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FABD_STAAM
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   03-AUG-2022, entry version 112.
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; Firmicutes; 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}.
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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   World-2DPAGE; 0002:Q99UN8; -.
DR   PaxDb; Q99UN8; -.
DR   EnsemblBacteria; BAB57392; BAB57392; SAV1230.
DR   KEGG; sav:SAV1230; -.
DR   HOGENOM; CLU_030558_0_1_9; -.
DR   OMA; AANYNCP; -.
DR   PhylomeDB; Q99UN8; -.
DR   BioCyc; SAUR158878:SAV_RS06625-MON; -.
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; 3.40.366.10; -; 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   Pfam; PF00698; Acyl_transf_1; 1.
DR   PIRSF; PIRSF000446; Mct; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   SUPFAM; SSF55048; SSF55048; 1.
DR   TIGRFAMs; TIGR00128; fabD; 1.
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
 
 
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