ID J9WPK4_MICAE Unreviewed; 3487 AA.
AC J9WPK4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=McyE {ECO:0000313|EMBL:AFS18059.1};
GN Name=mcyE {ECO:0000313|EMBL:AFS18059.1};
OS Microcystis aeruginosa FCY-26.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Microcystaceae; Microcystis.
OX NCBI_TaxID=1150859 {ECO:0000313|EMBL:AFS18059.1};
RN [1] {ECO:0000313|EMBL:AFS18059.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FCY-26 {ECO:0000313|EMBL:AFS18059.1};
RA Rhee J.-S., Dahms H.-U., Choi B.-S., Lee J.-S., Choi I.-Y.;
RT "Identification and analysis of whole microcystin synthetase genes from two
RT Korean strains of the cyanobacterium Microcystis aeruginosa.";
RL Genes Genomics 34:435-439(2012).
CC -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC family. {ECO:0000256|ARBA:ARBA00029443}.
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DR EMBL; JQ290085; AFS18059.1; -; Genomic_DNA.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:0009403; P:toxin biosynthetic process; IEA:UniProt.
DR CDD; cd05930; A_NRPS; 1.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd19531; LCL_NRPS-like; 2.
DR CDD; cd00610; OAT_like; 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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 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; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
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; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
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; 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; IPR013217; Methyltransf_12.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 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; PF00202; Aminotran_3; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 2.
DR Pfam; PF18558; HTH_51; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
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; PS00600; AA_TRANSFER_CLASS_3; 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 3: Inferred from homology;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 33..456
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 938..1013
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 2943..3018
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1461..1488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1956..1985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1956..1976
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3487 AA; 392095 MW; C450319B8EE92D6F CRC64;
MVESIDYKKL MATTLSKMEV MQARINELET RQSEAIAVVG MACRFPGGIN SPEKYWSFCQ
AGLDAIVEVP KSRWDISKLY SQEPTLGKMN TAYGGFLQEN ITEFDARFFS ISAREAASMD
PQQRLLLEVA WEALENANLP LKNLADNKVG VFVGITSIDH ALKVYGTNYD QIDSFFGTGN
ALSAAAGRLS YFLNLHGPCL SIDAACASSL VAVHQGIRSL RNRECELALV GGVNLILEPA
ITISLSQSGM MSPDGRCKTF DASANGYVRG EGCGVLILKT LSEAQKNGDH ILALLRGSAV
NHNGAAAGLT VPSGPAQQEL LRQALADARI VPEDVSYIEA HGTGTSLGDP IELNAIASVY
GKRSDPLYIA SVKTNIGHLE AAAGMAGIIK TILILQQGEI PSHLHLQSPN PLINWEDHPI
KIPTQNIPWP NNNKVPIAGV SSFGFSGTNA HVIVQQAPVS KISEIQQQIP SHLLTLSAHN
KTALKELAKR FHTLLESHPE IGDICYSAAV GRIDLPERLA IVGDTCPELQ QRLAAFAEEN
PLDDLTFYQR FTSEKSPKIV FLFTGQGACY PGMGHQLYQT QPTFRQYIDQ CAEILAKYLD
