THAF_BURTA
ID THAF_BURTA Reviewed; 1154 AA.
AC Q2T4N0;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Polyketide biosynthesis protein ThaF {ECO:0000305};
DE Includes:
DE RecName: Full=Malonyl CoA-acyl carrier protein transacylase;
DE Short=MCT;
DE EC=2.3.1.39 {ECO:0000250|UniProtKB:O34787};
GN Name=thaF {ECO:0000303|PubMed:20853892}; OrderedLocusNames=BTH_II1675;
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS E264).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=20853892; DOI=10.1021/ja105003g;
RA Ishida K., Lincke T., Behnken S., Hertweck C.;
RT "Induced biosynthesis of cryptic polyketide metabolites in a Burkholderia
RT thailandensis quorum sensing mutant.";
RL J. Am. Chem. Soc. 132:13966-13968(2010).
CC -!- FUNCTION: Involved in production of the polyketide antibiotic
CC thailandamide (Probable). Probably has an acyl transferase activity and
CC could also have a flavin mononucleotide-dependent oxidoreductase
CC activity (By similarity). {ECO:0000250|UniProtKB:O34787,
CC ECO:0000305|PubMed:20853892}.
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:0000250|UniProtKB:O34787};
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000305|PubMed:20853892}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: No production of thailandamide antibiotic.
CC {ECO:0000269|PubMed:20853892}.
CC -!- MISCELLANEOUS: Thailandamide is a polyketide that is toxic to human
CC cell lines but also has antibacterial activity on E.coli, S.typhimurium
CC and S.aureus. It probably acts on acetyl-CoA carboxylase in the fatty
CC acid synthesis pathway, which is rarely found to be an antibiotic
CC target. These data suggest it might be a good starting point for
CC engineering of novel antibiotics. {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the FabD family.
CC {ECO:0000305}.
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DR EMBL; CP000085; ABC34740.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2T4N0; -.
DR SMR; Q2T4N0; -.
DR PRIDE; Q2T4N0; -.
DR EnsemblBacteria; ABC34740; ABC34740; BTH_II1675.
DR KEGG; bte:BTH_II1675; -.
DR HOGENOM; CLU_008708_0_0_4; -.
DR OMA; SIRFLMG; -.
DR Proteomes; UP000001930; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0018580; F:nitronate monooxygenase activity; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd04742; NPD_FabD; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.40.366.10; -; 2.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR004410; Malonyl_CoA-ACP_transAc_FabD.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR004136; NMO.
DR InterPro; IPR014179; PfaD_fam.
DR Pfam; PF00698; Acyl_transf_1; 2.
DR Pfam; PF03060; NMO; 1.
DR SMART; SM00827; PKS_AT; 2.
DR SUPFAM; SSF52151; SSF52151; 2.
DR SUPFAM; SSF55048; SSF55048; 1.
DR TIGRFAMs; TIGR00128; fabD; 1.
DR TIGRFAMs; TIGR02814; pfaD_fam; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Antibiotic biosynthesis; Cytoplasm; Transferase.
FT CHAIN 1..1154
FT /note="Polyketide biosynthesis protein ThaF"
FT /id="PRO_0000452504"
FT REGION 330..714
FT /note="Acyl transferase"
FT /evidence="ECO:0000250|UniProtKB:O34787"
FT REGION 627..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..689
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1154 AA; 122962 MW; CFA40416991D9AB8 CRC64;
MFSGQGSQYV GMGRALYESE PTFRHHVDRF DEVTRDKTGT SLVARLYGRD ARAGEPFDDT
HVTHPALFAV QYALARTLQA RGAQPDIVLG SSLGDFVAAA LAQVAPAQEI VAWLIDQAAS
MARACEPGFM LAVLGPASIY RGSDTLREFS DLVGVNYAEH FVIGGNRADL VRVEAALARE
GVVFHRLPVR FGFHSRNVAP VVPWLHAREA NLSCRAPTIP WASCTAGGIV EAPTARFLTR
IAIDPLRFQE AARAIEQTGS PDTLHWVDLG PSGTLANFAR RLGVPNDRLH VVMGPFGDDA
RALGRVSNLH ASNARPAGAP AAPVSEGVSM HAFLFPGQGS QVKGMGAALF ARFPDRMRLA
NEILGYDLAA LCIENPDNRL GQTQFTQPAM YVVNALAYLA RREDDAGAPA FVAGHSLGEY
SALFAAGAFS FEDGLRLVKK RGELMSAARD GGMAAVLGLD EARVAEILAL SDLRGIDIAN
LNAPTQIVIA GPADEIRRAQ QWFEQGGCYA YVVLPVSGAF HSRMMRDAQR EFERFIAPFD
IGAPGIPVIA NVTGRPYRGD EVRRGLVEQI ASPVRWVDTI RYLSEQGVER FAEIGTGTVL
TDLLRKILPQ KAGASGAAAR PQAGAASAVA ASAPPRPTGM ADAQPPAASP ARAATAASTM
PPASASASAS APAPAPAPAP APAPAPAPAP ALAPAFARAP ASTSTNGIAP AARVEQLGCP
EFKRRFGLKY AYVAGGMVHG IASVRMVVAM AKAGMKGYFG TGGLSLDAIR DAVRAIRGAL
PAGEPYGMNL LSGRLEEATV DLYLREGVTS VEAAAYMHVT PALARFKLAG LSVDRDGATV
SAHKILAKVS RPEVATAFMS PIPEKFLERF VRDGVISDAQ ARAARAMPVA DAVCVEADSG
GHTDMGAMPA LLPAIRRLCA DIAGERGYRD KVPVGVAGGI GTPEAAAAAF VLGADFILTG
SINQCTVESG ISDVVKDMLQ QINVHDTDYA PAGDMFELGA KVQVLRRGVF FPARANRLYE
LYKQYDSVDD LPDAVRRQLE DKYFGKSLAE VYADCERYYP ADEIERARGN PKQKLALIFR
WYFGFATRAA LAGNEADKVN FQVQCGPALG AFNQWVRNTA LENWRNRHVA EMAARILQDA
ADLLSRRYLS MVGR
