ID SIDN_EPIFE Reviewed; 4690 AA.
AC K7NCX6;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 1.
DT 27-NOV-2024, entry version 44.
DE RecName: Full=Nonribosomal peptide synthetase 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 E2368).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Epichloe.
OX NCBI_TaxID=696363;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, DOMAIN,
RP INDUCTION, AND PATHWAY.
RC STRAIN=E2368;
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 synthetase 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}.
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DR EMBL; JN132403; AET13875.1; -; Genomic_DNA.
DR SMR; K7NCX6; -.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0043041; P:amino acid activation for nonribosomal peptide biosynthetic process; IEA:TreeGrafter.
DR GO; GO:0010106; P:cellular response to iron ion starvation; IEA:TreeGrafter.
DR GO; GO:0031169; P:ferrichrome biosynthetic process; IEA:TreeGrafter.
DR CDD; cd05918; A_NRPS_SidN3_like; 2.
DR FunFam; 3.30.300.30:FF:000015; Nonribosomal peptide synthase SidD; 1.
DR FunFam; 3.30.300.30:FF:000033; Nonribosomal siderophore peptide synthase SidC; 1.
DR FunFam; 3.40.50.12780:FF:000024; Nonribosomal siderophore peptide synthase SidC; 2.
DR Gene3D; 3.30.300.30; -; 3.
DR Gene3D; 1.10.1200.10; ACP-like; 3.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 5.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 3.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 5.
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_com.
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 PANTHER; PTHR45527:SF2; FERRICROCIN SYNTHETASE (NONRIBOSOMAL PEPTIDE SIDEROPHORE SYNTHASE ) (EUROFUNG); 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
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; SSF56801; Acetyl-CoA synthetase-like; 3.
DR SUPFAM; SSF47336; ACP-like; 4.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 10.
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 synthetase sidN"
FT /id="PRO_0000444381"
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 925..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; 516329 MW; B696F23D447239C9 CRC64;
MDQVAVTRFP ALHCFEGPKQ RQSVGSNARH HTIRGNIDTQ HQSQDETLRR FANFVSSLVG
DDEISFDFII SPSNGGSDIA ESGTAQAKKD PTQATSDYNG ITLLRSTPFV ESGHSEFGII
IRRQLRNNDS SLFTLEKSFV VAVDKSSYSV RICRDLVPRP LLQSISTSLC SYMGWTNPSQ
HSEEESNQEL QLQTLNFQGQ SVLNHPPLMT PPDFESQLCL PKRPQEYAKP LLHNAFLARV
RENPGRIALD ALSSTGRATY TYKSLDDLSS DLAEKILQII GVDADHTDRN ITVALSTSAE
LYIAWLGILK AGCVVSPVPT DCPSGLLQHM TGLTSSKVVL GSAETLEYFD RIIGDSSTFT
