ID Q2FZ54_STAA8 Unreviewed; 308 AA.
AC Q2FZ54;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=Malonyl CoA-acyl carrier protein transacylase {ECO:0000256|ARBA:ARBA00018953, ECO:0000256|PIRNR:PIRNR000446};
DE EC=2.3.1.39 {ECO:0000256|ARBA:ARBA00013258, ECO:0000256|PIRNR:PIRNR000446};
GN OrderedLocusNames=SAOUHSC_01198 {ECO:0000313|EMBL:ABD30304.1};
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061 {ECO:0000313|EMBL:ABD30304.1, ECO:0000313|Proteomes:UP000008816};
RN [1] {ECO:0000313|Proteomes:UP000008816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47 {ECO:0000313|Proteomes:UP000008816};
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington D.C
RL (2006).
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,
CC ECO:0000256|PIRNR:PIRNR000446};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194}.
CC -!- SIMILARITY: Belongs to the fabD family.
CC {ECO:0000256|PIRNR:PIRNR000446}.
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DR EMBL; CP000253; ABD30304.1; -; Genomic_DNA.
DR RefSeq; WP_000047348.1; NZ_LS483365.1.
DR RefSeq; YP_499736.1; NC_007795.1.
DR AlphaFoldDB; Q2FZ54; -.
DR SMR; Q2FZ54; -.
DR STRING; 93061.SAOUHSC_01198; -.
DR PaxDb; 1280-SAXN108_1230; -.
DR GeneID; 3919330; -.
DR KEGG; sao:SAOUHSC_01198; -.
DR PATRIC; fig|93061.5.peg.1100; -.
DR eggNOG; COG0331; Bacteria.
DR HOGENOM; CLU_030558_0_1_9; -.
DR OrthoDB; 9805460at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
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 {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|PIRNR:PIRNR000446};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000008816};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000446}.
FT DOMAIN 7..304
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
FT ACT_SITE 89
FT /evidence="ECO:0000256|PIRSR:PIRSR000446-1"
FT ACT_SITE 199
FT /evidence="ECO:0000256|PIRSR:PIRSR000446-1"
SQ SEQUENCE 308 AA; 33635 MW; C28AEC6CC50805C2 CRC64;
MSKTAIIFPG QGAQKVGMAQ DLFNNNDQAT EILTSAANTL 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
//
