ID   SIDN_EPIFF              Reviewed;        4690 AA.
AC   K7NCV2;
DT   20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2013, sequence version 1.
DT   23-FEB-2022, entry version 35.
DE   RecName: Full=Nonribosomal peptide synthase sidN {ECO:0000303|PubMed:23658520};
DE            Short=NPRS sidN {ECO:0000303|PubMed:23658520};
DE            EC=6.3.2.- {ECO:0000305|PubMed:23658520};
DE   AltName: Full=Epichloenin A synthetase {ECO:0000303|PubMed:23658520};
DE   AltName: Full=Extracellular siderophore synthetase N {ECO:0000303|PubMed:23658520};
GN   Name=sidN {ECO:0000303|PubMed:23658520};
OS   Epichloe festucae (strain Fl1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Epichloe.
OX   NCBI_TaxID=877507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, DOMAIN,
RP   INDUCTION, AND PATHWAY.
RC   STRAIN=Fl1;
RX   PubMed=23658520; DOI=10.1371/journal.ppat.1003332;
RA   Johnson L.J., Koulman A., Christensen M., Lane G.A., Fraser K.,
RA   Forester N., Johnson R.D., Bryan G.T., Rasmussen S.;
RT   "An extracellular siderophore is required to maintain the mutualistic
RT   interaction of Epichloe festucae with Lolium perenne.";
RL   PLoS Pathog. 9:E1003332-E1003332(2013).
CC   -!- FUNCTION: Nonribosomal peptide synthase required for the biosynthetis
CC       of epichloenin A, an extracellular siderophore that plays a crucial
CC       role in endophyte-grass symbioses (PubMed:23658520). SidN assembles
CC       epichloenin A by activating and incorporating three trans-
CC       anhydromevalonylhydroxyornithine (trans-AMHO), 1 glutamine and 4
CC       glycine moieties (PubMed:23658520). Trans-AMHO is produced from L-
CC       ornithine via 2 steps involving a L-ornithine N(5)-monooxygenase and an
CC       AHMO-N(5)-transacylase that have still to be identified
CC       (PubMed:23658520). The third adenylation domain (A3) of sidN
CC       incorporates the hydroxamate groups of the siderophore which forms an
CC       octahedral iron complex (PubMed:23658520). The other component amino
CC       acids are assembled by sidN adenylation domains A1 and A2
CC       (PubMed:23658520). {ECO:0000269|PubMed:23658520}.
CC   -!- PATHWAY: Siderophore biosynthesis. {ECO:0000269|PubMed:23658520}.
CC   -!- INDUCTION: Expression is repressed by iron (PubMed:23658520).
CC       {ECO:0000269|PubMed:23658520}.
CC   -!- DOMAIN: NRP synthetases are composed of discrete domains (adenylation
CC       (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation
CC       (C) domains) which when grouped together are referred to as a single
CC       module (By similarity). Each module is responsible for the recognition
CC       (via the A domain) and incorporation of a single amino acid into the
CC       growing peptide product (By similarity). Thus, an NRP synthetase is
CC       generally composed of one or more modules and can terminate in a
CC       thioesterase domain (TE) that releases the newly synthesized peptide
CC       from the enzyme (By similarity). Occasionally, methyltransferase
CC       domains (responsible for amino acid methylation) are present within the
CC       NRP synthetase (By similarity). SdiN has the following architecture: A-
CC       T-C-A-T-C-A-T-C-T-C-T-C (PubMed:23658520).
CC       {ECO:0000250|UniProtKB:A0A144KPJ6, ECO:0000305|PubMed:23658520}.
CC   -!- DISRUPTION PHENOTYPE: Leads to the accumulation of the intermediate N-
CC       5-trans-anhydromevalonyl-N-5-hydroxyornithine (trans-AMHO), displays
CC       sensitivity to oxidative stress and shows deficiencies in both
CC       polarized hyphal growth and sporulation (PubMed:23658520). Changes its
CC       interaction with the plant Lolium perenne from mutually beneficial to
CC       antagonistic (PubMed:23658520). {ECO:0000269|PubMed:23658520}.
CC   -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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; JN132407; AET13879.1; -; Genomic_DNA.
DR   SMR; K7NCV2; -.
DR   PHI-base; PHI:3607; -.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1200.10; -; 3.
DR   Gene3D; 3.30.300.30; -; 3.
DR   Gene3D; 3.30.559.10; -; 5.
DR   Gene3D; 3.40.50.12780; -; 3.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   Pfam; PF00501; AMP-binding; 3.
