ID R7XZI8_9ACTN Unreviewed; 394 AA.
AC R7XZI8;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=[acyl-carrier-protein] S-malonyltransferase {ECO:0000256|ARBA:ARBA00013258};
DE EC=2.3.1.39 {ECO:0000256|ARBA:ARBA00013258};
GN ORFNames=CF8_1144 {ECO:0000313|EMBL:EON24767.1};
OS Nocardioides sp. CF8.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=110319 {ECO:0000313|EMBL:EON24767.1, ECO:0000313|Proteomes:UP000015971};
RN [1] {ECO:0000313|EMBL:EON24767.1, ECO:0000313|Proteomes:UP000015971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF8 {ECO:0000313|EMBL:EON24767.1,
RC ECO:0000313|Proteomes:UP000015971};
RX PubMed=23833136;
RA Kimbrel J.A., Chang J., Arp D.J., Sayavedra-Soto L.A.;
RT "The Draft Genome Sequence of Nocardioides sp. Strain CF8 Reveals the Scope
RT of Its Metabolic Capabilities.";
RL Genome Announc. 1:e00439-e00439(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 -!- 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:EON24767.1}.
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DR EMBL; ASEP01000039; EON24767.1; -; Genomic_DNA.
DR RefSeq; WP_010832138.1; NZ_CM001852.1.
DR AlphaFoldDB; R7XZI8; -.
DR STRING; 110319.CF8_1144; -.
DR PATRIC; fig|110319.3.peg.1741; -.
DR eggNOG; COG0331; Bacteria.
DR eggNOG; COG0511; Bacteria.
DR HOGENOM; CLU_030558_1_2_11; -.
DR OrthoDB; 3248271at2; -.
DR Proteomes; UP000015971; Chromosome.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
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 Reference proteome {ECO:0000313|Proteomes:UP000015971};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EON24767.1}.
FT DOMAIN 5..346
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
SQ SEQUENCE 394 AA; 40718 MW; 9E859B8C5F817CEC CRC64;
MLVIVAPGQG AQTPGFLVPW LEDPVFASRL QWLSTVAGLD LADYGANADA ETIRDTRIAQ
PLLVATGLVA ALDLFPHPAD AFARIGAVAG HSVGELTAAA GARAITAEQA MVLVRERGAA
MATASAATPT GMTAVLGGDR EEVLAALAEH GLTAANDNGP GQIVAAGTLE QLAAFAAEPP
AKARLMPLSV AGAFHTSHMQ PAVSHLAALA RSVSTHDPRT PVISNRDGQV VHDGRDVVAR
IVGQIASPVR WDLCMEAMLD LGVTGILEMP PAGTLTGIAK RAMKGVETFA LKTPDQLDDA
RAFADKHGEA SMIETSPTWR MVVSPGKGTF HRSAEAADLA VLPAGCTIGE VASTRDSTRV
SARHGGSVVE WLVEDGDLVS PGQPLLRLHP EGVS
//
