ID K9B6K8_9STAP Unreviewed; 308 AA.
AC K9B6K8;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
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 ORFNames=C273_00400 {ECO:0000313|EMBL:EKU50437.1};
OS Staphylococcus massiliensis S46.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1229783 {ECO:0000313|EMBL:EKU50437.1, ECO:0000313|Proteomes:UP000009885};
RN [1] {ECO:0000313|EMBL:EKU50437.1, ECO:0000313|Proteomes:UP000009885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S46 {ECO:0000313|EMBL:EKU50437.1,
RC ECO:0000313|Proteomes:UP000009885};
RX PubMed=23929469;
RA Srivastav R., Singh A., Jangir P.K., Kumari C., Muduli S., Sharma R.;
RT "Genome Sequence of Staphylococcus massiliensis Strain S46, Isolated from
RT the Surface of Healthy Human Skin.";
RL Genome Announc. 1:e00553-13(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKU50437.1}.
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DR EMBL; AMSQ01000001; EKU50437.1; -; Genomic_DNA.
DR RefSeq; WP_009381686.1; NZ_AMSQ01000001.1.
DR AlphaFoldDB; K9B6K8; -.
DR STRING; 1229783.C273_00400; -.
DR PATRIC; fig|1229783.3.peg.84; -.
DR eggNOG; COG0331; Bacteria.
DR OrthoDB; 9805460at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000009885; Unassembled WGS sequence.
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 {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:UP000009885};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000446}.
FT DOMAIN 7..300
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; 33858 MW; 52F1C6CB1B99BCDF CRC64;
MGKTAIVFPG QGAQKVGMAE DLYNKNEAAT EILNIAQDSM DFDLLETMFT DSDEKLGETE
NTQPALLTHS IALYRALENL DADYTMGHSL GEYSSLVASG VLKFEDAVRI VRKRGELMAK
AFPTGVGSMA AVLGLSVEKV TEICHQLSND DVKVEPANIN APGQVVVSGH KEAIDTLVQK
GKELGAKRVM PLKVSGPFHS SMMQVIEDDF KAFIQIFDWN DANMPVVQNV NAQGEQEASI
IEANMVEQLY SPVQFIKSTE WLIDQGVDHF IEIGPGKVLS GLIKKINRDV KLTSIQTLED
VKEWNENE
//
