ID H8IKP0_MYCIA Unreviewed; 1773 AA.
AC H8IKP0;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:AFC41447.1};
GN OrderedLocusNames=OCU_02270 {ECO:0000313|EMBL:AFC41447.1};
OS Mycobacterium intracellulare (strain ATCC 13950 / DSM 43223 / JCM 6384 /
OS NCTC 13025 / 3600).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=487521 {ECO:0000313|EMBL:AFC41447.1, ECO:0000313|Proteomes:UP000008004};
RN [1] {ECO:0000313|EMBL:AFC41447.1, ECO:0000313|Proteomes:UP000008004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13950 / DSM 43223 / JCM 6384 / NCTC 13025 / 3600
RC {ECO:0000313|Proteomes:UP000008004};
RX PubMed=22535933; DOI=10.1128/JB.00295-12;
RA Kim B.J., Choi B.S., Lim J.S., Choi I.Y., Lee J.H., Chun J., Kook Y.H.,
RA Kim B.J.;
RT "Complete genome sequence of Mycobacterium intracellulare strain ATCC
RT 13950T.";
RL J. Bacteriol. 194:2750-2750(2012).
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DR EMBL; CP003322; AFC41447.1; -; Genomic_DNA.
DR RefSeq; WP_014378853.1; NZ_CP076382.1.
DR KEGG; mia:OCU_02270; -.
DR PATRIC; fig|487521.10.peg.229; -.
DR eggNOG; COG0236; Bacteria.
DR eggNOG; COG3319; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_26_1_11; -.
DR Proteomes; UP000008004; Chromosome.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:UniProt.
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; 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; 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 21..98
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 119..544
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1242..1319
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1351..1394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1361..1386
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1773 AA; 190583 MW; EB80FCCC079F308A CRC64;
MADTEHPEST DHPPAAKGTD MTVPEMRQWL RNWVGKAVGR SPDDIDESVP MVELGLSSRD
AVAMAADIED MTGVTLSVAV AFQHPTIESL ATRIVEGEPE IDTAADDAMD WTRTGPAERV
DIAIVGLSTR LPGDMNSPDE TWQALMEGRD AITDLPEGRW SEFLDEPRIA ARVGAARTRG
GYLKDIKGFD SEFFAVAKTE ADNIDPQQRM ALELTWEALE HARIPASSLR GEAVGVYVGF
SNNDYQFLAV SDPTVAHPYA ITGTASSIIA NRVSYFYDFR GPSVALDTAC SSSLVATHQA
VQALRNGECD VAVAGGVNAL LTPLVTLGFD EIGQVLSPDG RIKSFSSDAD GYTRSEGGGM
FVLKRVDDAR RDGDQILAVI AGSAVNHDGR SNGLIAPNQD AQAEVLRRAY KDAGIDPRTV
DYIEAHGTGT VLGDPIEAEA LGRIVGRGRP ADRPALLGAV KTNVGHLESA AGAASLAKVV
LALQHDKLPP SINFAGPSPY IDFDGMHLKV VDSATDWPRY GGYALAGVSS FGFGGANAHL
VVREVLPRDV VEREPEPAPQ AEAAAAAEAA EAPTLEAHSL RFDDFGNIIP DAEAPDEEED
YELPGVTEEA LRLKAIALEE LAAQEEAEPT RPLIPLAVSG FLTSRKKAAA AELADWMESP
EGQASSLESI GRALSRRNHG RSRAVVLAHD HEEAVKGLRA VAEGKQRPNV FSVDGPVTSG
PVWAMAGFGA QHRKMGKNLY LRNAVFAEWI EKVDALIQDE RGYSVLELIL DDSHEYGIET
SNVVIFAIQI ALGELLKHHG AKPAAVVGQS LGEPASAYFA GGLSLRDAAR VIASRSHLMG
EGEAMLFGEY IRFMALVEYS ADELKTVFAD FPGLEVCVYA APSQTVIGGP PEQIDAIVAR
AESEGRFARK LQTKGAGHTS QMDPLLGEFS AELQGIKPMS PTVGIFSTVH EGSYIKPGGE
PIHDVAYWVK GMRHSVYFTH GVRNAVDSGH TTFLELAPNP VALMQIGLTT AAAGLHDAQL
IPTLAKKQDD VESMISAMAQ LYVHGHELDI RTLFTRAQGP EDYANIPPTR FKRKEHWLDV
HFSGDGSVIM PGTHVALPDG RHVWEYAPRN GETDLAALVR SAATQVLSDA QLVASEQRAV
PGAGARLVTT MTRHPGGASV QVHARIDESF TLVYDALVSR AGQSVAALPT AVGAGAAIAA
PVTDGPVAEA PAEETDAETL SDSLTNRYLP SSVGRWSPDS GETIGERLGL IVSAAMGYEP
EDLPWEVPLI ELGLDSLMAV RIKNRVEYDF DLPPIQLTAV RDANLYNIET LIQYAVEHRD
EVEQLHEHQK TLTADEIAQE QARLLSGATV DSVTAPAPDP QAEPQTQPAP PSSDAPIPPP
PTDPSGPSGN GATANLAGAL SQEAVSKALN SDVPPRDAAE RVTFATWAIV TGKSPGGIFN
PLPKLDEDTA AKMAQRLSER ADGTITAEDV LTSETIEELA EKVRQYLEAG QIDGFVRTIR
APENDSQIPV FVFHPAGGST VVYEPLLNRL PAGTPMYGLE RVEGTIQERA AQYVPKLLEM
NDGKPFILAG WSLGGALAYA CAIGLKRAGA DVRFVGMIDT VRPGEEIPQT KEETRKRWDR
YARFAERTFN VEIPAIPYEQ LEELDDEGQV KFVLDIVQQS GVQIPGGIVE HQRTSYLDNR
ALETVVIEPY DGHVTLYMAD RYHDDVIEFE PRYAIRQPDG GWGEYVADLE VVPIGGEHIQ
AIDEPIIGKV GAHLTEVLNK VDAESTQTSE VGK
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