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Database: UniProt
Entry: W5WAK1_9PSEU
LinkDB: W5WAK1_9PSEU
Original site: W5WAK1_9PSEU 
ID   W5WAK1_9PSEU            Unreviewed;       313 AA.
AC   W5WAK1;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=[acyl-carrier-protein] S-malonyltransferase {ECO:0000256|ARBA:ARBA00013258};
DE            EC=2.3.1.39 {ECO:0000256|ARBA:ARBA00013258};
GN   ORFNames=KALB_1843 {ECO:0000313|EMBL:AHH95214.1};
OS   Kutzneria albida DSM 43870.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Kutzneria.
OX   NCBI_TaxID=1449976 {ECO:0000313|EMBL:AHH95214.1, ECO:0000313|Proteomes:UP000019225};
RN   [1] {ECO:0000313|EMBL:AHH95214.1, ECO:0000313|Proteomes:UP000019225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43870 {ECO:0000313|EMBL:AHH95214.1};
RX   PubMed=25301375; DOI=10.1186/1471-2164-15-885;
RA   Rebets Y., Tokovenko B., Lushchyk I., Ruckert C., Zaburannyi N.,
RA   Bechthold A., Kalinowski J., Luzhetskyy A.;
RT   "Complete genome sequence of producer of the glycopeptide antibiotic
RT   Aculeximycin Kutzneria albida DSM 43870T, a representative of minor genus
RT   of Pseudonocardiaceae.";
RL   BMC Genomics 15:885-885(2014).
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; CP007155; AHH95214.1; -; Genomic_DNA.
DR   AlphaFoldDB; W5WAK1; -.
DR   STRING; 1449976.KALB_1843; -.
DR   KEGG; kal:KALB_1843; -.
DR   PATRIC; fig|1449976.3.peg.1841; -.
DR   eggNOG; COG0331; Bacteria.
DR   HOGENOM; CLU_030558_1_2_11; -.
DR   OrthoDB; 3248271at2; -.
DR   Proteomes; UP000019225; Chromosome.
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; 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   ECO:0000313|EMBL:AHH95214.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019225};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AHH95214.1}.
FT   DOMAIN          12..313
FT                   /note="Malonyl-CoA:ACP transacylase (MAT)"
FT                   /evidence="ECO:0000259|SMART:SM00827"
SQ   SEQUENCE   313 AA;  32529 MW;  B7934B15152AE057 CRC64;
     MTVFSERVIA LLAPGQGSQA PGMLTPWLEL DGVEQLVRGW SQATGLDLLR LGTTAEAEEI
     KDTAITQPLI VAMSLLAHRE LVKRVELPEG TPVAGHSVGE LAAAAIAGVL SADDAVALAA
     VRGAAMARAC ALESTGMAAV MGGNAEELLA RLDDYGLTPA NRNGAGQTVA AGSVEALRKL
     SEDRPAGTKV VMLKVAGAFH THYMEPARVE LAERAAQVST ADPVLPLLSN ADGAVVTSGA
     EMLRRLVAQV TLPVRWDLCM DSLAELGVTT TVELPPAGAL TGLVKRQLKD VVTQPLACKT
     PADLDRVLEA VRA
//
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