ID A8YJW1_MICA7 Unreviewed; 2631 AA. AC A8YJW1; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 29-MAY-2024, entry version 91. DE SubName: Full=McyG protein {ECO:0000313|EMBL:CAO90231.1}; GN Name=mcyG {ECO:0000313|EMBL:CAO90231.1}; GN ORFNames=IPF_370 {ECO:0000313|EMBL:CAO90231.1}; OS Microcystis aeruginosa (strain PCC 7806). OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae; OC Chroococcales; Microcystaceae; Microcystis. OX NCBI_TaxID=267872 {ECO:0000313|EMBL:CAO90231.1}; RN [1] {ECO:0000313|EMBL:CAO90231.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PCC 7806 {ECO:0000313|EMBL:CAO90231.1}; RA Frangeul L.; RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0007829|PDB:4R0M} RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 1-643. RX PubMed=25849398; DOI=10.1107/S1399004715001716; RA Tan X.F., Dai Y.N., Zhou K., Jiang Y.L., Ren Y.M., Chen Y.X., Zhou C.Z.; RT "Structure of the adenylation-peptidyl carrier protein didomain of the RT Microcystis aeruginosa microcystin synthetase McyG."; RL Acta Crystallogr. D 71:873-881(2015). 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; AM778952; CAO90231.1; -; Genomic_DNA. DR RefSeq; WP_002742841.1; NZ_CP130696.1. DR PDB; 4R0M; X-ray; 2.45 A; A/B=1-643. DR PDBsum; 4R0M; -. DR SMR; A8YJW1; -. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter. DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro. DR GO; GO:0004312; F:fatty acid synthase activity; IEA:TreeGrafter. DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro. DR GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt. DR GO; GO:0071770; P:DIM/DIP cell wall layer assembly; IEA:TreeGrafter. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro. DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt. DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:TreeGrafter. DR CDD; cd05906; A_NRPS_TubE_like; 1. DR CDD; cd02440; AdoMet_MTases; 1. DR CDD; cd08955; KR_2_FAS_SDR_x; 1. DR CDD; cd00833; PKS; 1. DR Gene3D; 3.30.300.30; -; 1. DR Gene3D; 3.30.70.3290; -; 1. DR Gene3D; 3.40.47.10; -; 1. DR Gene3D; 1.10.1200.10; ACP-like; 2. DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1. DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 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; IPR045851; AMP-bd_C_sf. DR InterPro; IPR020845; AMP-binding_CS. DR InterPro; IPR000873; AMP-dep_Synth/Lig_com. DR InterPro; IPR042099; ANL_N_sf. 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; IPR020806; PKS_PP-bd. DR InterPro; IPR009081; PP-bd_ACP. 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; PF00501; AMP-binding; 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; 2. DR SMART; SM00827; PKS_AT; 1. DR SMART; SM00822; PKS_KR; 1. DR SMART; SM00825; PKS_KS; 1. DR SMART; SM00823; PKS_PP; 2. DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 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; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR SUPFAM; SSF53901; Thiolase-like; 1. DR PROSITE; PS00455; AMP_BINDING; 1. DR PROSITE; PS50075; CARRIER; 2. DR PROSITE; PS00606; KS3_1; 1. DR PROSITE; PS52004; KS3_2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:4R0M}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}; KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 