DR   Pfam; PF00668; Condensation; 5.
DR   Pfam; PF00550; PP-binding; 4.
DR   SMART; SM00823; PKS_PP; 4.
DR   SUPFAM; SSF47336; SSF47336; 4.
DR   PROSITE; PS00455; AMP_BINDING; 3.
DR   PROSITE; PS50075; CARRIER; 5.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 3.
PE   2: Evidence at transcript level;
KW   Ligase; Multifunctional enzyme; Phosphopantetheine; Phosphoprotein; Repeat.
FT   CHAIN           1..4690
FT                   /note="Nonribosomal peptide synthase sidN"
FT                   /id="PRO_0000444380"
FT   DOMAIN          779..856
FT                   /note="Carrier 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000305|PubMed:23658520"
FT   DOMAIN          1889..1965
FT                   /note="Carrier 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000305|PubMed:23658520"
FT   DOMAIN          3002..3079
FT                   /note="Carrier 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000305|PubMed:23658520"
FT   DOMAIN          3564..3637
FT                   /note="Carrier 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000305|PubMed:23658520"
FT   DOMAIN          4119..4195
FT                   /note="Carrier 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000305|PubMed:23658520"
FT   REGION          238..656
FT                   /note="Adenylation 1"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:23658520"
FT   REGION          924..1175
FT                   /note="Condensation 1"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:23658520"
FT   REGION          1349..1760
FT                   /note="Adenylation 2"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:23658520"
FT   REGION          2001..2285
FT                   /note="Condensation 2"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:23658520"
FT   REGION          2464..2869
FT                   /note="Adenylation 3"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:23658520"
FT   REGION          3121..3530
FT                   /note="Condensation 3"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:23658520"
FT   REGION          3679..4087
FT                   /note="Condensation 4"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:23658520"
FT   REGION          4262..4589
FT                   /note="Condensation 5"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:23658520"
FT   MOD_RES         816
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         1926
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         3040
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         3598
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         4156
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   4690 AA;  516466 MW;  6C9C23C5D2430475 CRC64;
