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Database: UniProt
Entry: Q9K5M2_9NOST
LinkDB: Q9K5M2_9NOST
Original site: Q9K5M2_9NOST 
ID   Q9K5M2_9NOST            Unreviewed;      2258 AA.
AC   Q9K5M2;
DT   01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 128.
DE   SubName: Full=Anabaenopeptilide synthetase ApdA {ECO:0000313|EMBL:AFW94565.1};
DE   SubName: Full=Peptide synthetase {ECO:0000313|EMBL:CAC01603.1};
GN   Name=adpA {ECO:0000313|EMBL:CAC01603.1};
GN   ORFNames=ANA_C11805 {ECO:0000313|EMBL:AFW94565.1};
OS   Anabaena sp. 90.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=46234 {ECO:0000313|EMBL:CAC01603.1};
RN   [1] {ECO:0000313|EMBL:CAC01603.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=90 {ECO:0000313|EMBL:CAC01603.1};
RX   PubMed=10931313; DOI=10.1046/j.1365-2958.2000.01982.x;
RA   Rouhiainen L., Paulin L., Suomalainen S., Hyytiainen H., Buikema W.,
RA   Haselkorn R., Sivonen K.;
RT   "Genes encoding synthetases of cyclic depsipeptides, anabaenopeptilides, in
RT   Anabaena strain 90.";
RL   Mol. Microbiol. 37:156-167(2000).
RN   [2] {ECO:0000313|EMBL:AFW94565.1, ECO:0000313|Proteomes:UP000010101}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=90 {ECO:0000313|EMBL:AFW94565.1};
RX   PubMed=23148582; DOI=10.1186/1471-2164-13-613;
RA   Wang H., Sivonen K., Rouhiainen L., Fewer D.P., Lyra C., Rantala-Ylinen A.,
RA   Vestola J., Jokela J., Rantasarkka K., Li Z., Liu B.;
RT   "Genome-derived insights into the biology of the hepatotoxic bloom-forming
RT   cyanobacterium Anabaena sp. strain 90.";
RL   BMC Genomics 13:613-613(2012).
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR   EMBL; CP003284; AFW94565.1; -; Genomic_DNA.
DR   EMBL; AJ269505; CAC01603.1; -; Genomic_DNA.
DR   STRING; 46234.ANA_C11805; -.
DR   KEGG; anb:ANA_C11805; -.
DR   PATRIC; fig|46234.3.peg.2014; -.
DR   eggNOG; COG1020; Bacteria.
DR   HOGENOM; CLU_000022_0_12_3; -.
DR   Proteomes; UP000010101; Chromosome chANA01.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   CDD; cd05930; A_NRPS; 1.
DR   CDD; cd17643; A_NRPS_Cytc1-like; 1.
DR   CDD; cd08700; FMT_C_OzmH_like; 1.
DR   CDD; cd08649; FMT_core_NRPS_like; 1.
DR   CDD; cd19531; LCL_NRPS-like; 1.
DR   Gene3D; 3.30.300.30; -; 2.
DR   Gene3D; 3.40.50.12230; -; 1.
DR   Gene3D; 3.40.50.980; -; 4.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR002376; Formyl_transf_N.
DR   InterPro; IPR036477; Formyl_transf_N_sf.
DR   InterPro; IPR011034; Formyl_transferase-like_C_sf.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 2.
DR   PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR   Pfam; PF00501; AMP-binding; 2.
DR   Pfam; PF13193; AMP-binding_C; 2.
DR   Pfam; PF00668; Condensation; 1.
DR   Pfam; PF00551; Formyl_trans_N; 1.
DR   Pfam; PF00550; PP-binding; 2.
DR   SMART; SM00823; PKS_PP; 2.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 3.
DR   SUPFAM; SSF50486; FMT C-terminal domain-like; 1.
DR   SUPFAM; SSF53328; Formyltransferase; 1.
DR   PROSITE; PS00455; AMP_BINDING; 2.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010101}.
