ID Q83GL2_TROWT Unreviewed; 339 AA. AC Q83GL2; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 08-OCT-2025, entry version 108. DE RecName: Full=[acyl-carrier-protein] S-malonyltransferase {ECO:0000256|ARBA:ARBA00013258}; DE EC=2.3.1.39 {ECO:0000256|ARBA:ARBA00013258}; GN Name=fabD {ECO:0000313|EMBL:AAO44351.1}; GN OrderedLocusNames=TWT_254 {ECO:0000313|EMBL:AAO44351.1}; OS Tropheryma whipplei (strain Twist) (Whipple's bacillus). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales; OC Tropherymataceae; Tropheryma. OX NCBI_TaxID=203267 {ECO:0000313|EMBL:AAO44351.1, ECO:0000313|Proteomes:UP000002200}; RN [1] {ECO:0000313|EMBL:AAO44351.1, ECO:0000313|Proteomes:UP000002200} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Twist {ECO:0000313|EMBL:AAO44351.1, RC ECO:0000313|Proteomes:UP000002200}; RX PubMed=12902375; DOI=10.1101/gr.1474603; RA Raoult D., Ogata H., Audic S., Robert C., Suhre K., Drancourt M., RA Claverie J.-M.; RT "Tropheryma whipplei twist: a human pathogenic Actinobacteria with a RT reduced genome."; RL Genome Res. 13:1800-1809(2003). CC -!- CATALYTIC ACTIVITY: CC Reaction=holo-[ACP] + malonyl-CoA = malonyl-[ACP] + CoA; 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:ARBA00048462}; 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; AE014184; AAO44351.1; -; Genomic_DNA. DR RefSeq; WP_011102456.1; NC_004572.3. DR AlphaFoldDB; Q83GL2; -. DR STRING; 203267.TWT_254; -. DR KEGG; twh:TWT_254; -. DR eggNOG; COG0331; Bacteria. DR HOGENOM; CLU_030558_1_2_11; -. DR OrthoDB; 3248271at2; -. DR Proteomes; UP000002200; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:TreeGrafter. 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_dom. DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase. DR InterPro; IPR050858; Mal-CoA-ACP_Trans/PKS_FabD. DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd. 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 ECO:0000313|EMBL:AAO44351.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002200}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AAO44351.1}. FT DOMAIN 21..322 FT /note="Malonyl-CoA:ACP transacylase (MAT)" FT /evidence="ECO:0000259|SMART:SM00827" SQ SEQUENCE 339 AA; 37499 MW; CC16D7A90F5A2952 CRC64; MASICDTTPE ECAAAGNAVI TCPGQGAQKS GLLNEWLDLP GSLEFFQAQS DFLKIDLIKH GTISDTDILR DTRIAQPLIV ALGIFVIRTL QQKAKIIQSM PEEGLNGANP TERIMRCVGL AGHSVGEITA AFGAGVLTEK NAMRLVKHRA NQMYKSTQIF DTGMVAVLGQ SENLEEYITQ RYKLFPANYN CPGQIVFAGL RENLDVLLAN PPEKIKVIPL QVAGAFHTRF MRPAVQNLKK LKFVTDKSFA KDPDKRIWTN YDGSEIFSGS EYVQLLIDQI ARPVRWDLCQ KNFENIDYLI ELPPAGTLTG LARRSLPKVK GIPINTIDDL EEASCCFLL //