     MDQVAVTRFP ALHCFEGPKQ RQSVGSNARH HTIRGNIDTQ HQSQDETLRR FANFVSSLVG
     DDEISFDFII SPSNGGSDIA ESGTAQAKKD PTQATSDYNG ITLLRSTPFV ESGHSEFGII
     IRRQLRNNDS SLFTLEKSFV VTVDKSSYSV RICRDLVPRP FLQSISTSLC SYMGWTNPSQ
     HSEEESNQEL QLQTLNFQGQ SVLNHPPLMT PPDFESQLCL PKRPQEYAKP LLHNAFLARV
     RENPGRIALD ALSSTGRATY TYKNLDDLSS DLAEKILQII GVDADHTDRN ITVALSTSAE
     LYIAWLGILK AGCVVCPVPT DCPSELLQHM TGLTSSKVVL GSAETLEYFD RIIGDSSIFT
     FINVETIARQ NCEHLLQRPP PLVNTSENDV AYILFTSGST GKPKGVQITH HAAVCSIAAN
     IAASPHSFES GPSSIRWFQM AAPTFDLSVL EIFVTFSIGG TICACDRTMM LTDAESVITQ
     LEATITMTTP TLASLLRPSR IPKLREVWVC GEMLKREASE LFARDRDPSV ADGDTNLLNA
     YGPTEATITC TVDARVSLKH RGSLIGPPLP TCSNIILDSS EPPKAVPLGF AGELAIGGPQ
     LSIGYLKSPE KTAAAFVDVE SYGKLYRTGD MARLIMGPDG TLQVEFLGRL SSDQIKILGR
     RVELGEIEAG LRNPLIAEVA AVALKPEVSG LPQVQLIAVV TCRTEKSDSD VLAACQERAE
     NVLQPHMRPS IYYVMDKLPR LASEKTDRKT LAKYCLSPEK SGLRRLRNGD VDGHREAGSS
     SIPMLQSVIE AVSSVAIVGS DKITSATTLL SLGIDSLRSV RLLQNFREIG IEGLQVTDIL
     TCHNLGDLDT KAQQALNRST PSLAKARNLQ TLLIDFENRH KKQCLSALGF NEDNIVSFLP
     VTTSQAVALA SFLLTADANG FQAAPGGKAF IQHTVYTVKP ELNSQRIVES WTRVLSRYDI
     MRSVFVEVND DLTPFAQCIL SPDHEAAQIK PHFYSAKSDN ECKDVIQAAQ KAAEEKISLY
     EPPRRLSVVQ SPTQTIIVFS QLHSVFDGGS ETLLLEDIER EYFGQPSIER TGVLTAVERH
     FSENRAEAAQ FWQAYMDGFL SPSFPCLRST VPGPDENVCG GYSFMSDLSL ESLTRQAAAL
     QCSPLSILQA AWAQILFTYT GERDVAFGNT MSDRFTTELA NCSAPVLTIQ STRVNLNEEN
     DKRNIDILLE RTAQNTAALS YLHTPITGAR YDTTIALQMY LNSGKGEALY ERVCHPGMHN
     DLAVMIEVYP DRSGLLEFRL TYQTALLDDD AAYTMLANLA RVTNHIMSYP NAKYMDPSVW
     TSLQGPGQLE QINGYHHLGQ QLLHECVAEF AQKSPNAIAL AFYDDLSVDH PKVQLTYADL
     EVKATRVAGF LMSQLPAKEG SKHVVPIFME KCPELYITLL GILKAGAAWC PVDPSYPPAR
     QIFLIEKTTA GICFTSKSTT SQLSSILPAS FKSISVSDLL EGGSCSTSRT LKASESARLD
     NLSIQRSDIA YVIFTSGTTG TPKGVPISHE SASLSIDSYI QRVNVDLDLR GCEVRFLQFA
     NYTFDAFVCD VFTAWRLGGT LVSATRDILL GSFIALANKV GATHTSMTPT FASTLQPQDF
     ETLRVATMGG EVLPQILADK WKSRMSLCNV YGPAETAINT TINRLSAASR SGNIGTALPA
     VNAYVMASGY PVMKHMLGEL VISGPQLSPG YWDNVHSSNN RFRWNSTLQC RVYHTGDYVR
     QLADGSFDFV GRKDDLVKIR GMRVELTEIS TVCSAGHESV VHSEVLLAKL PGSTQSSLIC
     FVDCGLQKSS DVDNFCILKN EEAQLVAQAV KRHATAELPR HMVPDVFMPL NCLPRNQSSK
     VNRKRLLEVV GREWSMQPMS PVADEQVDPA WCIKHRPLLE KIQGVIKIMP TTLSRSTTLS
     ELGVDSIGAI RLSSRLKNDG HDISAIQVLD SVTIEDLINH LSVKRQGTSN WKTLLSRYLD
     HWKPLVSRHL ARDPAHFSLV PTTVFQDGML VETLRDPMLY WASYSWRLPS TVDIARVRQA
     WQHVSKNHDI LKVSFVPTAY FEQEETQSSG PSSMFIQLID YNASMDWQEI VSDSGDWQQS
     IHALCANLQR TQHENNFSSP PWRVTILAQQ DQRIMNLTIH HSLCDGEMLR SLMHDVAWAY
     STAELPVKRC QVQEAVSRLA VRYSEPEGHK FWGDMLSPLV SQTSLGDATS NSPKAVVRKI
     RHRTTELQAT RSTSKLTGLA RRLGASSLSP LFRVTFGIML TEYYEQQSVL FGEVRSERLL
     ESQLVGAMAP LSATYPVPFR SSGNLKDMVH SQQILVMDSI RYGPPQPSDV RKILKKSRDE
