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Database: UniProt
Entry: Q20XM7_RHOPB
LinkDB: Q20XM7_RHOPB
Original site: Q20XM7_RHOPB 
ID   Q20XM7_RHOPB            Unreviewed;       311 AA.
AC   Q20XM7;
DT   18-APR-2006, integrated into UniProtKB/TrEMBL.
DT   18-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 88.
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   OrderedLocusNames=RPC_4587 {ECO:0000313|EMBL:ABD90109.1};
OS   Rhodopseudomonas palustris (strain BisB18).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=316056 {ECO:0000313|EMBL:ABD90109.1};
RN   [1] {ECO:0000313|EMBL:ABD90109.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB18 {ECO:0000313|EMBL:ABD90109.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL   Submitted (MAR-2006) 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         ECO:0000256|PIRNR:PIRNR000446};
CC   -!- SIMILARITY: Belongs to the fabD family.
CC       {ECO:0000256|PIRNR:PIRNR000446}.
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DR   EMBL; CP000301; ABD90109.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q20XM7; -.
DR   STRING; 316056.RPC_4587; -.
DR   KEGG; rpc:RPC_4587; -.
DR   eggNOG; COG0331; Bacteria.
DR   HOGENOM; CLU_030558_4_1_5; -.
DR   OrthoDB; 9808564at2; -.
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; IPR017554; Malonate_deCOase_MdcHsu.
DR   InterPro; IPR024925; Malonyl_CoA-ACP_transAc.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   NCBIfam; TIGR03131; malonate_mdcH; 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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000446}.
FT   DOMAIN          6..306
FT                   /note="Malonyl-CoA:ACP transacylase (MAT)"
FT                   /evidence="ECO:0000259|SMART:SM00827"
FT   ACT_SITE        86
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000446-1"
FT   ACT_SITE        195
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000446-1"
SQ   SEQUENCE   311 AA;  33076 MW;  0143CBE0285E5672 CRC64;
     MSIAFLFPGQ GSQRAGMLHE LPAHPSVALT IDEASQVLGR NVLELDEEKI LESTVSTQVA
     IYVAGVAVAR ALAAEGALPS AVAGLSVGAY AAATACGALA FPDGLRLVHL RASLMEQQFT
     TGYGLAAIVG LDEEQVTALV AKATTEQFPV YVGNLNAPRQ IVVAGALPGV DRVVELAIAT
     GCKKAERLAV RVPSHCPLLQ GVADVLLDKL KTLEPGTVRA QYMTNRRARP TRVLDRIRED
     VATNIAHPVR WHDSTEILVG LGTTLFVEIN PGQVLSKLTT EAFPQVPSIA MVAMPFDYAV
     RQIRDAMEVL D
//
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