HPLTEILFGE QTDLLNQTAY AQPAIFALEY SLTMLWKSWG ITPSLLIGHS VGEYVAACIA
GVFSLEAGLA LVVKRGQLMQ TTTSGKMASI FADEETVISL IKNYTQTVSI AAINHPQQIV
IAGESASLEE VISTCKKQKI PAQYLPVTQA FHSPLMEPIL KEFEKEARQI SYQRPQILLL
SGLDGEVLEN APDATYWSKQ CREPVRFLSS LITAFNKGYN LFLEVGPRPI LAEQGRRYKD
EVIWLSSLNR GLDNWQTILS ALGQLYLNGA PFNPEQFNRN YGYKKVRLPN YPFQRKPFQF
QPNPRTENQS IDKIFLDAQT SNLTDTETTV FNMQKHQQEI RNQLKSILAL LLKEDENELP
EDETLLNLGA DSIILTDFSR KIEEKFQVKV KIDQLFTDLQ TLVDIAEYLC QFVKEKPLEN
ASEITAKVID DETELSNYLQ VIDQLQPIAT AYIIKALESL GKKLNQGEQW TIETLRQTLP
VAPKYHILLN RYLQDLEQAN ILHNQGNIWT VKNLPESFSL PQALQKLEKT CPSAKPELEM
LQRCGENLAE VLKGNMDPLT LIFPEGSVAH AESIYGNSPV SRLMNQRVAQ AINQILTNFS
NSDRPYQILE IGGGTGATSE AILHHLNLDH VTYSFSEVSP FLLHQARQKF QKKYNLNFHQ
LDIEKSPISQ GIPAHNYHIV VAANVLHATR NITETLTHIR ELLRPGGYLV LLETVENNSW
LNLTFGLTPG WWRFQDQELR SDTPLLRGEN WCSVLKSCGF ATANSFSKQN NIPINNGQEL
ILACVPDEPL SIPARTKLTV SGESSGKEAL MMAQLQSLKD LKDLHEKTII KQLEVLQTAT
VSPSIAPEIL TNQTQIIPAQ SSKIETYPPV SQEKPKSPEK PSSPNLNPLA LKLTENKSLT
EQQQAFIQNL QSIYNQKTAK SKAYSQNSRK TMVDVKPTID FRMALKEFQY PIVSESAQGA
YFKDIDGNNY IDLAMGFGVN FFGHSPDFVI EAVQEQMNRG IGLGMQSNLA AETAALISEM
GRVERVAFSN TGTEAIMAAV RIARSRTKRQ KIVMFAGSYH GTFDGILARV GEDKTTAQPL
SLGTPLGMVE DVIVLSYGVE ESLDIIATHA DDLAAVLVEP VQSRKPDLQP QEFLQKLRQI
THKKGITLIF DEIITGFRIA PGGAQEWFNV EADIVIYGKA IGGGLPISMI CGKADFLDTV
DGGFWQYGDD SHPQTELTAF GGTFCRHPLA LAACRAVLLH LRENSPTIQE KVNQLTHRLA
TEVNQFFQEI GIPIRVVNFG SLFRFEPFGA YSIFLQPIEL PLFYYLLNLK GIYTWEKRVC
FLSTCHTNED IDKVIVAVKE AITELQQAGF FANAKRPQVK KEEKKPLSED EDGRGHLPSL
NQSFPTSEAQ RQLWLLAELD RNASASYNVT TSLELRGSLD VYILEKTINQ VINRHEALRT
QIIEQGELQE VVNQVNIKLK LINLKDEDNP EATALALRSQ FSQKPFDLSI APLFAVILMR
LKPDHYLLSL KTHHIVADGW SLGLILQEIG QLYSSQNNTT KEVLTPPMQF RQYLTLRAQE
TQSPQMLEHR DFWLKTYQED LPTFELPTDF PRPAVKTYTG GQESQVIPSE VGQNLQKVGR
KNKATLFMTM FAAYTAFLRR ISGHKDLVIG IPISGRQIEG SDNLVGFCSQ FLPLRIQVDA
TTSFIEHLQH TKQTLIDAFR HQSYTLEDLL AALQLPRDFS RSPLISVSFN MDPSLTLPEF
KDLKVSLPPS PISYTPFDLG FNLIELNDNL IIYCNYNTEL FKKETIKQFL ESFEILLRGI
IDDANHLLYQ LPLLTPVQQE KLLRQLTGKT RKLPEKATII DDFVAQVKLT PNAPALIAGK
ISLSYQELNE KVNRLTHYLQ QEYQLGVGKV IGVMLQRNHN LIIGILATFK TGATYVPIDS
QYPHSRIEFI LKDSGCHVCL TESNFISKLP EKMEKICLDK IDPIVEKYDK DEPKIFRDSS
QTAYIFYTSG STGNPKGVMG RHISILNVIQ SLRLTFDLDK HPEWRYIFTA AVTHDPSIRN
IFLPLTIGAS LYMYEIKYIG HLVSFLQENQ INALHTTPSI YREILGLLEP GETISSLKYI
SVGGEKLDRE TALALRKRFP AEIISNVYGS TETCVGVSQY EIKENLDSEI PLGQVFHNNR
LGVLDEFNNP VPLHVIGEIC VEGAALASGY HNQPEMTQEK FKPSFLDETK TLFRTGDLGK
QTAPGIIEFM GRKDNQVKVN GYRIDPGEIE YQLTRYAPIE RAIVLPVQVN NQTQLSAYCQ
TDKTLEIAEI REFLAKFLPV YMIPSYFIFL KQFPLTRHGK LDLHSLRELK ETSKSLVNSN
YVAPRNHLES NLVSIWEKIL SKHPIGIFDN FFEIGGHSLL LSRVVTRVHK ELNVSVKLAD
FFKVPTVAGL ATLISQTQYN YQEPISAIPP QKSYPMSHGQ RRLWALEFLD QNHNAYGMPS
AYQFKGNLNI DAFENAFQQL IQRHEILRTT FTLINNQPRQ VVHNQMNFVI KQIDLTAYVS
TEQENLIEEA ISHNAKTTFD LEVGPLLKVN LLKLSQENYI VLFNMHHIIS DGWSAGVLIK
DFLSHYHAYG QENSQLMPPL RIHYKDYTSW QESQLETSKL QDQRDYWLAK LTPVPVRLNL
PVDYLRPPVK SFQGNTITWQ PEPELIDTFE KLVKAQEASL FMGLVSLVKS FLFRYTEQNE
ITIGSAIAGR NHPDLEDQIG FYVNTLVLRD QIADHDSFTD VLSKVKTTTL EAYDNQDYPF
DQIVSDLNLQ RDPSRNALFD VAIVLQNNQN IDLALNGITV NSIDPKMMTA KFDLEFIFVE
EEELYLKLIY NTDIFIHERI LLLIDLFKNW LEQVLKFAHE PLINLSLASS ENLIQEGQDL
FTEDFNF
//
