ID Q8KUF5_ACTPA Unreviewed; 1589 AA.
AC Q8KUF5;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:AAM54077.1};
GN Name=asmC {ECO:0000313|EMBL:AAM54077.1};
OS Actinosynnema pretiosum subsp. auranticum.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinosynnema.
OX NCBI_TaxID=42198 {ECO:0000313|EMBL:AAM54077.1};
RN [1] {ECO:0000313|EMBL:AAM54077.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 31565 {ECO:0000313|EMBL:AAM54077.1};
RA Yu T.-W., Bai L., Clade D., Hoffmann D., Toelzer S., Trinh K.Q., Xu J.,
RA Moss S.J., Leistner E., Floss H.G.;
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAM54077.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 31565 {ECO:0000313|EMBL:AAM54077.1};
RX PubMed=12060743; DOI=10.1073/pnas.092697199;
RA Yu T.W., Bai L., Clade D., Hoffmann D., Toelzer S., Trinh K.Q., Xu J.,
RA Moss S.J., Leistner E., Floss H.G.;
RT "The biosynthetic gene cluster of the maytansinoid antitumor agent
RT ansamitocin from Actinosynnema pretiosum.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:7968-7973(2002).
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000256|ARBA:ARBA00004792}.
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DR EMBL; AF453501; AAM54077.1; -; Genomic_DNA.
DR BioCyc; MetaCyc:MONOMER-21916; -.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0033068; P:macrolide biosynthetic process; IEA:UniProt.
DR CDD; cd08952; KR_1_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_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; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR015083; Polyketide_synth_docking.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF51; PHENOLPHTHIOCEROL_PHTHIOCEROL POLYKETIDE SYNTHASE SUBUNIT E; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08990; Docking; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 35..460
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1422..1497
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1589 AA; 164713 MW; 5067CF9A772A525F CRC64;
MTDGTHEKLV DYLRWVTADL HETRRKLADL ESAGHEPIAI TGLACRAPGG VRTPEALWEL
VDGGVDAITG FPTDRGWDLA GLYDPDPTRP GTCYTREGGF LHDAAEFDAG FFGIGPREAV
TIDPQHRMLL ETSWEAVERA GLDPLSLRGT GTGVFSGVVY QNYGNRRRVA EEFEGHLAIG
SSGSVASGRV AYALGLHGPA ITVDTACSSS LVAIHLAAQS LRRGECAMAL AGGATVMPLS
DVFVEFARQR GLSPDGRCKA FSADADGTAW GEGVGVVLLE RLSDARRAGR PVLAVIRGSA
VNSDGASNGL TAPNGAAQQR VIEAALEDAG LRPSDVDLLE AHGTGTRLGD PIEAAALQAT
YGRARPEGRP LLLGSLKSNI GHAQGAAGVL GLVKVVQALR HGVAPRTLHA DRLTPEVDWT
SGALRVLTEP APWPRGERPR RAAVSAFGMS GTNAHLVVEE GDAPSAPGER RPAGALPLLL
SARGGAALRA AAADLVELPG EPVDVCWSLL TGRARLVDRA VVVAADRAGF TAGLEALAAD
RPSAAAVTGR ADVAGRTVLV FPGQGGQWVG MGARLLDESP VFAAAVARCA AAVEPLVDFR
VVDALRGGDL GRVDVVQPVS FVLMVALARL WRSVGVEPDV VVGHSQGEIA AACVAGALSL
EDAARVVVLR SRAIAAEAGG GGMASIPLPR AEVERLITGT GVSVAAVNGP GSVVVSGDVD
PLVARVEGAR RLPVDYASHS PAVDVLRGRL LADLARVTPR PAAIPMLSTV TGKWLDGAEL
DADYWFANLR EPVRFADAVT ELAGADCAAF VEVGAHPVLT AAIQDVLGER TAVVTGTLRR
DDGGLDRFLR SAAALHVRGV PVDWAPVFEG LDARRADLPT YPFQRARHWL QEAEPDARQA
GGDDPLWAAA RDADGLCAEL ELTEPDQRAA LRAVLPALTA WHERRSERAL LDSWRYRITW
RTLPEPPESA PRGDWLVVGP HPDLLADLLP GAALDPGDAD RAALADLLRP HTAVAGVLAT
PGADVLTLVQ ALGDAGATAP LWCATTGAVA ISPHDGPPDP AQAATWGLGR VVALEHPGRW
GGLVDLADPA DPRQRRGLAA VLAGPGVDDG GEDQVAIRAQ GVFARRLVRA EPQAPAAPWT
PRGTVLITGG TGGVAAHVAR RLAALGADHL VLTSRRGPSA PGAPALAADL EALGARVTTA
ACDVADRAAL AALLTGLERA GEQVTAVVHA AGANAQTPVA DTTPEEHARV QAAKALGAEH
LDELLGGRPL DAFVLFSSNA GVWGSGGQCA YAAANARLDA LAQRRRAHGR VATSVAWGAW
DGGGMSSATP DIAAQLAQAG LRLMPPDLAV SALLDAVARD ESTTVVTDVR WEAFAARFTA
LRRSPLLADL PEARPEPVAA TAEPDRGLAG ELAALPAPER LRRLTDLVRA HAAAALGHPG
PESVPADVAF RDLGVDSLAA VELRNRACAA TGAKLTPTAV FDHPTPRALA EHLAEHLAAA
RDSAAPDAAP DAEDPTSALR DLDALAAALP AAAGDDALRE RVTARLREVL GRWEELTGGP
GGPDDLDLDH ISDDELFRLA DSRLGPTGA
//
