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Database: UniProt
Entry: B8MLT4_TALSN
LinkDB: B8MLT4_TALSN
Original site: B8MLT4_TALSN 
ID   B8MLT4_TALSN            Unreviewed;      1002 AA.
AC   B8MLT4;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Polyketide synthase, putative {ECO:0000313|EMBL:EED13801.1};
DE            EC=2.3.1.94 {ECO:0000313|EMBL:EED13801.1};
GN   ORFNames=TSTA_100460 {ECO:0000313|EMBL:EED13801.1};
OS   Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS   1006) (Penicillium stipitatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441959 {ECO:0000313|EMBL:EED13801.1, ECO:0000313|Proteomes:UP000001745};
RN   [1] {ECO:0000313|Proteomes:UP000001745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC   {ECO:0000313|Proteomes:UP000001745};
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
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DR   EMBL; EQ962658; EED13801.1; -; Genomic_DNA.
DR   RefSeq; XP_002486039.1; XM_002485994.1.
DR   AlphaFoldDB; B8MLT4; -.
DR   STRING; 441959.B8MLT4; -.
DR   GeneID; 8097930; -.
DR   VEuPathDB; FungiDB:TSTA_100460; -.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_16_8_1; -.
DR   InParanoid; B8MLT4; -.
DR   OMA; WSENTEI; -.
DR   OrthoDB; 5396558at2759; -.
DR   PhylomeDB; B8MLT4; -.
DR   Proteomes; UP000001745; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0047879; F:erythronolide synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
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; 2.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR032088; SAT.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775:SF53; ATROCHRYSONE CARBOXYLIC ACID SYNTHASE-RELATED; 1.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF16073; SAT; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000313|EMBL:EED13801.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001745};
KW   Transferase {ECO:0000313|EMBL:EED13801.1}.
FT   DOMAIN          395..778
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
SQ   SEQUENCE   1002 AA;  109366 MW;  F711F54634418ACF CRC64;
     MLIFTPTTTS DSDLDSRKMK LVYFSNEFPR DDLQNFNDKH HSHLAQFICE ATWAIKEEAR
     NLPTELKKLI PPFKTLVSWS ENTEIREGLI CGAVDGVLLV VVQIATYIGY AENSPEELTD
     FPNLNLAGLG IGLLASTAVS LSSTLADLPL AGADAVRLAF RLGIHVLDVS ENLEARDLSE
     SPDTWAYVVH NIDPDIVRKE LDTLYLRDEI PGTGKIFVSA VSRTSVTVSG PPARLKALFN
     KSDFFRESTF IALPVYGGLC HAPHIYDMHD TQSIVDQNSL LTVRTKSWPG APIYSTSTSV
     TYPAKKDTEL FESVISEILT QAIYWDRVIS GVVERVKTTV TSEVALYSFG NSIPLNDLNS
     ALKSSITHSN VSISNLTTFV TQVAPKDTTP RSTSQSKLAI VGMSCRLPGG ATNTEKGLDV
     SRKIPADRFD IETHYDPAEK ELNKTMTQYG CFIGEPGLFD APFFNISPRE SQVTDSQMRL
     VLITAYEALE RAGYIGNCTA STQLQRIGTF YGQAADDYRE INQGQEVSTY YIPGGCGVLG
     PGRINYFFKF AGPSYSIDTA CSSGLAAIEV TCQALWNGEV DTAVTGGVNV LTNPDGFSGL
     CNGHFLTKGY NACKTWDTTT DGYCRADGIG SLAIKRLEDA EADNDNILGV ILGAGTNHSA
     EAVSITHPHA GHQAYLSRQV LRQAGVDPLD VSYIEIHGTG IQAGDHEEMQ GIMDVYAPLT
     RRRSKDQPLK YWRRKSKSLI KVLLMLQKNA VPPHIGIKTE INPKFEIDPR KTHIIAISAK
     VKTSLTGNID RLIGYLDSHP NTNSADLSYT TTARRYHHTH RVAIATSDVA HLKRQLSSSL
     DKVDLINPVG MSGPPLVAFS FTGQGASYKS MSLELYRGVP TFRKHIQYLE SLGQGQGFPS
     FIAALDASYP NEHAHSAVIT QLALVCTEIA LAKHWATLGV KPDVVLGHSL GEYAAIHTAG
     VITASDAIFM VGRRAQMLEE KCKVGSYIMM AVRASVAEIV ES
//
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