     ALYSAVYVLR QRSEDDGGSL APWEEFKDIF EIFVDHEFAL NVLEGADDTV TISLSVDETL
     MSSSAQAIFL QQLDALLIAF DKSAPEISLS GLNAHFPLDL LSIASSKVSA QYTSTVPPSH
     YIETWAKTHP EWKAVEVATG FLGSQEIVTE DWTYKKLNET ANQVANLIIY ASLHGRAIAV
     SLDRSLIAFA IIVGIMKSGN TYVPIEAGLP NDRKSFLLRD SRAAMAFVCD NKLDGVELPP
     ETKVLDTKNK SFIENLSTQD TSDILNNYPE NLDAYLLYTS GSTGAPKGVR VSRHNLSSFS
     DAWGKLIGNV APKSLELGGV GKFLCLASRA FDVHIGEMFL AWRFGLCAVT GERLSMLDDL
     PRTFRELGVT HAGIVPSLLD QTGLVPEDAP HLVYLGVGGE KMTPRTQQIW SSSDRVALVN
     VYGPTEVTIG CSAGRILPDS DTRCIGHPLG DSVAHVLAPG SNEHVKKGMA GELVIEGSLV
     ANGYLNRPDA KGFCDINGRK MYRTGDIVRM DADSSILFLG RKDEQVKVRG QRLELGEVSE
     VIRSLSPTDI DVVTLLLNHP GTSKQFLVSF VASSGAAVRG ELRWINENYK EINNSLRQAC
     EQTLPAYMVP DFIIPISFIP LRDTSAKTDA KALEHMFHTL SLGELFGESS SLVNKPTTAP
     SRDLTSIEKQ ILTVVKSVVG QDDKRDARPG STLFQLGLDS IASVKLSFKL KKLGFSTTVA
     RLLQNPTIEE LGRMKNALKE SHDAEPSNSE SITTRFEELE KKTMNSLKDR ETTHIESIRP
     CMPLQEVLVA HTMSHGSEAD NAYVSHMIFE LDPAVVVEHV KAAWAAVVKN TELLRTCFID
     RENDIVQLVI KENHATPVWK HLSNGTNMLK EELLSCKKEI ADDIVTNIDK SPPVRFTLAS
     CDGADETNEM SLFMLSIHHA LYDMVSIEMI FQDFEVAYTD SSLPRRPSTL PLLEHIAAQQ
     QNESKAKSYW TTLFDGYDHG IEKISPRTAQ TTARTLNASL TTLESLCSQT NMTLSALIQG
     VFAYVLARTL KRPDLIFGVV LSGRSIDVEG IDAMAAPCIS TIPQRLNIGT DGETIAELIT
     TVQDRLFKSM EYQYTSLRSL SRWLEISGPL FSSLFSFTKL SPPEDSGSSK SRILKPTEGE
     MFLDFELALE CEADPGTDTV TLRTRSTMFD KMEELDALLE QMESLVTSFT RGENKAVDGD
     FGSMLHTRLL PPHGSLQEES DDWSVLEQQI RDVVVAFSGA LPNEVKRTTP FIKYGIDSIT
     TIRFSTLLRK NGFWVSGADV LRNPSVAKLA THIQTTSSFN GTAKDSDNEA SEPAGIGNWS
     KALLAGAVST KVLDDVVAVY PLTPLQAGMI SATVMMDPTL YAHHHPFRLP QGTSIDQVRS
     AWSRLVAKHD ILRTSFHEIN QPRPQLVGAV HQESILNWHE VATEDVQVAI DDLIKRTQFP
     SVSSFETPPV KATVIRSPED MLLVVSLHHA TYDGTSIRFI FEDLWAILRG NRVPERNPFY
     ETAMKIHNMS SGSVGFWADS LSGYGGAAAI AEAEDIQNKM TSKTMLLAQD TSALEQWCTE
     KGVTIQTICQ LAVSKAVCAQ TKSRDVVLGQ VHAARLDING ADKVAGPMLN TVPLRLCIYD
     DSFTNHDYLR DLQAFQNKSL DHLHASLSDI QRLWRKENGR DGQLFEVLFI FRKGEDATEA
     PFWQPFEPEG SKESLPPSHY DLVIEVHQKS RGGLELEVHS RFADDTTSNL MSLLVESFES
     IRKHPDELAI SSPGVLSKVP KPGLTRETGA VPTSPFDQSA IDQFLDPLRK VLSETTDTPV
     SSIDAQTSIF SIGVDSIVAI RVAGACRKAH IPLHTMEIMR NAKIGKLCEV AFAKSGQAAP
     NRSTTESNGV APLLDQEVKK AAASKLGRAE AEIQEILPVL PGQEYHLACW LTSGKTLLEP
     VWVFKAENGL DAGRLRDTWI SLVQKNDSLR TCFAQVKPTL AVQAILKPDC VDAAKSFTVQ
     QVPENMTMEE YVKSEIHHLS LSPSSLYEPP VRIVLIQGGR EGVSVLLRLH HALYDAWSMG
     ILIDELSSLY CGTMQKPCPP LSVSHFAQFT QQKLRGKNEE QFWTETLGQC DPTILTPKAD
     INTDSKSCNR AFVSFECVDV SMGALKSAAR AFGITPQCLI QVAFGRMLSD VTESSSPVFG
     YYTAGRSADL EGIEALASPT LNMLPVAVPK DLVASQLAGT SLSILLQSFQ DRTNSQSDYE
     QSRLRDVIKW APNKGVSPLF NAHLNILWND EILLKPQVSK DTLLRPWPLG VPSDYASPTP
     LSRGSSVDGL DTSFLPTNVL FADVGPSRET ANLAIGIGCD PTLRDAQGLE EIARMFSGHL
     SRLVGSRDLV