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
//