ID SIDN_EPIFI Reviewed; 1928 AA.
AC K7NCP5;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 1.
DT 27-NOV-2024, entry version 58.
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};
DE Flags: Fragment;
GN Name=sidN {ECO:0000303|PubMed:23658520};
OS Epichloe festucae var. lolii (Neotyphodium lolii) (Acremonium lolii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Epichloe.
OX NCBI_TaxID=73839;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, DOMAIN,
RP INDUCTION, AND PATHWAY.
RC STRAIN=Lp19;
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).
RN [2] {ECO:0007744|PDB:3ITE}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 617-1174, FUNCTION, CATALYTIC
RP ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=Lp19;
RX PubMed=19923209; DOI=10.1074/jbc.m109.071324;
RA Lee T.V., Johnson L.J., Johnson R.D., Koulman A., Lane G.A., Lott J.S.,
RA Arcus V.L.;
RT "Structure of a eukaryotic nonribosomal peptide synthetase adenylation
RT domain that activates a large hydroxamate amino acid in siderophore
RT biosynthesis.";
RL J. Biol. Chem. 285:2415-2427(2010).
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:19923209, PubMed:23658520).
CC SidN assembles epichloenin A by activating and incorporating three
CC trans-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:19923209). The third adenylation domain (A3) of sidN
CC incorporates the hydroxamate groups of the siderophore which forms an
CC octahedral iron complex (PubMed:19923209). The other component amino
CC acids are assembled by sidN adenylation domains A1 and A2
CC (PubMed:19923209, PubMed:23658520). {ECO:0000269|PubMed:19923209,
CC ECO:0000269|PubMed:23658520}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=40 uM for adenylation of cis-AMHO (by adenylation A3 domain)
CC {ECO:0000269|PubMed:19923209};
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000269|PubMed:19923209,
CC 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). SidN 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; JN132404; AET13876.1; -; Genomic_DNA.
DR PDB; 3ITE; X-ray; 2.00 A; A/B=617-1174.
DR PDBsum; 3ITE; -.
DR AlphaFoldDB; K7NCP5; -.
DR SMR; K7NCP5; -.
DR EvolutionaryTrace; K7NCP5; -.
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; 1.
DR FunFam; 3.30.300.30:FF:000033; Nonribosomal siderophore peptide synthase SidC; 1.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 3.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 3.
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 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; 1.
DR Pfam; PF00668; Condensation; 2.
DR Pfam; PF00550; PP-binding; 3.
DR SMART; SM00823; PKS_PP; 3.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR SUPFAM; SSF47336; ACP-like; 3.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 5.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 3.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Ligase; Multifunctional enzyme; Phosphopantetheine;
