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Database: UniProt
Entry: A0A1A3IGS3_9MYCO
LinkDB: A0A1A3IGS3_9MYCO
Original site: A0A1A3IGS3_9MYCO 
ID   A0A1A3IGS3_9MYCO        Unreviewed;      1797 AA.
AC   A0A1A3IGS3;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Polyketide synthase {ECO:0000313|EMBL:OBJ58998.1};
GN   ORFNames=A9W95_11455 {ECO:0000313|EMBL:OBJ58998.1};
OS   Mycobacterium sp. 1423905.2.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1856859 {ECO:0000313|EMBL:OBJ58998.1, ECO:0000313|Proteomes:UP000092291};
RN   [1] {ECO:0000313|Proteomes:UP000092291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1423905.2 {ECO:0000313|Proteomes:UP000092291};
RA   Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Garcia-Basteiro A.,
RA   Lopez-Varela E., Palencia S.;
RL   Submitted (JUN-2016) 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:OBJ58998.1}.
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DR   EMBL; LZLE01000075; OBJ58998.1; -; Genomic_DNA.
DR   RefSeq; WP_067409367.1; NZ_LZLE01000075.1.
DR   OrthoDB; 9778690at2; -.
DR   Proteomes; UP000092291; Unassembled WGS sequence.
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; cd00833; PKS; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 2.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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   InterPro; IPR029058; AB_hydrolase.
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; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR001031; Thioesterase.
DR   InterPro; IPR016039; Thiolase-like.
DR   NCBIfam; NF040607; mycolic_Pks13; 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; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF00550; PP-binding; 2.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 2.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          24..101
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          123..548
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1244..1321
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          558..582
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1354..1415
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1381..1395
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1396..1411
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1797 AA;  193159 MW;  003518A6BC9BD0C8 CRC64;
     MADTDAESPE NSTAPNAPAK QTDMTVPEMR EWMRNWVAKA TGQSADKIDE SVPMVELGLS
     SRDAVAMAAD IEDMTGVTLS VAVAFQHPTI ESLAARIIEG EPEHEDDGSL DNADWSRKGP
     AERVDIAIVG LSTRLPGDMN TPDETWQALL EGRDAITDLP EGRWSEFLEE PRLAARIKSA
     RTRGGYLKDI KGFDSEFFAV AKTEADNIDP QQRLALELTW EALEHARIPA SSLRGEAVGV
     YVGVSNNDYS FLAVSDPTIA HPYAITGTAT SIIANRVSYF YDFRGPSVAV DTACSSSLVA
     MHQAVQALRN GEADVAVAGG VNALITPVVT LGFDEIGQVL SPDGRIKSFS SDADGYTRSE
     GGGMLVLKRV DDARRDGDQI LAVIAGSAVN HDGRSNGLIA PNQDAQADVL RRAYKDAGID
     PRTVDYIEAH GTGTVLGDPI EAEALGRVVG KGRPADRPAL LGAVKTNVGH LESAAGAASM
     AKVVLALQHD KLPPSINYAG PSPYIDFDAM RLKVVDQATD WPRYGGYALA GVSSFGFGGA
     NAHLVVREVL PRDVIEREPE PEAAPQVPVV SAGDDPAEGQ GHSLRFDEFG EIVADDPAAQ
     EEEYELPGVT EEALRLKAAA LEELAAQEPA APLIPLAVSA FLTSRKKAAA AELADWLESP
     EGQASSLESI GRALSRRNHG RSRAVVLAHD HDEAVKGLRA IAEGKQRPGV FSTDGPVTNG
     PVWVLAGFGA QHRKMGKSLY LRNEVFAEWI EKVDALVQDE LGYSVLELIL DDSQDYSIET
     TQVTIFAIQI ALGELLKHHG AKPAAVVGQS LGEAASAYFA GGLSLQDATR TICSRSHLMG
     EGEAMLFGEY IRLMALVEYS AEEIKTVFSD FPNLEVCVYA APTQTVIGGP PDQVDAIIAR
     AESEGKFARK FQTKGASHTT QMDPLLGELA AELQGIKPMS PTAGIYSTVH EGRYIKPGSE
     PIHDVDYWKK GLRHSVYFTQ GIRNAVDSGH TTFLELAPNP VALMQVGLTT AAAGLHDAQL
     IPTLARKQDE VESMVSTMAQ LFVYGHDLDV RTLFTRAQSP QDYANIPPTR FKRKEHWLDA
     HFAGDAAVIM PGTHVALPDG RHVWEYAPRD GEVDLAALVR AAAEQVLSDA QLTAAEQRAV
     PGAGARLVTT MTRHPGGASV QVHARIDESF TLVYDALVTR AGQQSVLPTA VGAGTAVATP
     LATTAAPAAP EQPVDEAAAE TLTDSLTNRY FSASMGKWSP DSGETIAERL GLIVGSAMGY
     EPEDLPWEVP LIELGLDSLM AVRIKNRVEY DFDLPPIQLT AVRDANLYNV EKLIEYAVEH
     RDEVQQLHEH QKTQTAEEIA RAQAELVSGA SAASLVAPAP DPQAEPETQA DPEAESAVPP
     ASDVPIPPPP TNPLGPSGGN GSGNGSAEQR NGTPDLKGAA EALNQEAVAK ALNSDVPPRD
     AAERVTFATW AIVTGKSAGG IFNPLPKLDE ASAAKMAQRL SERAEGPITV EDVLTSKNIE
     ELADKVRGYL EAGVVDGFVR TLRPRQEGST KVPVFVFHPA GGSTVVYEPL LSRLPTDTPM
     YGFERVEGSI EERAEQYVPK LIEMQGDGPY VLVGWSLGGV LAYACAIGLK RLGKDVRFVG
     LIDAVRAGEE IPQTKEEIRK RWERYARFAE KTFNVTIPEI PYEHLEQLDD EGQVRFVLEA
     VSQSGVEIPA GIIEHQRTSY LDNRAIDTAQ IQPYDGHVTL YMADRYHDDA IMFEPRYAVR
     QPDGGWGEYV SDLEVVPIGG EHIQAIDEPI ISKVGAHMTR ALAQVEAEAP ADTSRVR
//
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