ID A0A100W3D2_9MYCO Unreviewed; 1797 AA.
AC A0A100W3D2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Polyketide synthase pks13 {ECO:0000313|EMBL:GAS90878.1};
GN ORFNames=RMCB_4974 {ECO:0000313|EMBL:GAS90878.1};
OS Mycolicibacterium brisbanense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=146020 {ECO:0000313|EMBL:GAS90878.1, ECO:0000313|Proteomes:UP000069620};
RN [1] {ECO:0000313|EMBL:GAS90878.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM15654 {ECO:0000313|EMBL:GAS90878.1};
RA Katahira K., Ogura Y., Gotoh Y., Hayashi T.;
RT "Draft Genome Sequences of Five Rapidly Growing Mycobacterium Species, M.
RT thermoresistibile, M. fortuitum subsp. acetamidolyticum, M. canariasense,
RT M. brisbanense, and M. novocastrense.";
RL Genome Announc. 4:e00322-16(2016).
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:GAS90878.1}.
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DR EMBL; BCSX01000044; GAS90878.1; -; Genomic_DNA.
DR RefSeq; WP_062830905.1; NZ_JACKTM010000047.1.
DR STRING; 146020.RMCB_4974; -.
DR Proteomes; UP000069620; Unassembled WGS sequence.
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 SMART; SM01294; PKS_PP_betabranch; 1.
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 29..103
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 120..545
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1254..1331
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1378..1421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1391..1414
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1797 AA; 192393 MW; D4C806BFED9B5600 CRC64;
MDEAQSNSNL PATTESAGQP ASRPDMTVAE MREWLRKAVA TATGQSADAI DETTPLIELG
LSSRDAVAMA SDIEDLTGVT LTATVLFRHP TIESLATVII EGEPEPEDTS DEDWSRERDV
EDIAIVGVST RFPGDLNTPD EMWEALLAGK DCITDLPEGR WEEFLSEPRI AERVGKARTR
GGYLSDIKGF DSEFFALSKM EADNIDPQQR MALELTWEAL EHARIPASSL RGGSVAVYIG
SSNNDYSYLS LADPTVTHPY AITGNQTAII ANRVSYFYDF RGPSVSVDTA CSSSLVAAHQ
GVQALRSGEA DVAIVGGVNA LITPLVTIGF DEVGGVLASD GRIKSFSSDA DGYARSEGGG
MLVLKRVSDA RRDGDQILAV IAGSAVNHDG RSNGLLAPNP DAQEEVLRRA YKDAGINPRN
VDYIEAHGTG TILGDPIEAD ALGRVVGRGR DADKPALLGA VKSNVGHLES AAGAASLAKM
TLALANDKLP PSINYAGPNP YIDFDKEHLK VNDTVSEWPR YSGHAITGVS GFGFGGANAH
LVLREVLPSD LVEPEPEPEA VEEKSTADDA NAVYVGGVRM DEYGEFIHDE PEADEYPAYD
EAAHELPGLT DEAKRLIEKA REELAAREAA EPVKKVVPLA VSAFLTSRKK AAAAELADWI
DSPAGREASL ESIGRSLSRR NHGRSRAVVL ATDHDEAIKG LRALAEGKQH PSVITADGPV
TNGPVWVLAG FGAQHRKMGK ELYLREPVFA EWINKVDAHI QDERGYSVVE LILDDAIDYT
NETCEYPIEV VQTVIFAIQI ALGEFLKAHG AKPGAVVGQS LGEAAAAYFS GGLSLADATR
TICSRAHLMG EGEAMLFGEY IRLMALVEYS ADEIKTVFAD YPGLEVCVYA APTQTVIGGP
PEQIDAIIAR AESEGKFARK LQTKGASHTQ QMDPLLGELS AEIQGIEPHP LTTGYFSTVH
EGKFIRAGAE PIHDVEYWKK GLRHSVYFTH GIRNAVDNGH TTFLELAPNP VALMQVGLTT
ASAGLHDAQL IATLARKQDE VTSMTTAMAH LFVHGHDLDI RTLFPRKSSG LAGALDFANI
PPTRFKRKQH WLDAHFTGDS SAVMPGNHVA TPDGKHVWEF VPKGAIDLAA LVKAAAAQVL
PDARLTASEQ RAVPAEGSRL VTTLTRHPGG ASVQVHARID ESFTLVYDAI VTRGGAAATL
PTAVGAGVVA EQVSAAPAAV EPEPEDDAEI LQDNLTKGAG MGAGFEKWSP ESGETVAQRL
GTIVGAAMGY EPEDLPWEVP LIELGLDSLM AVRIKNRVEY DFDLPPIQLT AVRDANLYNV
EELIKYAIEH RDEVDQIAES QKGKSAEDIA AEQSELLGGA STVAELEAKL AEAGHPLADK
DSEDSVAPAA PIDIPAPPTD PSGPSIPAPP SDPSGPSKAT AAAAAAKVLT QEAVTEALGA
DVPPRDAAER VTFATWAIVT GKSPGGIFNE LPSVDDATAT KLAERLSERA EGTITVDDVK
SATTIEELST IVRDQLEEGV VDGFVRTLRA PKEGSSHVPL FVFHPAGGST VVYEPLMKRL
PPDTPVYGFE RVEGAIEERA AEYVPKLLAM HDGPFVLAGW SLGGALAYAC AIGLKRAGAD
VRFVGLIDLA LPGEPIDQSK EGMRARWDRY ALFAERTFNV EIPAIPYEEL EQLDDEGQVK
FVLDAIKDSG VRIPGGIIEH QRTSYLDQRA LATIEVQPYD GHVTLYLADR YHDDAIVFEP
AYATRKPDGG WGEYVKDLEV VPIGGEHIQA IDEPYIAKVG AHMSEALNRI EAESESK
//
