ID U5WV50_MYCKA Unreviewed; 1850 AA.
AC U5WV50;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:AGZ53024.1};
GN ORFNames=MKAN_24040 {ECO:0000313|EMBL:AGZ53024.1};
OS Mycobacterium kansasii ATCC 12478.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=557599 {ECO:0000313|EMBL:AGZ53024.1, ECO:0000313|Proteomes:UP000017786};
RN [1] {ECO:0000313|EMBL:AGZ53024.1, ECO:0000313|Proteomes:UP000017786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12478 {ECO:0000313|EMBL:AGZ53024.1,
RC ECO:0000313|Proteomes:UP000017786};
RG McGill University Mycobacterium genome consortium;
RA Veyrier F.J., Behr M.A.;
RT "Genome sequence of Mycobacterium kansasii.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP006835; AGZ53024.1; -; Genomic_DNA.
DR RefSeq; WP_023372272.1; NC_022663.1.
DR GeneID; 29701939; -.
DR KEGG; mkn:MKAN_24040; -.
DR eggNOG; COG1020; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_35_0_11; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000017786; Chromosome.
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; cd05274; KR_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
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; 2.
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; 2.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
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; 2.
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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 9..83
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 101..526
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1735..1812
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1850 AA; 196580 MW; 8B3A511513C1FC59 CRC64;
MTASINDEAD LRHWLVDYLV TNIGCTPDEV DPNLSLADLG VSSRDAVVLS GELTELLGKT
VSPIDFWEHP TINALAAYLT APEPDSESDV AFKRPGRSSL EEPIAVIGMG CRFPGGITSP
DALWQFLCDR RSAIGKVPDE RWEQFDDGSP EVRALLDRTT RWGSFLPDID AFDAEFFEIS
PSEADKMDPQ QRLLLEVAWE ALEHAGIAPS ALRRSQTGVF AGSCLSEYGA IASTDLSQVD
GWSNTGGAMS IIANRLSYFL DLRGPSVAVD TACSSSLVAI HLACQGLRTQ DCNLAIAAGV
NLLLSPAVFR GFDQVGALSP TGHCRAFDAA ADGFVRGEGA GVVVLKRLTD AQRDGDRVLA
VICGSAVNQD GRSNGLMAPN PAAQMAVLRA AYTNAGMQPN EVDFVEAHGT GTLLGDPIEA
RALGTVLGRG RPEDAPLLIG AVKTNLGHTE AAAGIAGFIK TVLAVQHGRI PPNQRFESPN
PHIPFADLRM KVVDTLTEWP ETGHPRRAGV SSFGFGGTNA HVVIEQGQEV SPSPERDLDP
AVSTLVVAGK TAQRVAATAG VLADWMEGPG AEVPLADIAH TVNHHRSRQA KFGTVVARDR
AQAVAGLRAL AAGQHAIGVV GPQEGSPGPG IVFVYSGRGW QWPGMGRQLL ADEPAFAEAI
ADLEPVFVEQ AGFSLHDVLA NGEELVGIEQ IQLGLIGTQL ALTALWRSYG VQPDAVIGHS
MGEVAAAVVA GALTPAEGLR VTATRSRLMA PLSGQGGMAL LELDATETKA LITDYPQVTL
GIYNSPRQTV IAGPTGQIDD LITRVRARDR FASRVNIEVA PHNPAMDALQ PRMRSELADL
SPRTPTIPVI STTYEDVDTC PVFDAEHWAT NMRNPVHFQQ AIARAGGNHH AFIEISAHPL
LTQAVMDTLR SAQHGTRYTS IGTLQRDSDD TITFRTNLNT VHTDHPPHTP HPPEPHPPIP
TTPWQHHRHW ITTKRSGHVA AAAPAAGTLL GQHTSVLSSP PSHLWQARLA PDAMPYRGRY
RFHGVELVPA SVVLHTMVSA ATELGYGALT DIRFEQPVFA DQPRLIQVVA DNLSISLASV
PAAEASSNRW TRHATARLSS SPAGSALPDN GYHRQSVHGD EIPDVAALFA VHGVDGLPFT
WSVDSWAPRD TGLVVGVELP EALPEGSIAP LLDAAVHVGA LADDTDPRLY VPAGIEQMWF
GDAVAAPRAS LILDRTARDS DGITVDVAIA ARGGAAAVSM RALRYRALDF GDGQPVAESS
DARSFVHTID WQPRVDVVDA QAHPAPGRLT GPQPVAVIGD DGAPLRAHLE NAGYPPAAVS
DAGYLLYVAD SQPATAEETD VDFCVRVTAE IGSLVRTLAA EGAERSAALW IVTRGVHESV
TPSALRQSFL WGLAGVIAAE HPELWGGLVD LPAGADLAES APILAELLVA PSKSILVARD
GVVLTPALAP VRGTPVRQPL QCRPDAAYLI TGGMGALGLL MADWLADRGA RRLVLTGRTP
LPPRRDWELD TLDGELRKKI GAIRALEMRG VTVEAVAVDV GCREDVQALL TKRDRDGAAP
IRGIIHAAGV TNDQLVTQLT EDAVRQVVWP KVAGSQVLNE AFPAGSVDFF FLTASAAGIF
GIPGQGSYAA ANAYLDALAR ARRQQGCHTM SLDWVAWRGL GFAADAQIVS EELKRMGSRD
ITAPEAFTAW EYADGYDVAQ AVVVPVPSTA AVPGAVGAAA HLKPAQDWSQ MPATAVRTEL
EKGLRRIIAA ELRLPETDLD TDRPFAELGL NSLMAMAIRR EAEQFVGIEL SATMLFNHPT
VATLARYLTN RVAPQQDSSA DEMAALSASA GSVLDSLFDR IESTSAEGER
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