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Database: UniProt
Entry: Q6DNE1_9CYAN
LinkDB: Q6DNE1_9CYAN
Original site: Q6DNE1_9CYAN 
ID   Q6DNE1_9CYAN            Unreviewed;      1956 AA.
AC   Q6DNE1;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   SubName: Full=CurL {ECO:0000313|EMBL:AAT70107.1};
GN   Name=curL {ECO:0000313|EMBL:AAT70107.1};
OS   Lyngbya majuscula.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Oscillatoriaceae; Lyngbya.
OX   NCBI_TaxID=158786 {ECO:0000313|EMBL:AAT70107.1};
RN   [1] {ECO:0000313|EMBL:AAT70107.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=19L {ECO:0000313|EMBL:AAT70107.1};
RX   PubMed=15332855; DOI=10.1021/np0499261;
RA   Chang Z., Sitachitta N., Rossi J.V., Roberts M.A., Flatt P.M., Jia J.,
RA   Sherman D.H., Gerwick W.H.;
RT   "Biosynthetic pathway and gene cluster analysis of curacin A, an
RT   antitubulin natural product from the tropical marine cyanobacterium Lyngbya
RT   majuscula.";
RL   J. Nat. Prod. 67:1356-1367(2004).
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DR   EMBL; AY652953; AAT70107.1; -; Genomic_DNA.
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; cd02440; AdoMet_MTases; 1.
DR   CDD; cd08955; KR_2_FAS_SDR_x; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 6.10.250.3430; -; 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; 3.40.50.150; Vaccinia Virus protein VP39; 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; IPR049490; C883_1060-like_KR_N.
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; IPR013217; Methyltransf_12.
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; IPR020803; PKS_MeTfrase.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
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; PF21394; Beta-ketacyl_N; 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; PF08242; Methyltransf_12; 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; SM00828; PKS_MT; 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; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          38..462
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1827..1905
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1956 AA;  215948 MW;  CA71015F97E0676C CRC64;
     MNLKQEQEKE QSLSALQRAL IALKDARSKL EKYETQSKEP IAIIGMSCRF PGGVDSPESF
     WQLLNDGVDA ISEVPSNRWN INNYYDPDPD ATGKISTRDG GFLSQIDGFD APFFCISPRE
     VQSLDPQQRL LLEVSWEAIE RANIVPDQLF NSLTGVFIGI GSSDYLNQLA TSEVPQAYWG
     TGNAPSAATG RLSYILGLTG PNLAVETACS SSLVSLHLAC QSLRQQECNL ALAGGVNLLL
     SPETSIIFSQ AKMLSPDGRC KTFDASANGY VRGEGCGVIV LKRLSDAVAN GDNVLAVIRG
     TAINQDGASG GLTVPNGPSQ VAVIRKALSN GGVDPASVSY IEAHGTGTSL GDPIEVGAIG
     TVFGKTHSQE QPLIVGTAKT NIGHLEVAAG IAGLMKVVLQ LQHQQIAPSL HFKQPNPYIN
     WSQLPVQVST QLTPWQTNGK SRIAGVSSFG FSGTNAHVVI EEAPKEGNSL SATVEENGNS
     TVKEDTLERA VYLLTLSAKT QAALDDLVNS YQNYLKNYPE LRIADICYTA NTCRSHFNNR
     LAVVASNQQE LVEKLRQHQQ GEEVTGIYSI ELPNNSTAPK IALLFTGQGS QYVNMGRQLY
     QQAPVFRKAL EQCNEILLGT ETFREKSLLE ILYPANQEQS NSSLLDQTAY TQPCLFALEY
     ALFKLWQSWG IQPDVVMGHS VGEYVAATVA GVFSLEEGLK LIAARGRLMQ QLPAGGEMVS
     VIASESKVLE IFKAMSLEEK VAIAAINGPE STVISGEAEA VGAIATHLES LSIKTKQLQV
     SHAFHSRLME PMLAEFEAVA KQVTYSQPQI SLISNVTGQQ VGSEITSAEY WVNHVRQPVR
     FSESMTTLHQ EGYELFLEIG PKPILLGMGR QCLPEGVGVW LPSLRPGVEA WQQMLQSLGQ
     LYMKGIKVNW SGFDQDYACH KVAIPTYPFQ RESYWIDTDK NQGQKAVNGS SSLIVDLLNQ
     SDIEGLNQEL SFSTELTADE QKMLPKLLGI LVNRHQDYLE FKGNVVYDYY NSFAEISQEK
     LSKEKQQENN SLQFLTFGIL PESIPGFSWL KMLTNSNQNP THKTALLEAQ QELRRLCFSQ
     VDFSSTKKVL DFGCGYGSDL ITLAKNHPHL QLNGYTISSG QAKFAANQVN DYQLQEQIQI
     FNRDSSKDEF PDNYNLAFGF EVAHHIKDKS LLFSNISRHL QEEGLLVMAD FIANSDVDID
     HEETSSYFIT KQHWVEQLSP NKLQLISAID ISHEVSNYLY DAEFEENLRE LYEQNHDDNV
     KSAFQSYNQL GKLLSKGLAS YVLLTAKKQE NLPQEQSYQL NREMLAQLSS YSEVAVKQWV
     YELKWETKKH QQLLSPNKPG NWLIFADQQT QALKTVLAKQ NQNCLIVTPG SSYKQLDDQH
     YQLNPTNAQE FQQLIKELFT TQDTLEGVVH LWNINTSTEE LEAAQELGCA SVLYLVQALV
     SNSQSSIVPL WLVTQGTQNV EENEPKLAVQ QAPVWGLSRV IALEHPELKC RRVDLDQTRN
     SLEALEALGK ELLNPDDEDQ IAIRGGVRYS ARLARRTQKS ISEQEQQIAF GTEGSYLLTG
     GLGALGLEVA QWMVKQGARH IVLNGRRTPS ETAQETIQQL EQTGAKISVI LGDVSKEEDV
     ASILKQIEAS QAPLRGVIHA AGFLDDGVLQ QMSWERFRKV MAPKLQGAWY LHQLTQKLPL
     DFFVCFSSIA SLLGSPGQGN YAAANAFMDT LADYRRSMGL PGLSINWGAW AQGGMASRLG
     SQHQSRLRTT GMNLITPEKG LQVLGELLSQ PVSQVGVFPI NWSQFLGQLP VGHTISFLEA
     FASRKLQKET TKDENFLEQL ALAIESERNQ ILIGXLXVIV GKLLGFDKXK LXNPELGFFD
     MGMDSLLTVE LRNLLSSNLG CSISAAELFG TSNIQNLAEH LIKEILPEGQ EEEEVDLDDS
     QNTQNLDSAQ IETQGKVDHA IAAELQEIKN LLKEGN
//
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