ID FABD_STAAM Reviewed; 308 AA. AC Q99UN8; DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 27-MAR-2024, entry version 118. DE RecName: Full=Malonyl CoA-acyl carrier protein transacylase; DE Short=MCT; DE EC=2.3.1.39; GN Name=fabD; OrderedLocusNames=SAV1230; OS Staphylococcus aureus (strain Mu50 / ATCC 700699). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=158878; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Mu50 / ATCC 700699; RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2; RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y., RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., RA Hiramatsu K.; RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus."; RL Lancet 357:1225-1240(2001). 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; BA000017; BAB57392.1; -; Genomic_DNA. DR RefSeq; WP_000047343.1; NC_002758.2. DR PDB; 3IM9; X-ray; 1.46 A; A=5-308. DR PDBsum; 3IM9; -. DR AlphaFoldDB; Q99UN8; -. DR SMR; Q99UN8; -. DR KEGG; sav:SAV1230; -. DR HOGENOM; CLU_030558_0_1_9; -. DR PhylomeDB; Q99UN8; -. DR BRENDA; 2.3.1.39; 3352. DR UniPathway; UPA00094; -. DR EvolutionaryTrace; Q99UN8; -. DR PHI-base; PHI:7916; -. DR Proteomes; UP000002481; 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. DR World-2DPAGE; 0002:Q99UN8; -. PE 1: Evidence at protein level; KW 3D-structure; Acyltransferase; Fatty acid biosynthesis; KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Transferase. FT CHAIN 1..308 FT /note="Malonyl CoA-acyl carrier protein transacylase" FT /id="PRO_0000194224" FT ACT_SITE 89 FT /evidence="ECO:0000250" FT ACT_SITE 199 FT /evidence="ECO:0000250" FT STRAND 5..8 FT /evidence="ECO:0007829|PDB:3IM9" FT TURN 16..25 FT /evidence="ECO:0007829|PDB:3IM9" FT HELIX 27..39 FT /evidence="ECO:0007829|PDB:3IM9" FT HELIX 44..49 FT /evidence="ECO:0007829|PDB:3IM9" FT HELIX 59..76 FT /evidence="ECO:0007829|PDB:3IM9" FT STRAND 83..88 FT /evidence="ECO:0007829|PDB:3IM9" FT HELIX 91..98 FT /evidence="ECO:0007829|PDB:3IM9" FT HELIX 104..120 FT /evidence="ECO:0007829|PDB:3IM9" FT STRAND 126..134 FT /evidence="ECO:0007829|PDB:3IM9" FT HELIX 137..147 FT /evidence="ECO:0007829|PDB:3IM9" FT STRAND 154..161 FT /evidence="ECO:0007829|PDB:3IM9" FT STRAND 164..170 FT /evidence="ECO:0007829|PDB:3IM9" FT HELIX 171..180 FT /evidence="ECO:0007829|PDB:3IM9" FT TURN 181..185 FT /evidence="ECO:0007829|PDB:3IM9" FT STRAND 187..191 FT /evidence="ECO:0007829|PDB:3IM9" FT HELIX 201..206 FT /evidence="ECO:0007829|PDB:3IM9" FT HELIX 207..214 FT /evidence="ECO:0007829|PDB:3IM9" FT TURN 229..231 FT /evidence="ECO:0007829|PDB:3IM9" FT STRAND 233..235 FT /evidence="ECO:0007829|PDB:3IM9" FT HELIX 238..248 FT /evidence="ECO:0007829|PDB:3IM9" FT HELIX 255..264 FT /evidence="ECO:0007829|PDB:3IM9" FT STRAND 267..276 FT /evidence="ECO:0007829|PDB:3IM9" FT HELIX 278..286 FT /evidence="ECO:0007829|PDB:3IM9" FT STRAND 288..295 FT /evidence="ECO:0007829|PDB:3IM9" FT HELIX 298..304 FT /evidence="ECO:0007829|PDB:3IM9" 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 //