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Database: UniProt
Entry: L0J6V9_9MYCO
LinkDB: L0J6V9_9MYCO
Original site: L0J6V9_9MYCO 
ID   L0J6V9_9MYCO            Unreviewed;      1801 AA.
AC   L0J6V9;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Polyketide synthase family protein {ECO:0000313|EMBL:AGB26046.1};
GN   ORFNames=Mycsm_05876 {ECO:0000313|EMBL:AGB26046.1};
OS   Mycobacterium sp. JS623.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=212767 {ECO:0000313|EMBL:AGB26046.1, ECO:0000313|Proteomes:UP000010844};
RN   [1] {ECO:0000313|Proteomes:UP000010844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS623 {ECO:0000313|Proteomes:UP000010844};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A., Rutledge P.,
RA   Paulsen I., Coleman N., Woyke T.;
RT   "Complete sequence of chromosome of Mycobacterium smegmatis JS623.";
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP003078; AGB26046.1; -; Genomic_DNA.
DR   RefSeq; WP_015309621.1; NC_019966.1.
DR   STRING; 212767.Mycsm_05876; -.
DR   KEGG; msa:Mycsm_05876; -.
DR   PATRIC; fig|710686.3.peg.5921; -.
DR   HOGENOM; CLU_000022_35_5_11; -.
DR   OrthoDB; 9778690at2; -.
DR   Proteomes; UP000010844; Chromosome.
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   CDD; cd08955; KR_2_FAS_SDR_x; 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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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; 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; 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   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 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; 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; 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   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          33..455
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1688..1763
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1779..1801
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1787..1801
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1801 AA;  190357 MW;  949F59BD83E69A88 CRC64;
     MAATAFSRIA AMTNAQRDAL VDQFGKASRL AAAEPVAVVG IGCRFPCDVV GPERYWTFLA
     DGRDAVGEVP PDRWDADAYY DPDLAAPGRM ASKWGGFLRE IAEFDADFFG ISPREAEAMD
     PQQRVLLEVA FEALEHAGIA TDHLGGIRAA VLMGVYYTEY QGISAANPDA IDAYCATGNA
     HSITVGRIAY TLGLRGPAVA VDTACSSSLV SIHLACQSLR LRESDVALAG GVNLILRPET
     QLALSKWGML SPRGRCRAFD AGADGFVRGE GAGVVVLKRL IDAVSDGDRV LAVVRGSAVN
     QDGRSNGLTA PNALAQQDVI SRALQSADVT ASSVNLIETH GTGTALGDPI EFDALAAVYG
     RGDGPCALGA VKTNFGHLEA AAGIAGFIKA VLALQRSRIP TNLHFTHWNP AIDPVPTRLF
     VPTETTAWPQ CAGPRRAAVS SFGLGGTNAH VVLEQGPDPL SSSRDGESPA VTTLVVSGKT
     SERLASTAAM LADWIEGDGS SVALSAVAET LNHRARYAIC ATVCGRDRGE AVDGLRALAA
     GRSAPGVQER RGESRGPGIV FVYSGQGSQW AGMGRRLLAD EPSFAAAVAE LEPIFVAQCG
     FSLQHVLQAG EPIAGIDHIQ PVLVGIHLAL TQLWRSYGVQ PDAVIGHSMG EVSAAIVSGA
     LTVADGLRVI ATRSRLMARL SGQGAMALLE SDAPATEALI ADHPDVALAV YASPRQTVIA
     GPPDEVDSLI AAVTAQNRLA RRIDVDVASH HPTIDPILPE LLGALADLDP VTPKIPLISA
     TAPAGQPPAF DASYWVANVR NPVRFAQAVA VAAENHSTFI EISPHPLLTH ALTEAIESVR
     PGGNGFVTGT LNRDDDETLT FHTQLVGVQT PTGSTGSRSR LADVPPTPWQ HQRYWLANRP
     TGQMPTGAHL LLGMHVEMPS GHDHVWQADV GTDAVGWLAD HRVHGQPVMP AAGFAEIALA
     AGSEALSLPP AGVAVTRLEV EQMLPLNGET RVTTQLTRSA DDEIRIEIHS RSTGGHWCRH
     AVAQVEATQP SHRAVLANEE ADPGTEVAVG DFYSALRRTG AQHGPAFAAL TRIVRRDNGS
     AETEIALPDT ATAHRGLRIH PVMLDAALQT LAAAMPAETL DASTEVTYLP VSIDRIQLLG
     AVGRRGRCRA ELVSLDDDGA GKLGRITLMD ASGTPTAEIS GVYLRRVERR AVPLPLDQKI
     FDTGWLECPT PARNDVLPAG SWLLLHNDSD SEALADAFAT RLGSPSMRVI TEDLFDEAAV
     LEAFAKTASA PGLPPAGVVI LVGGHLFDGT AAPDALQRTR ELIWAISTTL RAVIGGWHGQ
     SPRLWLVTRS GLAVTKDESG DPGIGALRGL VRVLAYEHPD LHTTLVDVGP ADDAVATVTT
     ELQSPAADDV IAWRGGRRYV ERLRRAALSV AVHDPVVRRD GSYVVTGGLG GLGMVVARWL
     VDRGAGRVVL NGRTPPSDAQ EADLADLRAH TEITFVAGDI ASPGVAEQLV CTAEENGLPL
     RGVMHAAAVI EDALVATLNK ESLGRVWAPK AEGALRLHEA TAHRQLDWWA GFSSVASLLG
     SPGQGAYACA NAWLDALVEW RRTSGLPAIA LNWGQWSEVG VARSLRFGVL DPISPAEGVA
     ALDSLLGSDL VRVGITRLRL DRAAAAFPEI RKLGYFAEMV EELDAIDSGG DWPGVDALRE
     LTPDDVDRIV TERLRQRISA IMGYPDQSAI PGTKPLTEIG MDSLMAVRIR NTLRDDFGVE
     PAVALLLQGA SLGDLANELT QQLGLGSHDD ADRPNALRDR AHQRAAARQR AATRRKVGQR
     V
//
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