ID K4LHZ8_THEPS Unreviewed; 311 AA.
AC K4LHZ8;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Malonyl CoA-acyl carrier protein transacylase {ECO:0000256|PIRNR:PIRNR000446};
DE EC=2.3.1.39 {ECO:0000256|PIRNR:PIRNR000446};
GN Name=fabD {ECO:0000313|EMBL:AFV11590.1};
GN OrderedLocusNames=Tph_c13740 {ECO:0000313|EMBL:AFV11590.1};
OS Thermacetogenium phaeum (strain ATCC BAA-254 / DSM 26808 / PB).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermacetogenium.
OX NCBI_TaxID=1089553 {ECO:0000313|EMBL:AFV11590.1, ECO:0000313|Proteomes:UP000000467};
RN [1] {ECO:0000313|EMBL:AFV11590.1, ECO:0000313|Proteomes:UP000000467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-254 / DSM 26808 / PB
RC {ECO:0000313|Proteomes:UP000000467};
RX PubMed=23259483; DOI=10.1186/1471-2164-13-723;
RA Oehler D., Poehlein A., Leimbach A., Muller N., Daniel R., Gottschalk G.,
RA Schink B.;
RT "Genome-guided analysis of physiological and morphological traits of the
RT fermentative acetate oxidizer Thermacetogenium phaeum.";
RL BMC Genomics 13:723-723(2012).
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; CP003732; AFV11590.1; -; Genomic_DNA.
DR RefSeq; WP_015050471.1; NZ_KI912609.1.
DR AlphaFoldDB; K4LHZ8; -.
DR STRING; 1089553.Tph_c13740; -.
DR KEGG; tpz:Tph_c13740; -.
DR eggNOG; COG0331; Bacteria.
DR HOGENOM; CLU_030558_0_1_9; -.
DR OrthoDB; 9805460at2; -.
DR Proteomes; UP000000467; 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; 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:UP000000467};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000446}.
FT DOMAIN 7..310
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
FT ACT_SITE 91
FT /evidence="ECO:0000256|PIRSR:PIRSR000446-1"
FT ACT_SITE 199
FT /evidence="ECO:0000256|PIRSR:PIRSR000446-1"
SQ SEQUENCE 311 AA; 33637 MW; A7A56ACEF26D90EE CRC64;
MLRLAFVFPG QGAQFVGMGK DLAEEFNEVR KVYDLADEVM GFPLSKICFE GPPEVLNKTE
ITQPAVLTTS IAIYELLRDH GINPVMAAGL SLGEYSALVS SGVLRFEDAL RIVSRRGRIM
QEAVPEGKGM MAAVLGLDNA TIERTCQEAA CKGIVNIANY NCPGQIVISG EREAVLEAIK
LLKDKGAKAV PLAVSVPSHS RLMEGAAAAL RKELNGINWS SPAFPVISNT EAREIQPSDL
PEILVKQIYS PIKWEQSVIL MADKIDFFLE VGPGKVLSGL IKKTARSKPV GNVGDTASFK
RTLAQLKEAE Q
//
