ID U5WUW5_MYCKA Unreviewed; 1535 AA.
AC U5WUW5;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:AGZ53023.1};
GN ORFNames=MKAN_24035 {ECO:0000313|EMBL:AGZ53023.1};
OS Mycobacterium kansasii ATCC 12478.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=557599 {ECO:0000313|EMBL:AGZ53023.1, ECO:0000313|Proteomes:UP000017786};
RN [1] {ECO:0000313|EMBL:AGZ53023.1, ECO:0000313|Proteomes:UP000017786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12478 {ECO:0000313|EMBL:AGZ53023.1,
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.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP006835; AGZ53023.1; -; Genomic_DNA.
DR KEGG; mkn:MKAN_24035; -.
DR eggNOG; COG0300; 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; 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 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; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
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; PF00550; PP-binding; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SMART; SM01294; PKS_PP_betabranch; 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.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 33..458
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1417..1492
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1535 AA; 162271 MW; BFD5E77FDF93BB2B CRC64;
MIRTAFSRIS GMSAQQRATL AEEFTKISRI AVAEPVAVVG IGCRFPGDAT DPDSFWDLLI
EGRNAISRVP ADRWDADAFY DPDPLAPGRM TTKWGGFVPD VAGFDAEFFG ITPREAAAMD
PQQRMLLEVS WEALEHAGIP PDSLAGTRTG VMMGVYFNEY QSMLAASPEN VDAYSGTGNA
HSITVGRISY LLGLRGPAVA VDTACSSSLV AVHLACQSLR LRETDLALAG GVSITLRPET
QIAISAWGLL SPQGRCATFD AAADGFVRGE GAGVVVLKRL TDAVRDGDRV LAVVRGSAVN
QDGRSNGVTA PNTAAQCDVI ADALRSGDVA PESVNYVEAH GTGTVLGDPI EFEALASTYG
RGQGSCALGA VKTNIGHLEA AAGIAGFIKA ALAVQHATIP PNLHFSQWNP GIDAAPTRFF
VPTENTAWPA TEGGGGPRRA AVSSFGLGGT NAHVIIEQGP ELTPASDAGS HPDTHPDAQV
STLVVTGKTA QRVAATAAVL AEWMDGPGAA VALADVAHTV NHHRARHAKH GIVVARQRAQ
AVAGLRALAA GQHSPGVVRP LDGSRGPGTV FVYSGRGSQW AGMGRQLLAD EPAFAAAVAE
LEPVFVEQAG FSLHEVIAGG LELVGIERIQ LGLIGMQLTL TQLWRSYGVQ PDLVIGHSMG
EVAAAVVAGA LTPAEGLRVT ATRSRLMAPL SGQGGMAMLG LGAEQTEALI ADYPQVTLGI
YNSPRQTVIA GPTAQIDELI ARVRAQNRFA SRVNIEVAPH NPAMDALQPQ MRSELADLTP
RTPTIPIIST TYENLDTRPA FDAEHWATNM RNPVRFQQAI ARAGAQTFIE ISAHPLLTQA
IADTLEAARP EPAIYANIGT LQRDTDDTVT FRTNLYTALD HPPQTPHPPE PHPAIPATPW
QHTRHWITAA AGAGRRTPNT VAAPGQVRSE NGALDDWCYE LAWPARPAPD TETSNPARWL
VVADAGLCAE MRRAAGADTR VELLAQAALA ADGDPGTLLE ALRDVDHVLY APPVGDDPLD
VAQAYRLFHA ARRLSAAMTG SSSPAKLFIV TRNAQPVAEG DRANPGHAVL WGLGRSLALE
HPEIWGGLID LDDSVPTALA ARQVLAAAGS ADEEDQVVYR LGTRLVPRLR WRPVTTEPVT
LSSDTSQLVI GATGNIGPHL IRRLAQMGAG TVVAVSRNPG DRLHELAETL AAAGKNLVTV
AADATDEDAM TALFDRFGAD LPPLEGIYLA AFAGQPVLLS QMTYDDVTAM FAPKLDAAAL
LHRLSVTTPV RHFVLFSSIS GLTGSRWLAH YTATSGYLDA LAYARRVMGL PATVVDWGLW
KSLADAEHQA GQVSVGSGLL PMDDEIAIGA LPLVLNPQAG VRTAVVAADW PLLAAAYRTR
GSLRIVDDLL PAPADVALPE SEFRKALRDC QAERRHDMLF DHVAGLAATV MGMPATATLD
PAAGFFQLGM DSLMSVTLQR SLSESLGEFL PASVVFDYPT VYSLTDYLAT ILPELLETSQ
AAGTAASDQP AAETYEEFTE DELLEQLSER LRGTR
//
