ID   B1Y601_LEPCP            Unreviewed;       307 AA.
AC   B1Y601;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=[acyl-carrier-protein] S-malonyltransferase {ECO:0000256|ARBA:ARBA00013258};
DE            EC=2.3.1.39 {ECO:0000256|ARBA:ARBA00013258};
GN   OrderedLocusNames=Lcho_0073 {ECO:0000313|EMBL:ACB32348.1};
OS   Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS   discophora (strain SP-6)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Leptothrix.
OX   NCBI_TaxID=395495 {ECO:0000313|EMBL:ACB32348.1, ECO:0000313|Proteomes:UP000001693};
RN   [1] {ECO:0000313|EMBL:ACB32348.1, ECO:0000313|Proteomes:UP000001693}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51168 / LMG 8142 / SP-6
RC   {ECO:0000313|Proteomes:UP000001693};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT   "Complete sequence of Leptothrix cholodnii SP-6.";
RL   Submitted (MAR-2008) 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};
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DR   EMBL; CP001013; ACB32348.1; -; Genomic_DNA.
DR   RefSeq; WP_012345110.1; NC_010524.1.
DR   AlphaFoldDB; B1Y601; -.
DR   STRING; 395495.Lcho_0073; -.
DR   KEGG; lch:Lcho_0073; -.
DR   eggNOG; COG0331; Bacteria.
DR   HOGENOM; CLU_030558_4_0_4; -.
DR   OrthoDB; 9808564at2; -.
DR   Proteomes; UP000001693; Chromosome.
DR   GO; GO:0016740; F:transferase 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   PANTHER; PTHR42681:SF6; BLL0263 PROTEIN; 1.
DR   PANTHER; PTHR42681; 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.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001693};
KW   Transferase {ECO:0000313|EMBL:ACB32348.1}.
FT   DOMAIN          6..303
FT                   /note="Malonyl-CoA:ACP transacylase (MAT)"
FT                   /evidence="ECO:0000259|SMART:SM00827"
SQ   SEQUENCE   307 AA;  32255 MW;  2428D69A31EC7EA2 CRC64;
     MTLGLLFPGQ GTQHPDMLPW LGHGCAPLPA LALLESRLGA DWRNRLADSA WATRNEVAQT
     LLTGLSLAAW QQLQPLLPAP AVVAGYSVGE LAAFSAAGVF GADDALAMAS LRARLMDECV
     QGQPTGLLSI SGAAPGAIDD LCRRHALAVA IRIGADRVIV GGLRSDLQAA EDEAGAAGAS
     CTRLAVSIAS HTPWMAAGVP RLAEALAARP FERPRVALVC NHTGTTLRTV DALRQALAAQ
     IAATVPWDRC MDTVAERRVR CVLEVGPGNT LARMWNARHP AIPARSVDEF QAPDAAARWV
     HEALGTD
//