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Database: UniProt
Entry: A0A0E9LWU0_9BACT
LinkDB: A0A0E9LWU0_9BACT
Original site: A0A0E9LWU0_9BACT 
ID   A0A0E9LWU0_9BACT        Unreviewed;       283 AA.
AC   A0A0E9LWU0;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Malonyl CoA-acyl carrier protein transacylase {ECO:0000256|PIRNR:PIRNR000446};
DE            EC=2.3.1.39 {ECO:0000256|PIRNR:PIRNR000446};
GN   ORFNames=JCM15548_12269 {ECO:0000313|EMBL:GAO30027.1};
OS   Geofilum rubicundum JCM 15548.
OC   Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinilabiliaceae;
OC   Geofilum.
OX   NCBI_TaxID=1236989 {ECO:0000313|EMBL:GAO30027.1, ECO:0000313|Proteomes:UP000032900};
RN   [1] {ECO:0000313|EMBL:GAO30027.1, ECO:0000313|Proteomes:UP000032900}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 15548 {ECO:0000313|EMBL:GAO30027.1};
RX   PubMed=25736980;
RA   Inoue J., Oshima K., Suda W., Sakamoto M., Iino T., Noda S., Hongoh Y.,
RA   Hattori M., Ohkuma M.;
RT   "Distribution and evolution of nitrogen fixation genes in the phylum
RT   bacteroidetes.";
RL   Microbes Environ. 30:44-50(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|PIRNR:PIRNR000446};
CC   -!- SIMILARITY: Belongs to the fabD family.
CC       {ECO:0000256|PIRNR:PIRNR000446}.
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:GAO30027.1}.
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DR   EMBL; BAZW01000016; GAO30027.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0E9LWU0; -.
DR   STRING; 1236989.JCM15548_12269; -.
DR   Proteomes; UP000032900; Unassembled WGS sequence.
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; IPR024925; Malonyl_CoA-ACP_transAc.
DR   InterPro; IPR004410; Malonyl_CoA-ACP_transAc_FabD.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   NCBIfam; TIGR00128; fabD; 1.
DR   PANTHER; PTHR47170; MALONYL-COA ACP TRANSACYLASE, ACP-BINDING; 1.
DR   PANTHER; PTHR47170:SF2; PKS_AT DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   PIRSF; PIRSF000446; Mct; 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   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|PIRNR:PIRNR000446};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032900};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000446}.
FT   DOMAIN          1..283
FT                   /note="Malonyl-CoA:ACP transacylase (MAT)"
FT                   /evidence="ECO:0000259|SMART:SM00827"
FT   ACT_SITE        75
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000446-1"
FT   ACT_SITE        182
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000446-1"
SQ   SEQUENCE   283 AA;  30372 MW;  5A02C32162BD131D CRC64;
     MGMGKDLYEQ SPMAKELFEK ANDILGFRIT DLMFEGTEED LRQTKVTQPA IFLHSVILAK
     TLGDGFKPNM TAGHSLGEFS ALVTAGALSF EDGLKLVSQR AQAMQKACEM EPSTMAAIVG
     LDDQVVEEAC KNIDAVVVPA NYNCPGQLVI SGSFEGIDQA CEKLTELGAK RALKLSVGGA
     FHSPLMEPAR AELAAAIENT AINTPVCPVY QNVSGRPFTN PAEIKENLIA QLTAPVKWTQ
     TVQNMLADGA NHFTEIGPGK VLTGLIKKIN RQAECENISA FQG
//
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