ID A3VDR8_9RHOB Unreviewed; 297 AA.
AC A3VDR8;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Malonyl CoA-acyl carrier protein transacylase {ECO:0000256|ARBA:ARBA00018953, ECO:0000256|PIRNR:PIRNR000446};
DE EC=2.3.1.39 {ECO:0000256|ARBA:ARBA00013258, ECO:0000256|PIRNR:PIRNR000446};
GN ORFNames=RB2654_03049 {ECO:0000313|EMBL:EAQ13657.1};
OS Maritimibacter alkaliphilus HTCC2654.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Maritimibacter.
OX NCBI_TaxID=314271 {ECO:0000313|EMBL:EAQ13657.1, ECO:0000313|Proteomes:UP000002931};
RN [1] {ECO:0000313|EMBL:EAQ13657.1, ECO:0000313|Proteomes:UP000002931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2654 {ECO:0000313|EMBL:EAQ13657.1,
RC ECO:0000313|Proteomes:UP000002931};
RX PubMed=20729358; DOI=10.1128/JB.00873-10;
RA Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA Giovannoni S.J.;
RT "Genome sequences of Pelagibaca bermudensis HTCC2601T and Maritimibacter
RT alkaliphilus HTCC2654T, the type strains of two marine Roseobacter
RT genera.";
RL J. Bacteriol. 192:5552-5553(2010).
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 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:EAQ13657.1}.
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DR EMBL; AAMT01000004; EAQ13657.1; -; Genomic_DNA.
DR AlphaFoldDB; A3VDR8; -.
DR STRING; 314271.RB2654_03049; -.
DR eggNOG; COG0331; Bacteria.
DR HOGENOM; CLU_030558_0_1_5; -.
DR Proteomes; UP000002931; 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; 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 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|ARBA:ARBA00023315,
KW ECO:0000256|PIRNR:PIRNR000446};
KW Reference proteome {ECO:0000313|Proteomes:UP000002931};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000446}.
FT DOMAIN 1..284
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
FT ACT_SITE 77
FT /evidence="ECO:0000256|PIRSR:PIRSR000446-1"
FT ACT_SITE 186
FT /evidence="ECO:0000256|PIRSR:PIRSR000446-1"
SQ SEQUENCE 297 AA; 30663 MW; 38E08D198341E6F7 CRC64;
MGRDLAEAYP AARAVFDEVD EALGIKLSNI IWNGEQDELT LTQNAQPALM ATSLAAMRAL
EAEGVTMDAA GFVAGHSLGE YSALAAAGAL TVSDTARLLR TRGEAMQKAV PVGVGAMAAL
LGLDFEAAKA VAEEAAQGEV CQAANDNDPA QVVVSGHKAA VERAVEIAKE KGARRAVMLP
VSAPFHCALM QPAADVMAEA LAGVTINAPA VPVVANVRAE AVSDPDTIRA LLIEQVTGSV
RWRESVAWMA ANGVTETWEI GAGKALTGMI RRIDKSLNTL TIGAPDEVKV AAEQAAG
//