KW Phosphoprotein; Repeat.
FT CHAIN <1..>1928
FT /note="Nonribosomal peptide synthetase sidN"
FT /id="PRO_0000444382"
FT DOMAIN 65..141
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:23658520"
FT DOMAIN 1178..1255
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:23658520"
FT DOMAIN 1740..1813
FT /note="Carrier 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:23658520"
FT REGION 177..460
FT /note="Condensation 1"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:23658520"
FT REGION 640..1045
FT /note="Adenylation"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:23658520"
FT REGION 1297..1706
FT /note="Condensation 2"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:23658520"
FT REGION 1855..1920
FT /note="Condensation 3"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:23658520"
FT MOD_RES 102
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1216
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1774
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:AET13876.1"
FT NON_TER 1928
FT /evidence="ECO:0000312|EMBL:AET13876.1"
FT HELIX 636..644
FT /evidence="ECO:0007829|PDB:3ITE"
FT STRAND 648..655
FT /evidence="ECO:0007829|PDB:3ITE"
FT STRAND 664..669
FT /evidence="ECO:0007829|PDB:3ITE"
FT HELIX 670..686
FT /evidence="ECO:0007829|PDB:3ITE"
FT STRAND 693..697
FT /evidence="ECO:0007829|PDB:3ITE"
FT HELIX 702..713
FT /evidence="ECO:0007829|PDB:3ITE"
FT STRAND 717..720
FT /evidence="ECO:0007829|PDB:3ITE"
FT HELIX 727..737
FT /evidence="ECO:0007829|PDB:3ITE"
FT STRAND 740..744
FT /evidence="ECO:0007829|PDB:3ITE"
FT TURN 746..751
FT /evidence="ECO:0007829|PDB:3ITE"
FT STRAND 759..762
FT /evidence="ECO:0007829|PDB:3ITE"
FT HELIX 766..774
FT /evidence="ECO:0007829|PDB:3ITE"
FT STRAND 788..795
FT /evidence="ECO:0007829|PDB:3ITE"
FT STRAND 803..808
FT /evidence="ECO:0007829|PDB:3ITE"
FT HELIX 809..826
FT /evidence="ECO:0007829|PDB:3ITE"
FT HELIX 828..832
FT /evidence="ECO:0007829|PDB:3ITE"
FT TURN 834..836
FT /evidence="ECO:0007829|PDB:3ITE"
FT STRAND 838..840
FT /evidence="ECO:0007829|PDB:3ITE"
FT HELIX 849..859
FT /evidence="ECO:0007829|PDB:3ITE"
FT STRAND 863..866
FT /evidence="ECO:0007829|PDB:3ITE"
FT HELIX 869..874
FT /evidence="ECO:0007829|PDB:3ITE"
FT HELIX 876..882
FT /evidence="ECO:0007829|PDB:3ITE"
FT STRAND 887..890
FT /evidence="ECO:0007829|PDB:3ITE"
FT HELIX 892..898
FT /evidence="ECO:0007829|PDB:3ITE"
FT HELIX 902..904
FT /evidence="ECO:0007829|PDB:3ITE"
FT STRAND 910..916
FT /evidence="ECO:0007829|PDB:3ITE"
FT HELIX 920..926
FT /evidence="ECO:0007829|PDB:3ITE"
FT STRAND 933..938
FT /evidence="ECO:0007829|PDB:3ITE"
FT HELIX 941..943
FT /evidence="ECO:0007829|PDB:3ITE"
FT STRAND 947..951
FT /evidence="ECO:0007829|PDB:3ITE"
FT STRAND 960..964
FT /evidence="ECO:0007829|PDB:3ITE"
FT STRAND 969..973
FT /evidence="ECO:0007829|PDB:3ITE"
FT STRAND 987..993
