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Database: UniProt
Entry: A0A1X2LU25_9MYCO
LinkDB: A0A1X2LU25_9MYCO
Original site: A0A1X2LU25_9MYCO 
ID   A0A1X2LU25_9MYCO        Unreviewed;      2111 AA.
AC   A0A1X2LU25;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Polyketide synthase {ECO:0000313|EMBL:OSC40418.1};
GN   ORFNames=B8W66_12895 {ECO:0000313|EMBL:OSC40418.1};
OS   Mycobacterium decipiens.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1430326 {ECO:0000313|EMBL:OSC40418.1, ECO:0000313|Proteomes:UP000193247};
RN   [1] {ECO:0000313|EMBL:OSC40418.1, ECO:0000313|Proteomes:UP000193247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TBL 1200985 {ECO:0000313|EMBL:OSC40418.1,
RC   ECO:0000313|Proteomes:UP000193247};
RA   Tortoli E., Trovato A., Cirillo D.M.;
RT   "The new phylogeny of genus Mycobacterium.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OSC40418.1}.
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DR   EMBL; NCXP01000014; OSC40418.1; -; Genomic_DNA.
DR   STRING; 1430326.B8W66_12895; -.
DR   OrthoDB; 9778690at2; -.
DR   Proteomes; UP000193247; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   CDD; cd05195; enoyl_red; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 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; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 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; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR011032; GroES-like_sf.
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; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020807; PKS_DH.
DR   InterPro; IPR049551; PKS_DH_C.
DR   InterPro; IPR049552; PKS_DH_N.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR016039; Thiolase-like.
DR   NCBIfam; NF041183; Pks2_ls1_myc; 1.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 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; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          5..428
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2025..2100
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   2111 AA;  223622 MW;  A978B504A92FD1BC CRC64;
     METRVTPIAV IGMGCRLPGG IDSPDKLWES LVRGDNLVTE VPADRWDADD YYDPEPGVPG
     RSVSRWGGFL DDVAGFDAEF FGVSEREATS IDPQQRLLLE TSWEAIEHAG LDPASLAGSS
     TAVFTGLTHE DYLVLTTAAG GLASPYVVTG LNNSVASGRI AHALGLHGPA MTFDTACSSG
     LMAVHLACRS LHDGESDLAL AGGCAVLLEP HASVAASAQG MLSSSGRCQS FDADADGFVR
     SEGAAMVLLK RLPDALRDGN RIFAVVRGTA ANQDGGTETL MMPSEDAQVA VYRAALATAG
     VAPETVGVVE AHGTGTPIGD PIEYRGLAQV YGAGTPCALG SAKSNMGHST ASAGTVGLIK
     AILSLRHGVV PPLLHFKKLP DELADIETGL FVPQAVTPWP NGDEHTPKRV AVSSFGMSGT
     NVHAIVEEAP AEASAPETST GDATAGRRLF MVSSTSSDAL RQTARRLATW VEDRQDSVTP
     SDLAYTLARG RAHRPVRTAV VAADLPELIE GLREVADGDA LYDAAVGQGD RGPVWVFSGQ
     GSQWAAMGEQ LLASEPVFAA TIAKLEPVIA AESGFSVTEA ITASETVTGI DKVQPAVFAV
     QVALAATMEQ TYAVRPGAVI GHSMGESAAA VVAGALSLED AARVICRRSK LMTRIAGGGA
     MGSVELPAKQ VNSELMARGI EDVVVSVVAS PQSTVIGGAT DTVRDLIARW EQRDVMAREV
     AVDVASHSPQ VDPILDELAA ALADIAPMTP KVAYYSATLF DPRERPVCNA TYWVENLRNT
     VQFAAAVQAA MEDGYRVFAE LSPHPLLTHA VEQTARGLDM SVAALAGMRR EQPLPHGLRG
     LLTDLHSAGA GLDYSALYPA GRLLDAPLPV WTHAHLFIDT DGQEQRAQGA CTVTVHPLLG
     SHVRLLEEPE RHIWQGDVGT SALSWLADHQ VHNVAALPGA AYCEMALAAA VEVFGEAAEV
     RDIAFEQMLL LDEATPIDAI ASVDAPGVVN FMVQANSDGE KTRNATATLH AAADDDCPPP
     AYDIAALLEA HPSSVNGTDM RESFAQRGVA LGPAFAGLAT ARTPEEEAGT VLAEVALPAS
     IRFQQSAYHI HPALLDACFQ SVGAGVDAAK AAGKGGLLLP LGVGRLRVYG PTRNARYCYT
     RLTKVGATGG EADLDVLDEH GTVLLAVRGL HMGTGTSESG ERDRQFSERL LTLGWQQRTL
     PEVSHAEAGS WLLIDASNAA DTPDMLASAL TDALKSHGPQ GTECASLSWS IQDAPPNNPT
     GLEKLGSQLR GRDGVVILFG PRGGDPDEQG LLAGREQVRH LVRITRELAE LEGELPRLFV
     VTRQAQVVKS HDSGERANLE QAGLRGLLRV ISSEHPMLRT TLVDVDEHTD VERVAQQLLS
     GSEEDETAWR NGDWYVARLT PSPLGHEERR TAVLDPEQDG MRLHVRRPGD LQTLEFVASD
     RVPPGPGQLE VAVSMSSINF ADVLIAFGRF PIIDDREPQL GMDFVGVVTA VGEGVTGHQV
     GDRVGGFSEG GCWRTFLTCD ANLAATLPPG LTDEQAIAAA TAHATAWYGL NDLAQIKAGD
     KVLIHSATGG VGQAAISIAR AKGAEIFATA GNPAKRAMLH DMGIEHVYDS RSVEFAEQIR
     NDTDGYGVDI VLNSLTGAAQ RAGLELLAFG GRFVEIGKAD VYGNTRLGLF PFRRGLTFYY
     LDLALMSVTQ PDRVRELLTT VYKLTADGVL TAPECTHYPL ADAANAIRAM SNAEHTGKLV
     LDIPRSGSRS VVVPPEQAPV YRRDGSYIIT GGLGGLGLFF ASKLAEGGCG RIVLTARSQP
     NPKARQTIER LRAAGADIVV ECGNIAEPDT AQRLVSAATA TGLPLRGVLH SAAVVEDATL
     TNITDELIDR DWSPKVYGSW NLHRATIGQP LDWFCLFSSG AALLGSPGQG AYAAANNWVD
     VFAHWRRAQG LPVTAIAWGA WGEVGRATFL AEGGEIMITP DEGAYAFETL VRHDRAYSGY
     IPILGAPWLA DLVRRSPWGE MFASTGQGSR GPSKFRMELV ALPQDEWAGR LRRLLVEQAS
     VILRRTIDAD RSFIEYGLDS LGMLEMRTHV ETETGIRLTP KVIATNNTAR ALAQHLADTL
     AEEEAAAPAA S
//
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