FINVETIARQ NYEHLLQRPP PLVNTSENDV AYILFTSGST GKPKGVQITH HAAVCSIAAN
IAASPYSFES GPSSIRWFQM AAPTFDLSVL EIFVTFSIGG TICACDRTMM LTDAESVITQ
LEATITMTTP TLASLLRPSR IPKLREVWVC GEMLKREASE LFARDRDPSV ADGDTNLLNA
YGPTEATITC TVDARVSLKH RGSLIGPPLP TCSNIILDSS EPPKAVPLGF AGELAIGGPQ
LSIGYLKSPE KTAAAFVDVE PYGKLYRTGD MARLIMGPDG TLQVEFLGRL SSDQIKILGR
RVELGEIEAG LRNPLIAEVA AVALKPEVSG LPQVQLIAVV TCRTEKSDSD ILAACQERAE
NVLQPHMRPS IYYVMDKLPR LASEKTDRKT LAKYCLSPEK SGLRRLRNGD VDGHREAGSS
SIPMLQSVIE AVSSVAIVGS DKITSATTLL SLGIDSLRSV RLLQNFREIG IEGLQVTDIL
TCHNLGDLDT KAQQALNRST PSLAKARNLQ TLLIDFENRH KKQCLSALGF NEDNIVSFLP
VTTSQAVALA SFLLTADANG FQAVPGGKAF IQHTVYTVKP ELNSQRIVES WTRVLSRYDI
MRSVFVEVND DLTPFAQCIL SPDHEAAQIK PHFYSAKSDN ECKDVIQAAQ KAAEEKISLY
EPPRRLSVVQ SPTQTIIVFS QLHSVFDGGS ETLLLEDIER EYFGQPSIER TGVLTAVERH
FSENRAEAAQ FWQAYMDGFL SPSFPCLRST VPGPDENVCG GYSFMSDLSL ESLTRQAAAL
QCSPLSILQA AWAQILFTYT GERDVAFGNT MSGRFTTELV NCSAPVLTIQ STRVNLNEEN
DKRNIDILLE RTAQNTAALS YLHTPITGAR YDTTIALQMY LNSGKGEALY ERVCHPGMQN
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
VNRKRLLEVI GREWSMQPMS PVADEQVDPA WCIKHRPLLE KIQGVIKIMP TTLSRSTTLS
ELGVDSIGAI RLSSRLKNDG HDISAIQVLD SVTIEDLINH LSVKRQGTSN WKTLLSRYLD
HWKPLVSRHL ARDPAHFSLV PTTVFQDGML VETLRDPMLY WASYSWRLPS TVDIARVRQA
WQHVSKNHDI LKVSFVPTAY FEQEETQSSG PSSMFIQLID YNASMGWQEI 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 FLGSQKIVTE DWTYKKLNET ANQVANLIIH ASLHGRAIAV
SLDRSLIAFA IIVGIMKSGN TYVPIEAGLP NDRKSFLLRD SRAAMAFVCD NNFDGVELPP
ETKVLDTKNQ 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 LGRMKNALKG SHHAEPSNSE SITTRFEELE KETMNSLKDR ETTHIESIRP
CMPLQEVLVA HTMSHGSEAD NAYVSHMIFE LDPAVVVEHV KAAWAAVVKN TELLRTCFID
RENDIVQLVI KENHATPVWK HLSNGTNMLK EELLSCKKEI ADDIVTNIDK SPPVRFTLAS
CDGADETNEM SLFMLSIHHA LYDMVSIEMI FQDFEVAYTD SSLSRRPSTL PLLEHIAAQQ
QNESKAKSYW TTLFDGYDHR 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 SPNEVKRTTP FIKYGIDSIT
TIRFSTLLRK NGFWVSGADV LRNPSVAKLA THIQTTSSFN GTAKDSDDEA SESAGIGNWS
KALLAGAVST KVLDDVVAVY PLTPLQAGMI SATVMMDPTL YAHHHPFRLP QGTSIDQVRS
AWSRLVAKHD ILRTSFHEIN QPRPQLVGAV HQESILNWHE VATEDVQVAI DDLIKRTQFP
SVSSFETPPV KATVIRSPED MLLVVSLHHA TYDGTSIRFI FEDLWAILRG NRVPERNPFY
ETAMKIHNMS SGSVGFWADS LSGYGGAAAI AEAEDIQNKM TSKTMLLAQD TSALEQWCTE
KGITIQTICQ LAVSKAVCAQ TKSRDVVLGQ VHAARLDING ADKVAGPMLN TVPLRLCIHD
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
YYTAGRSAEL EGIEALASPT LNMLPVAVPK DLVASQLAGT SLSILLQSFQ DRTNSQSDYE
QSRLRDVIKW APNKGVSPLF NAHLNILWND EILLKPQVSK DTLLRPWPLG VPSDYASPTP
LSRGSSVDGL DTSFLPTNVL FADVGPSRET ANLAIGIGCD PTLRDAQGLE EIARMFSGHL
SRLVGSRDLV
//