FT   DOMAIN          1087..1162
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          2163..2238
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   2258 AA;  253026 MW;  32F5D3AF06D81172 CRC64;
     MANHQNKFNC FIIGEGTLPI QCAEILINQG HVIYGIISAD ASIINWAEGK NIPYIKPTDH
     LGEFLSQQPF DYLFSIVNRY VLPQEILELP RQFAINYHDA PLPRYAGVNA TSWALMNQEK
     THGVTWHIMA AMVDAGDILK QVIIDIADDE TALTLNGKCY ESAINAFAQL VDELSSGTFV
     ATKVNLNQRT YFSRFKRLRA GGIISWKRCA YELDALIRAL DFGSYPNPLG RPKLAIDSNL
     FIVSKLEVQG NLSNYPPGTI TNIEPTYITV STASYDIALR QVLAINSQAL SISYLVEKFG
     LQVGYQFCDL EPNQVKQIEK FDQSIVKHEA FWVERLGILE SITIPEAKQT ASLHLKEPQY
     ARARMFVPDE AITLWLQRHP QWHRSDFLAA AFITYLARIG GSGCFDIGFK DIELQRQLVG
     LESLFASVVP YRVNIDYEQS FAALKKQFEF TQLPLTYVRD VVTRYPSLRS LSDHRGSEQF
     FPVVVERVEK LEDYQSPLGS DLTFIISSDG KKCCWFYNTD VLNDDSIARM QEQFTVFLQG
     ILTEPDQCIA YLPLLSEQQR REILLEWNDT QVDDPQDKCI HQLFESQVDL TPDAVAVVFE
     NQQLTYHELN CRANQLAHYL QSLGVGTDVL VGICVERSLE MVVGLLGILK AGGAYVPLDP
     EYPTERLTFM LADAQVSVLL TQQHLVEKLP ENQEPVVCLD TDWLVICESS QESPITEVQP
     GNLAYVIYTS GSTGTPKGVM LSHSNLCNHM SWMQATFPLT EKDKVLQKTP FGFDASVWEF
     YAPLLAGGQL LIAKPGGHTD SAYLLRLIAQ QQVTIVQLVP SLLQMLLEQG GIETCHSLKH
     VFCGGEVLPV ALLEGLLSKL DVNLHNLYGP TETCIDATFC NCQREIYAQI VPIGRPISNT
     QIYILDQNLQ ALPVGVPGEL HISGAGLARG YLNRPELTQE KFIANPFSTY PGSRLYKTGD
     LARYLPNGNI EYLGRIDNQV KIRGFRIELA EIEAVLNQRD DVQVACVIAR EDDPGNKRLV
     GYIVPSSQMT CTVSELPQFL KTKLPDYMVP NIFVMLDSLP LTPNGKINRG ALPVPDLQGQ
     GTDKYVAPRT PTEEILSLIW AQVLKLEQVG IHDNFFTFGG HSLLATQLVS RIRTSFKVEL
     PLRSLFAAPT VAQLSPHIQR LQQQELELTS PPILPRAENA ELPLSYAQQR LWFLDQLQPN
     SSLYNIPIAL RLVGTLNQAA LAQSLEEIIH RHEALRTNFI TVDGTPRQVI QTATNWTVSV
     VNFRHLSTSA QEIAAQQLAQ KQAIQSFDLA SEVLIRVTLV VLSETEHLLN VCMHHIVSDG
     WSMGVFVAEL AALYNAYSIG LPSLPDATRI PLTPLPIQYA DFAIWQRNWL VGDVLQSQLN
     YWQQQLKDAP ALLVLPTDRP RPAVQTFVGA YQDFALSVEL TQGLMQLSQQ QDCTLFMTLL
     AAFDTLLYRY TGTEDILVGT PIANRDRSEI EGLIGFFVNT LVMRSNLSEN PSFAELLTRV
     RSMALSAYAH QNLPLEMLVE ALQPERDLSH TPLFQVMFAL QNPYLSEVEL SGLSISSLPI
     EGATAKFDLT LAMENTGNGL IGVWEYNTDL FDASTIERMT GHFLTLLSSI VANPLEQISQ
     LPLLTEVERQ QLLIEWNHTQ VNYPVDQCIH QLFESQVERT PDAVAVVFEE QQLTYHELNC
     RANQLAHYLQ SLGVGADVLV GICVERSWEM IVGLLGILKA GGAYVPLDPE YPPERLSFIL
     TDTQVKVLLT QQQLVNKLPA HTAQLVCLDT DLEKITQNSN SNPVNTATSP NLAYVIYTSG
     STGQPKGVLV NHHHVTRLFA ATNSWYKFNS QDVWTMFHSY AFDFSVWEIW GALLYGGRLV
     VVPYLLTRSP ESFYKLLSQE QVTILNQTPS AFRQLIQAEQ SIGMSNLNLR LVIFGGEALE
     LESLQPWFER HGDQKPQLVN MYGITETTVH VTYRPLSLDD LNRTASVIGR PIPDLQVYVL
     DQHLQPVPIG VPGEMYVGGE GVTRGYLHRD ELTGQRFISN PFQRSKGGER LYRTGDLARY
     LPNGELEYLG RIDQQVKIRG FRIELGEIEG LLAQHPAVWE SVVVVREDEP SNKRLVAYVV
     PQVAQAPTTA ELRSFLKKKL PDYMIPNAIV ILESLPLTSN GKIDRRSLPV PESRAGIEES
     LVAPRTPVEE KLAQIWAKVL RVEQVGIHDN FFELGGHSLL ATQLVSRIRT SFKVELPLRS
     LFAAPTVAEL APLIQQLQQQ NIEIKVPPIL PRKKNAKS
//
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