ID A0A2A7N2B7_MYCAG Unreviewed; 1789 AA.
AC A0A2A7N2B7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:PEG37907.1};
GN ORFNames=CQY20_14390 {ECO:0000313|EMBL:PEG37907.1};
OS Mycolicibacterium agri (Mycobacterium agri).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=36811 {ECO:0000313|EMBL:PEG37907.1, ECO:0000313|Proteomes:UP000220914};
RN [1] {ECO:0000313|EMBL:PEG37907.1, ECO:0000313|Proteomes:UP000220914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG37673 {ECO:0000313|EMBL:PEG37907.1,
RC ECO:0000313|Proteomes:UP000220914};
RA Tortoli E., Trovato A., Cirillo D.M.;
RT "The new phylogeny of genus Mycobacterium.";
RL Submitted (OCT-2017) 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:PEG37907.1}.
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DR EMBL; PDCP01000023; PEG37907.1; -; Genomic_DNA.
DR Proteomes; UP000220914; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000220914};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 32..454
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1696..1771
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1789 AA; 189841 MW; 8C6F2C560B7D8EDB CRC64;
MRTTFSRISD MTAAQRAALD DQFEKASRLA AAEPIAVIGI GCRFPGGSVG PQAYWEFLAD
GGDAIGEVPS DRWDVEEFYD PDPFSPGRMS SKWAGFLPDV SGFDADHFGI SPREAETMDP
QQRLLLEVAW EALEHGGFAP EAMGGSRTAV MMGVYYTEYQ TASAANPDAI DAYCATGNAH
SITVGRIAYL LGLHGPAVAV DTACSSSLVA VHLACQSLRM RESDVALAGG VNLILRPETQ
LALSKWGMLS PHGHCRSFDA GADGFVRGEG AGVVVLKRLT DAVCDGDRVL AVVRGSAVNQ
DGRSNGLTAP NALAQHDVIT RALRGADVAA GSVNFVEAHG TGTALGDPIE FDALSATYGQ
GNGPCAVGAV KTNMGHLEGA AGIAGFIKAV LAVHRAQIPP NLHFLQWNPA IDASATRLFV
PTDLMQWPDC SGPRRAAVSS FGLGGTNAHV VLEQGPDMPA SSGGSSESSV STLVVTGRTT
ERVSSWATAL ADWLERDTTD VELADLARTL RHRQGEGKFA AVCAVDRQQA VTGLRTLAAG
VPAPGVVLPR EAPAASGTVF VYSGQGSQWA GMGRQLMADE PAFAAAIADL EPVFVAQVGF
SLRKVLTDGE QLIGIDRIQP VLVGMHLALT ELWRHHGVRP DAVIGHSMGE VSAAVVAGAL
TPADGLRVIA TRSRLMSRLS GQGAMALLEL DAAATEELMA GYPDITLAVY ASPRQTVVAG
PPAQVDAMIA VVDAQGRLAR RIEVDVASHH PTIDPILFDL RSALADLTPS APQILLFSTT
GNAGRQTPVF DAGHWVANLR HPVRFSQAVA IAGAKHANFV EVSPHPLLTH AITETLEFVG
SCGDIRVAAT INRDSPETIT FHANLSTVHF PVDAESCDEK GCDGGSNGLV DLPPRPWMHS
KYWVNDRADG RPTGMHPMLG MHVEMPQGRD HAWQADVGTD LLPWLQDHKV HGQPVMPAAA
FAEIALAAGC EAFGLPADAV TVNRLEVEQM LPVESRTQLT TVLNSGAGNS VRVEVYSRST
GGTWCRHAVA CVHAGQGAVD TTWNGALGDT GTIVSPVDFY TALRRTGAHH GRAFAALTRI
IHSDNGFAEA EIALPDDATS HREFRVHPVM FDAALQTLAA AMPTESQQGM TEVTYLPVAM
ETIRVHKQVG RRGRCRAELI NVDDTGAVGR ITLLDDTGAP TASISGVYLR RVNRRAVPLP
LAQKLFDSVW RQTPLSPDSV APRPCPPAGS WLVLTHGVDM KDIAEDFTTG FATSSRRVIT
ANLGDESAVL DAFAKTAADP DLPPVGVVIF VGQPGIDGMA PDDEPTRARD VIWAVSAAVR
AIVSGWHGKS PRMWLVSRNG LLVHDDERGH PTVGALKGLI RVLAYEHPDL RATLVDLDMD
ADVRAMLTAE LAAQGSDDVV AWRGQDRYAE RLARATLNAR VRDPVVRADG AYIITGGLGG
VGMVVARWLV DSGAARVVLN GRSGPSESQR KDLSELEARA EVAVVCGDIA APGMAERLVA
AAEATGRPLR GIVHSAAVID DQIVVKLTRE SLERVWAAKA MGAWRLHKAT TERKLDWWVG
FSSVASLLGS PGQTSYACAN AWLDALVSWR RASLLTATTI NWGQWAEVGV ASALNFGVLD
PISPAEGIEA LEAVLAGDLA RVGVTRLRLD RAVAAFPEIQ QLNYFTDLAG EVGSESDDDW
PGTDALQHLD SGEVNRVVTG RLRRRVSAIM GYPDDRAVAT DEPLTGLGMD SLMAVRIRNT
VRGDFGVEPP VALLLQGASL VDVATELIGQ LGLSEHDEIR PNNEGDFRG
//