ID A1SI65_NOCSJ Unreviewed; 399 AA.
AC A1SI65;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=[acyl-carrier-protein] S-malonyltransferase {ECO:0000256|ARBA:ARBA00013258};
DE EC=2.3.1.39 {ECO:0000256|ARBA:ARBA00013258};
GN OrderedLocusNames=Noca_1990 {ECO:0000313|EMBL:ABL81500.1};
OS Nocardioides sp. (strain ATCC BAA-499 / JS614).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=196162 {ECO:0000313|EMBL:ABL81500.1, ECO:0000313|Proteomes:UP000000640};
RN [1] {ECO:0000313|Proteomes:UP000000640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Mattes T., Gossett J.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Nocardioides sp. JS614.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABL81500.1, ECO:0000313|Proteomes:UP000000640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
RX PubMed=21551312; DOI=10.1128/JB.05109-11;
RA Coleman N.V., Wilson N.L., Barry K., Brettin T.S., Bruce D.C., Copeland A.,
RA Dalin E., Detter J.C., Del Rio T.G., Goodwin L.A., Hammon N.M., Han S.,
RA Hauser L.J., Israni S., Kim E., Kyrpides N., Land M.L., Lapidus A.,
RA Larimer F.W., Lucas S., Pitluck S., Richardson P., Schmutz J., Tapia R.,
RA Thompson S., Tice H.N., Spain J.C., Gossett J.G., Mattes T.E.;
RT "Genome Sequence of the ethene- and vinyl chloride-oxidizing actinomycete
RT Nocardioides sp. strain JS614.";
RL J. Bacteriol. 193:3399-3400(2011).
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};
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DR EMBL; CP000509; ABL81500.1; -; Genomic_DNA.
DR RefSeq; WP_011755447.1; NC_008699.1.
DR AlphaFoldDB; A1SI65; -.
DR STRING; 196162.Noca_1990; -.
DR KEGG; nca:Noca_1990; -.
DR eggNOG; COG0331; Bacteria.
DR eggNOG; COG0511; Bacteria.
DR HOGENOM; CLU_030558_1_2_11; -.
DR OrthoDB; 3248271at2; -.
DR Proteomes; UP000000640; Chromosome.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
DR Gene3D; 2.40.50.100; -; 1.
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 InterPro; IPR039562; MFP_biotin_lipoyl_2.
DR InterPro; IPR011053; Single_hybrid_motif.
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 Pfam; PF13533; Biotin_lipoyl_2; 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 SUPFAM; SSF51230; Single hybrid motif; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000313|EMBL:ABL81500.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000640};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABL81500.1}.
FT DOMAIN 5..326
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
SQ SEQUENCE 399 AA; 41267 MW; 3BE113219B420E30 CRC64;
MLVIVAPGQG AQSPGFLRPW LEDPTFASRF AWLSTVAGLD LAHYGTEADA ETIRATEIAQ
PLLVATGLVA ALELFPSPAD AFEQVGAVAG HSVGEIAAAA GARVITAEQA MVLVRERGNA
MARAAAATPT GMTAVLGGDR DEVLAALAEH GLTPANDNAA GQLVAAGTLE QLEALAAHPP
AKARLMPLSV AGAFHTHHME PAVGHLAALA RSVSVHDPRT RVISNRDGRV VHDGRDVLAR
IVGQIASPVR WDLCLETMED LGVTGILEMP PAGTLTGIAR RRFSGSALRG VETFALKTPD
QLDDARAFCA KHGESSGLGI SPTWRMVVSP AKGTFHQDGA AAGTDVLVPG AAIGEVASLR
DRSRITAAHG GTVVEWLVED GDLVSPGQPL LRLHPEGGA
//
