ID I4EQF0_9ACTN Unreviewed; 322 AA.
AC I4EQF0;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
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:CCH85613.1};
GN OrderedLocusNames=MODMU_0141 {ECO:0000313|EMBL:CCH85613.1};
OS Modestobacter marinus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Modestobacter.
OX NCBI_TaxID=477641 {ECO:0000313|EMBL:CCH85613.1, ECO:0000313|Proteomes:UP000006461};
RN [1] {ECO:0000313|EMBL:CCH85613.1, ECO:0000313|Proteomes:UP000006461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC501 {ECO:0000313|EMBL:CCH85613.1,
RC ECO:0000313|Proteomes:UP000006461};
RX PubMed=22887672; DOI=10.1128/JB.01029-12;
RA Normand P., Gury J., Pujic P., Chouaia B., Crotti E., Brusetti L.,
RA Daffonchio D., Vacherie B., Barbe V., Medigue C., Calteau A.,
RA Ghodhbane-Gtari F., Essoussi I., Nouioui I., Abbassi-Ghozzi I., Gtari M.;
RT "Genome Sequence of Radiation-Resistant Modestobacter marinus Strain BC501,
RT a Representative Actinobacterium That Thrives on Calcareous Stone
RT Surfaces.";
RL J. Bacteriol. 194:4773-4774(2012).
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 ---------------------------------------------------------------------------
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; FO203431; CCH85613.1; -; Genomic_DNA.
DR RefSeq; WP_014738230.1; NC_017955.1.
DR AlphaFoldDB; I4EQF0; -.
DR STRING; 477641.MODMU_0141; -.
DR KEGG; mmar:MODMU_0141; -.
DR PATRIC; fig|477641.3.peg.141; -.
DR eggNOG; COG0331; Bacteria.
DR HOGENOM; CLU_030558_1_1_11; -.
DR OMA; LNKTQFT; -.
DR OrthoDB; 3543921at2; -.
DR Proteomes; UP000006461; Chromosome.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
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; 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:CCH85613.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006461};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCH85613.1}.
FT DOMAIN 27..301
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
FT REGION 302..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 322 AA; 32690 MW; ACAF6C4E433375B6 CRC64;
MTALAPGAAV VLPGEDSARP HALDAWLGDA AARDVVAEAS DVLGRDVVPW WGDPLNLCDP
VAAHLTTVVT GVAGYRSLTA AGLQPVVVAG HGVGEYAALV AAGALPLEQV VAFVDWRAEA
LAHAPRPSCA GMAAVVGPGA AEVARSVVTG LPAGGLSIAS LDGPAQVVLS GSREELEQAR
TAVTAAGLDM VRLRGRAACH GPLMQSVADH LAAPLADLDW SVPDVPVVPN ADGRPTRDPD
HLARCLRAHL TSPVQWETTS RALVGAGATW VVEVGPVPTL GPLIRQVHPD LPLHLATAPG
ALTPIALPEP ELTGPAPTGG ER
//