FT /evidence="ECO:0007829|PDB:3ITE"
FT STRAND 999..1002
FT /evidence="ECO:0007829|PDB:3ITE"
FT STRAND 1008..1012
FT /evidence="ECO:0007829|PDB:3ITE"
FT STRAND 1015..1026
FT /evidence="ECO:0007829|PDB:3ITE"
FT STRAND 1032..1037
FT /evidence="ECO:0007829|PDB:3ITE"
FT HELIX 1051..1061
FT /evidence="ECO:0007829|PDB:3ITE"
FT STRAND 1066..1072
FT /evidence="ECO:0007829|PDB:3ITE"
FT STRAND 1083..1089
FT /evidence="ECO:0007829|PDB:3ITE"
FT HELIX 1108..1118
FT /evidence="ECO:0007829|PDB:3ITE"
FT HELIX 1122..1124
FT /evidence="ECO:0007829|PDB:3ITE"
FT STRAND 1129..1131
FT /evidence="ECO:0007829|PDB:3ITE"
FT STRAND 1141..1144
FT /evidence="ECO:0007829|PDB:3ITE"
FT HELIX 1146..1151
FT /evidence="ECO:0007829|PDB:3ITE"
SQ SEQUENCE 1928 AA; 214117 MW; 969E7AB22C01B7F8 CRC64;
LVAQAVKRHA TAELPRHMVP DVFMPLNCLP RNQSSKVNRK RLLEVVGREW SMQPMSPVAD
EQVDPAWCIK HRPLLEKIQG VIKIMPKTLS RSTTLSELGV DSIGAIRLSS RFKNDGHDIS
AIQVLDSVTI EDLNNHLSVK RQGTSNWKTL LSRYLDHWKP LVSRHLARDP AHFSLVPTTV
FQDGMLVETL RDPMLYWASY SWRLPSTVDI ARVRQAWQHV SKNHDILKVS FVPTAYFEQE
ETQSSGPSSM FIQLIDYNAS MDWQEIVSDS GDWQQSIQAV CANLQRTQHE NNFSSPPWRV
TILAQQDQRI MNLTIHHSLC DGEMLRSLMH DVAWAYSTAE LPVKRCQVQE AVSRLAVRYS
EPEGHKFWGD MLSPLVSQTS LGDATSNSPK AVVRKIRHRT TELQATRSTS KLTGLARRLG
ASSLSPLFRV TFGIMLTEYY EQQSVLFGEV RSERLLESQL VGAMAPLSAT YPVPFRSSGN
IKDMVHSQQI LVMDSIRYGP PQPSDVRKIL KKSRDEALYS AVYVLRQRPE DDGGSLAPWE
EFKDIFEIFV DHEFALNVLE GADDTVTISL SVDETLMSSS AQAIFLQQLD ALLIAFDKSA
PEISLSGLNA HFPLDLLSIA SSKVSAQYTS TVPPSHYIET WAKTHPEWKA VEVATGFLGS
QKIVTEDWTY KKLNETANQV ANLIIHASLH GRAIAVSLDR SLIAFAIIVG IMKSGNTYVP
IEAGLPNDRK SFLLRDSRAA MAFVCDNNFD GVELPPETKV LDTKNQSFIE NLSTQDTSDI
LNNYPENLDA YLLYTSGSTG TPKGVRVSRH NLSSFSDAWG KLIGNVAPKS LELGGVGKFL
CLASRAFDVH IGEMFLAWRF GLCAVTGERL SMLDDLPRTF RELGVTHAGI VPSLLDQTGL
VPEDAPHLVY LGVGGEKMTP RTQQIWSSSD RVALVNVYGP TEVTIGCSAG RILPDSDTRC
IGHPLGDSVA HVLAPGSNEH VKKGMAGELV IEGSLVANGY LNRPDAKGFC DINGRKMYRT
GDIVRMDADS SILFLGRKDE QVKVRGQRLE LGEVSEVIRS LSPTDIDVVT LLLNHPGTSK
QFLVSFVASS GAAVRGELRW INENYKEINN SLRQACEQTL PAYMVPDFII PISFIPLRDT
SAKTDAKALE HMFHTLSLGE LFGESSSLVN KPTTAPSRDL TSIEKQILTV VKSVVGQDDK
RDTRPRSTLF QLGLDSIASV KLSFKLKKLG FSTTVARLLQ NPTIEELGRM KNALKESHDA
EPSNSESITT RFEELEKKTM NSLKDRETTH IESIRPCMPL QEVLVAHTMS HGSEADNAYV
SHMIFELDPA VVVEHVKAAW AAVVKNTELL RTCFIDREND IVQLVIKENH ATPVWKHLSN
GTNMLKEELL SCKKEIADDI VTNIDKSPPV RFTLASCDGA DETNEMSLFM LSIHHALYDM
VSIEMIFQDF EVAYTDSSLP RRPSTLPLLE HIAAQQQNES KAKSYWTTLF DGYDHRIEKI
SPRTAQTTAR TLNASLTTLE SLCSQTNMTL SALIQGVFAY VLARTLKRPD LIFGVVLSGR
SIDVEGIDAM AAPCISTIPQ RLNIGTDGET IAELITTVQD RLFKSMEYQY TSLRSLSRWL
EISGPLFSSL FSFTKLSPPE DSGSSKSRIL KPTEGEMFLD FELALECEAD PGTDTVTLRT
RSTMFDKMEE LDALLEQMES LVTSFTRGEN KAVDGDFGSM LHTRLLPPHG SLQEESDDWS
VLEQQIRDVV VAFSGALPNE VKRTTPFIKY GIDSITTIRF STLLRKNGFW VSGADVLRNP
SVAKLATHIQ TTSSFNGTAK DSDNEASEPA GIGNWSKALL AGAVSTKVLD DVVAVYPLTP
LQAGMISATV MMDPTLYAHH HPFRLPQGTS IDQVRSAWSR LVAKHDILRT SFHEINQPRP
QLVGAVHQ
//
