ID Q9RNB5_MICAE Unreviewed; 2631 AA.
AC Q9RNB5;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 19-JAN-2010, entry version 51.
DE SubName: Full=McyG;
GN Name=mcyG;
OS Microcystis aeruginosa PCC 7806.
OC Bacteria; Cyanobacteria; Chroococcales; Microcystis.
OX NCBI_TaxID=267872;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PCC7806;
RX MEDLINE=20491409; PubMed=11033079; DOI=10.1016/S1074-5521(00)00021-1;
RA Tillett D., Dittmann E., Erhard M., von Dohren H., Borner T.,
RA Neilan B.A.;
RT "Structural organization of microcystin biosynthesis in Microcystis
RT aeruginosa PCC7806: an integrated peptide-polyketide synthetase
RT system.";
RL Chem. Biol. 7:753-764(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PCC7806;
RX PubMed=15528494; DOI=10.1128/AEM.70.11.6370-6378.2004;
RA Pearson L.A., Hisbergues M., Borner T., Dittmann E., Neilan B.A.;
RT "Inactivation of an ABC transporter gene, mcyH, results in loss of
RT microcystin production in the cyanobacterium Microcystis aeruginosa
RT PCC 7806.";
RL Appl. Environ. Microbiol. 70:6370-6378(2004).
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DR EMBL; AF183408; AAF00957.1; -; Genomic_DNA.
DR HSSP; O30409; 1DNY.
DR GO; GO:0000036; F:acyl carrier activity; IEA:InterPro.
DR GO; GO:0048037; F:cofactor binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR InterPro; IPR001227; Ac_transferase_dom.
DR InterPro; IPR009081; Acyl_carrier_prot-like.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPlipase.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR000794; Beta-ketoacyl_synthase.
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; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR006163; Phsphopanteth_bd.
DR InterPro; IPR020842; PKS/FAS_KR.
DR InterPro; IPR020801; PKS_acyl_transferase.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR016038; Thiolase-like_subgr.
DR Gene3D; G3DSA:3.40.366.10; Ac_transferase_reg; 1.
DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR Gene3D; G3DSA:3.40.47.10; Thiolase-like_subgr; 2.
DR PANTHER; PTHR11712; Ketoacyl_synth; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00501; AMP-binding; 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; SM00823; PKS_PP; 2.
DR PROSITE; PS50075; ACP_DOMAIN; 2.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
PE 4: Predicted;
KW Transferase.
SQ SEQUENCE 2631 AA; 294159 MW; 6A71AE21AFDAA657 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
KDFEQGLFST 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
//