ID A0A0C2Q9P0_9CYAN Unreviewed; 2075 AA.
AC A0A0C2Q9P0;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Non-ribosomal peptide synthase {ECO:0000313|EMBL:KIJ75065.1};
GN ORFNames=SD81_21570 {ECO:0000313|EMBL:KIJ75065.1};
OS Tolypothrix campylonemoides VB511288.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1245935 {ECO:0000313|EMBL:KIJ75065.1};
RN [1] {ECO:0000313|EMBL:KIJ75065.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VB511288 {ECO:0000313|EMBL:KIJ75065.1};
RA Tripathy S., Das S., Gupta A., Malar M.C., Adhikary S.P.;
RT "Draft whole genome shotgun sequence of Tolypothrix campylonemoides
RT VB511288.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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:KIJ75065.1}.
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DR EMBL; JXCB01000009; KIJ75065.1; -; 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; cd19534; E_NRPS; 1.
DR CDD; cd08953; KR_2_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 2.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 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; 3.30.559.30; Nonribosomal peptide synthetase, condensation 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; IPR049490; C883_1060-like_KR_N.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
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; IPR010060; NRPS_synth.
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; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR01720; NRPS-para261; 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; PF21394; Beta-ketacyl_N; 1.
DR Pfam; PF00668; Condensation; 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 SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 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; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 12..438
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1518..1592
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 861..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..897
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2075 AA; 229870 MW; B26DD36122C223E3 CRC64;
MTSPAASTST NGSEIAIIGL AGRFPGAKNI DEFWKNLQNG RESISFFSDE ELLSSGISSS
ILNDPNYVKA LAILEDAELF DASFFGFNPR EAEITDPQHR IFLECAWSAL ENAGYDSQTY
KGAIGVYGGS SLSSYLLNIY LNQNIINSID PQQLTIAANK DFLTTRVSYK LNLEGPSYAV
QTACSTSLVA VHLACQSLLN GECDIALAGG VAINATRKAG YMYTEGGIMS PDGHCRAFDA
NAQGSVGGEG VGIVVLKRLE DALSHRDTIH AVIKGSAINN DGSFKVSYTA PRIDTQAKVI
RTAQVIAEVE PETITYIEAH GTGTALGDPI EIAALTQAFQ ASTQKKGFCA IGSVKTNIGH
LDTAAGVTGL IKTVLALKHK QIPPSLHFER PNPEIDFANS PFYVNTKLSE WETNGTPRRA
GVSSFGLGGT NAHVILEEAP PEEQGSRGTG ELGRKYHLLV LSTKTESALE KATTNLANYL
REHPDLNLAD AAYTLLFGRR VFEHRCAVVC RDIQDAVNAL VEPKRVFTST QKGQERPVAF
MFSGLGTHYV NMAFELYQTE PTFRACVDQC CLLLRPHLGL DLRDVLYPKR NTKGVNQQQQ
NNGSASLDLR KMLGRGEEQA DVATQKLNQT VFTQPALFVI EYALAQLWIS WGIRPTAMIG
YSIGEYVAAT LAQVLSLEDA LTLVAKRAQM IQELPFGAML AVGLSEEEIQ PLLNEKISMS
AINGSSLCVI AGFTDAVEEL ERQLSQKGIV GKRLQSSHAF HSVMMEAIAP TLHDLVKTFS
LKPPKIPYLS NVTGTWITQD QATDPSYWVK HLCQTVRFAS GVQELWKKDN PILLEIGPGQ
ALNSFALQCI ADFSRHLEKP TQNLTPQPHS LRGNGENSKP LKKQERGMEA RLTDPVKSKQ
CIESDDTKAV MLSSLRHSYE QQSDVAFLLN TLGRLWLAGV KVDWSGFYAN EQRHRIPLPT
YPFERQRYWI EANPEAALAT PSQQTLHKKP NIADWFYIPS WKRSSHVTSK SEQKLCCLVF
VDTVGVGSQV AKQVELQGHD VISVTLGEQF TQLGERCYAI NPQASSDYDT LLKELDSLDL
TPNAISHFWS LIPNAQGESP HQFFEECQNL GFYSLLFLAQ ALGKQEVTDS VQILVVTNNV
QEVNGDEKLC PEKAPVMGIC KVIPQEYPNI TCRNIDLVIP ESGTRQKNQL IDQLLAELTQ
TASENIVAYR GKHRWVQTFE PIQLEEPDEG TIPIREEGVY LITGGLGEIG LVLAEYLAQT
AHAKLILTGR SGLPPKQEWS QWLATHDENN DISRKIKKVQ ALEALGAEVL ICRADVANFE
QMQAVMTEAS KRFGQIHGVI HAAGIKLSRT VQQISRTECE SQLSSTGYGL FVLENILQGK
ELDFCVIISS LASVLGVLGM AAYPAAHIFT DAFVHKHNQT SLVPWLSINY DNWITQESLE
SVTIPKGADS MMTRQEGLEA FRRALSTGMT QVVTSTVDLQ ASIKKWVKLE FNKNSQLQEK
ASSSSFYSRP NLDNAYVAPR NEVEQTIANI WQELLGIEQV GIHDNFFELG GDSVLGIQVS
ARAAKAGYRL APQQLFEHQT IAELAEVTST KQIVQAEQGL VTGSLPLTPI QHWFFEQNLS
ELHHWNMAFF VEVMQVLDPA LFEQAWQHLF IHHDALRLRF TLSGSGWQQV NSGFESQVNF
THIDLSALSS EAQKSFMEAT ATELQGSLNL STGPIVRGIL FELGANKPSR LLIIIHHLAV
DFGSWRILLE DLETAYHQLY QGKAIQLPQK TTSFKQWSER LKEYAQSEKL QKRQNDCLSD
RHKQVSRLPI DYPGGMNTVA SSQTVSVALS EKETQALLQE VLAVYRINTQ EVLLTALVQA
FTQWTGINCL LFDTEEDGRE ASTIIDNVDI SRTVGWLTTL YPVLLDLEGA ENLGDALKAV
KEQFRCIANR SIDYGVLRYL SEDTTLTQKM RSLPQAEVFF LYLGQFGKSF DQSSMLRPTE
ESTGLLYSPQ GTQPYLLSVI AWVNEEGQLR LEFGYSTNLH RRETIEKLSD SFIEALKSLI
THCRSLETVE YTPSDFSAAN INQENLNNLL AQIGQ
//
