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Database: UniProt
Entry: U2QI90_9ACTN
LinkDB: U2QI90_9ACTN
Original site: U2QI90_9ACTN 
ID   U2QI90_9ACTN            Unreviewed;       316 AA.
AC   U2QI90;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=[acyl-carrier-protein] S-malonyltransferase {ECO:0000256|ARBA:ARBA00013258};
DE            EC=2.3.1.39 {ECO:0000256|ARBA:ARBA00013258};
GN   ORFNames=HMPREF0682_2111 {ECO:0000313|EMBL:ERK56216.1};
OS   Propionibacterium acidifaciens F0233.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Propionibacterium.
OX   NCBI_TaxID=553198 {ECO:0000313|EMBL:ERK56216.1, ECO:0000313|Proteomes:UP000017052};
RN   [1] {ECO:0000313|EMBL:ERK56216.1, ECO:0000313|Proteomes:UP000017052}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0233 {ECO:0000313|EMBL:ERK56216.1,
RC   ECO:0000313|Proteomes:UP000017052};
RA   Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA   Methe B., Sutton G., Nelson K.E.;
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
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:ERK56216.1}.
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DR   EMBL; ACVN02000161; ERK56216.1; -; Genomic_DNA.
DR   RefSeq; WP_021797406.1; NZ_ACVN02000161.1.
DR   AlphaFoldDB; U2QI90; -.
DR   OrthoDB; 3248271at2; -.
DR   Proteomes; UP000017052; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
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, ECO:0000313|EMBL:ERK56216.1}.
FT   DOMAIN          5..297
FT                   /note="Malonyl-CoA:ACP transacylase (MAT)"
FT                   /evidence="ECO:0000259|SMART:SM00827"
SQ   SEQUENCE   316 AA;  32569 MW;  1FC2DB597D958007 CRC64;
     MLVIVAPGQG AQTPGFLAPW LEIDAFAEGL ARLSEVTGLD LARLGTGADA ETIRDTAVAQ
     PLLMGAGLHA ALVTAPRLDH GLFSLADVAA GHSVGEITAA AGTGVLDPLQ AAVFIRERGR
     GMADASAVEP TGMAAVVAGD PDEVLARIEQ CGLTAANNNG SGQIVAAGTL DRLQALRDDP
     PARARVIPLS VAGAFHTAHM APARPRLAEL AATMTTSDPI TRLLSNRDGE VVASGAEYLE
     RLVAQVTTPV RWDLCMDTMR GLGATGLLEL PPAKTLTGIA KRNLKGVELF SLNTPDQIDE
     ALAFCQGHAG TTAQEV
//
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