569..644 FT /note="Carrier" FT /evidence="ECO:0000259|PROSITE:PS50075" FT DOMAIN 668..1109 FT /note="Ketosynthase family 3 (KS3)" FT /evidence="ECO:0000259|PROSITE:PS52004" FT DOMAIN 2515..2591 FT /note="Carrier" FT /evidence="ECO:0000259|PROSITE:PS50075" SQ SEQUENCE 2631 AA; 294145 MW; 07AAACEA818BA657 CRC64; MSKHSISLGG QLEDNWRTLS EVLETATKHN NHGITYIRND ATEYFQSYQD LYQDALVILN GLEQKGIKLG HKVILQIAKN QDFIPALWAC FLGGIIPVPL TVAPSYDLEN SAVKKLENVW KILDNPLILS DSELITEIEK LGTYSHLEGW QVISVNELRK APSKIEQLPI LDPQDAALLL FTSGSTGMPK GVILTHHNIL SMTAGTVVMN HFTQQEVTLN WMPLDHVGAI VFLGIMAVDL ACDQIHVPME LVLRQPLQWL ELIQKHQVSI SWSPNFAFSL INQQAEELKH VSYNLSSMKF LVNAGEQVSV KTIRLFLEIL EKHQLQERAI KPAFGMTESC SGITWSAGLS KNELTEENSF VSLGKPIPGA TIRIVDQENN PLPEREIGRL QIQGNSVTKG YYNNNELNQE VFQEGWFTTG DLGYLSKGEL FITGREKQEI IINGVNYFAH ELETTIEELE GVKVSYTAAF AVFDQSRETD LLIITFSPES EQFEQGIKVV RKIRSHVTQK FGIAPAYVIP LERNLVPKTS IGKVQKSKLK KDFEQGLFSS RIQEIDQYLA KERQKNQTLP QSENERQIAA VWSEVLQLTS VGLEDNFFEL GGHSIHLIRV QNELEKLFNR QLSLAEMFKN PTVATLARFL SEESNTNQVI AQKSRQRAEN RSRRHNETHD IAIIGMTGQF PGAKNLTTFW ENLKNGIETI SFFSEEELQE SGVSSELFNQ PNYVRARPIL EQVEYFDSEF FGYTDREAEL LDPQQRLLLE CSWECLENAG YNPNTYQGSI GIFAGASMNT YLINNCYPNR GKLDSNDELQ PFTLDSMGGF QTMVANDKDY LTTRISYKLN LHGPSVNVQT ACSTGLVVVH LACQSLISGE SDMALAGAAS INSPQKIGYL YQEGLIMSPD GHCRAFDAEA KGTIFGSGVG VIMLKRLSDA LADHDHIYAV IKGSAINNDG GQKLGFTAPG GEGQIAAATE ALAFAGVDAN TISFVEAHGT GTPLGDPIEV DALAKVYQGA NEGECALGSV KTNIGHMQIA SGIAGLIKAT LALKYRVIPP TLHFQNPNPQ INFSQTPFYI NNEAISWTTK QDKSEKLPRR AGVNSLGIGG VNAHVILEEA PPIIPQDNQS QRPYHLLTLS ARTELALTEL VSRYIDFLES QPEKDLSDVV FTANTGRVHF SNRLALTGYK NSDFIEQLRQ FKQLDYESTI YGIVDEKRPS KIAFLFTGQG SQYVGMAHQL YQTQPTFRKT LDAGEKYHQK LTGKSLLNVV FADTDDSLNQ TAYTQPALFL IEVALAQLWH SWGIQPAAIL GHSLGEYSAA CFAGVFDLES GLKLVSHRGN LMGQLPQNQG EMAAIFLDKN SVVEHCQSQG IKIAIAAINA EQHTVISGEK NVIQKLCNHF TNAGVKVRQL KVAHAFHSPL VEPMVAEFKT ILQEISFSQP QISLVSNLTG EIADDSIMTP EYWLQHLLNT VQFHQGALFL QSLGCDTFIE IGPQPILSGI IQSSLSSSEP LTLPSLRSGF SDWQVLLESL GKLYVRGAKI DWFSFDQDYH PRRCALPTYP FQKRQHWISL KTPSATVPRE SNLVKMLSEK DKTTLMQTLL ETGHYSEDEK PTISAIVQQL IKLYYQEKED FDFAKLLYQV AWLPCDLANG KLENLTSLKT DLEVYLEPQL QSSELMGVSL AFSEMEKLAA DFVVKALKDL ELFQMNTFLD PDQSFIQAGL KQEYKSFWNY VLEILAKVGI LEKQNTRWKI VKEPEQSNPD LAVEDLINHY PNAQIELNLF RQVATNLAAI ITGKISPLSI LFSQDGQGGA SEFYKNTSSA KILNLGISKT VELLLSSYPP SASLRILEIG AGTGATTQQV LKACNSRQIT YTFTDVSPFF LEKARDNLAE FSELEYKVLD IEKDPKLQGF CCHSYDLIIA ANVLHSTANL QEETLPHIQS LLRPGGHLLL LELTQQSSWI DLIFGVTQGW WRFSDYHLRP NHPIITASTW ESMLLKSGFS QVEFVSPDQK IGTALFQQSI ILAQSSEISS NTAKNWLIFT DVEPQQNTFA LGIQEQLLKK CDSCRIIYQG EKNTQISSSE SCLNANQLQQ LEEWFASNPS PDRIIYLLNS DGKDQPESIL LNRCNYLLNL LKAIQKIPNP PQLFLVTQGA QPFELEQPSF GFQSPLWAMG RVIALENPQL WGGMLDLDPD VDINQNITAL LLGLTHAHDE DHLVFRKGQG YVARLLPLKS LETKTIKIQP EATYLITGGI GHLGLELAEH LVNLGAKHLI LTTRRSLPVR FLWDSAAELA QISQKIRKLE EKGASIAVTS ADVGNFEAMQ AIFTQIEETA YPLRGIFHLA GISGRQAQLK DCTLQDLEAV FQAKVKGSWN LHQLSLGSQL DYFVLFSSAG AIWGAKEQGL YDTVSHWLDA LAHFRHLQGL PATTLNWALL AGHGIVSQDY EDWLKQIGIR EIAPDMALRV MDAIMASNQT QVLIADVDWV RFKNIYQFKG EKPLLKNLGL SEIPINSVQE SDSVLHLLEE MPFGERREYL LEYVSKQVRM ILGIKSMPDT EQGLIEMGID SLSSIELKNR LEKRLEVLLP TSLVFDFPNI RRLVDYLFDR IFGEKVQKTA EKMINFTEVQ QEISEDLILQ ELTDLEAFLG D //