCE 308 AA; 33649 MW; B2FAEF8A200804C3 CRC64; MSKTAIIFPG QGAQKVGMAQ DLFNNNDQAT EILTSAAKTL DFDILETMFT DEEGKLGETE NTQPALLTHS SALLAALKNL NPDFTMGHSL GEYSSLVAAD VLSFEDAVKI VRKRGQLMAQ AFPTGVGSMA AVLGLDFDKV DEICKSLSSD DKIIEPANIN CPGQIVVSGH KALIDELVEK GKSLGAKRVM PLAVSGPFHS SLMKVIEEDF SSYINQFEWR DAKFPVVQNV NAQGETDKEV IKSNMVKQLY SPVQFINSTE WLIDQGVDHF IEIGPGKVLS GLIKKINRDV KLTSIQTLED VKGWNEND //