ID A0A1E8Q7C4_9MYCO Unreviewed; 1837 AA.
AC A0A1E8Q7C4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:OFJ53939.1};
GN ORFNames=BEL07_09610 {ECO:0000313|EMBL:OFJ53939.1};
OS Mycobacterium grossiae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1552759 {ECO:0000313|EMBL:OFJ53939.1, ECO:0000313|Proteomes:UP000178953};
RN [1] {ECO:0000313|EMBL:OFJ53939.1, ECO:0000313|Proteomes:UP000178953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCH {ECO:0000313|EMBL:OFJ53939.1,
RC ECO:0000313|Proteomes:UP000178953};
RA Greninger A.L., Qin X., Jerome K., Vora S., Quinn K.;
RT "genome sequence of Mycobacterium sp. 739 SCH.";
RL Submitted (SEP-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:OFJ53939.1}.
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DR EMBL; MCHX01000018; OFJ53939.1; -; Genomic_DNA.
DR Proteomes; UP000178953; 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 Reference proteome {ECO:0000313|Proteomes:UP000178953};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 29..106
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 125..550
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1270..1347
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1418..1465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1426..1453
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1837 AA; 196107 MW; 20F5402123F974E3 CRC64;
MIMTEPQEPS PVLSEAVAAD AEQPNRTDVS VPEMREWLRN WVANATGQSP DAINENAPLI
ELGLASRDAV AMASDIEDYC GVTVTATMAF RHPTIEALAT VIVEGEPEEE KAADEDWSRE
VDEGRTNIAI VGVGTRFPGD MNTPDEMWQA LLEGRDAITD LPEGRWSEFL AEPRVAERVA
KARVRGGYLS DIKGFDAEFF ALSKMEADNI DPQQRMALEL TWEALEHARI PASSLRGANV
GVFIGSSVND YMFMSVADPA VAHPYAITGN SSAVIANRVS YFYDFRGPSM AIDTACSSSL
VAVHEGIKAL RAGDADVVLA GGVNALITPL VTLGFDEVGG VLAPDGRIKS FSSDADGYAR
SEGGGMVVLK RLEDARRDGD DILAVIAGGA VNHDGRSNGM LAPNPDAQEA VLRKAYKDAG
IDPTTVDYVE AHGTGTILGD PIEADALGRV IGRGRAADRP ALLGAVKSNV GHLESAAGAA
SLAKMALALK NDKLPPSINY AGPNPYIDFD REHLKVNDVV SDWPRYSGHA IAGVSGFGFG
GANAHLVLRE VLPTDLVEPE TEADVAVVTP ANGDAQAVYV GGVRMDEYGE FITDDADDDL
DRPAAAAVDE PELPGLTDEA LRLLETAREK LAAAHAENPP KPIVPLAVSG FLTSRKRSTA
AELADWIESP EGQASSLEAI GRSLSRRNHG RSRAVVLAHD HAEAVKGLRA IAEGKQSPLV
ISADGPVTNG PVWVLAGFGA QHRKMGKDLY LRNEVFAEWI NKVDALIQDE RGYSVVELIL
DDAIDYTNET CEYPIEVVQT VIFAIQIALG ELLKHHGANP GAVVGQSLGE AAAAYFSGGL
SLEDATRTIC SRAHLMGEGE AMLFGEYIRL MALVEYSADE IKTVFSDYPG LEVCVYAAPT
QTVIGGPPEQ IDAIVARAES EGKFARKLQT KGASHTQQMD PLLGELSAEI QGIEPHPLRT
AYYSTVHEGM LVRAGADPIH DVDYWKKGLR HSVYFTHGIR NAVDNGHTTF LELAPNPVAL
MQVGLTTASA GLHDGQLIAT LARKQDEVDS MTTAMANLFV YGHDLDVRTL FPLGADDERD
RATAFANIPP TRFKRKPHWL DARFTGDSSG VVPGNHVATP DGRHVWEYHP RGAVDAKALA
ALVKAAAAQV LPDAALTAYE QRALPTEGAQ LVTTLTRHPG GATVQVHARI EESFTLVYDA
IVTRGGQAST LPTAAPVGAA IAVPAATATE AAPAPVEEEP EDDAAILQDN LTAGAGLAAN
FAKWSPDSGE TIGQRLGTIV GSAMGYEPED LPWEVPLIEL GLDSLMAVRI KNRVEYDFDL
PPIQLTAVRD ANLYAVEKLI QYAIEHRDEV GELAEAQKGQ TAEEIAAAQA ELMGGATTVA
ELEAKLAEAG HPLGDRAADD PSKVAPAQEI TPDSVATDAA LVPPPNVGAG APPPPPSDPL
GPGVPPPPTN PAGPSVEAKQ NAAKAAASVL TQEAVTEALG ADVPPRDAAE RVTFATWAIV
TGKSPGGIFN ELPAIDDAAA EKMAQRLSER ADGIITAEQV QAARTIQDLA TPVREQMDAG
ELDGFVRTIR ARPEGSNRVP VFVFHPAGGS TTVYEPLLKR LPADTPMYGF ERVEGTVEER
AAAYLPKLME IQGNGPYVLV GWSLGGALAY ACAIGLKRAG ADVRFVGLID MVRPGEEVPQ
TKEETRARWD RYALFAQRTF NVEIPEIPYE DLEALDDEGQ VRFVLDAVKE AGVDIPGGII
EHQRTSYLDN RLLETAEIQP YDGHVTLYMA DRYHDDAIFF EPRYAIRQPD GGWGEFVEDL
EIVPIGGEHI QAIDEPYIAK VGAHMSAAVN QIEGESE
//
