ID B8NZ48_ASPFN Unreviewed; 389 AA.
AC B8NZ48;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=[acyl-carrier-protein] S-malonyltransferase {ECO:0000256|ARBA:ARBA00013258};
DE EC=2.3.1.39 {ECO:0000256|ARBA:ARBA00013258};
GN ORFNames=AFLA_012430 {ECO:0000313|EMBL:EED44714.1};
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952 {ECO:0000313|EMBL:EED44714.1, ECO:0000313|Proteomes:UP000001875};
RN [1] {ECO:0000313|EMBL:EED44714.1, ECO:0000313|Proteomes:UP000001875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC SRRC 167 {ECO:0000313|Proteomes:UP000001875};
RX PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963488; EED44714.1; -; Genomic_DNA.
DR RefSeq; XP_002385613.1; XM_002385572.1.
DR AlphaFoldDB; B8NZ48; -.
DR STRING; 332952.B8NZ48; -.
DR EnsemblFungi; EED44714; EED44714; AFLA_012430.
DR VEuPathDB; FungiDB:AFLA_012896; -.
DR eggNOG; KOG2926; Eukaryota.
DR HOGENOM; CLU_030558_5_0_1; -.
DR OMA; AANYNCP; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 48..371
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
SQ SEQUENCE 389 AA; 43496 MW; 110EC4D05E87CCC6 CRC64;
MLFTSGSNYT LYIKSTLHHV PCRSLFILKC QRRWYSVSRK ATLRTALFFP GHGVQRVGMV
SSWINNFPDI AGSFLDEMDS VLGFRLSRVI SEGPNSELNK TENSQPAIMA TSILILRILE
QKFGFDTKSR VDVTLGHSLG EFSALVTGGY IDFGDALKLV RRRAEIMAQC TRRASTESGE
DYGMVALVCE PDHLNGLASN GMRDDLSYGM PPIEKVMVAN VNSKNQIVLS GSIERIRTLL
IQLRQFGGHD PRAVRLNSES PFHSPIMMPA AEYMVRALDK IKLNFPAHMP CVSNVSGLPF
RSADELRRLL SQQCVDTVRW WDSIRYLDQE RGVKRWVGIG PGKVGRNLVG KEVGKVMTKG
GGVWAICDTR ELEDIVRSLE QTEFEASCD
//
