ID NRPS9_ASPFU Reviewed; 1135 AA.
AC Q4WMK2;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 27-NOV-2024, entry version 114.
DE RecName: Full=Nonribosomal peptide synthetase 9;
DE EC=6.3.2.-;
GN Name=NRPS9; Synonyms=pesJ; ORFNames=AFUA_6G09610;
OS Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS Af293) (Neosartorya fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [2]
RP NOMENCLATURE.
RX PubMed=16962256; DOI=10.1016/j.gene.2006.07.008;
RA Cramer R.A. Jr., Stajich J.E., Yamanaka Y., Dietrich F.S., Steinbach W.J.,
RA Perfect J.R.;
RT "Phylogenomic analysis of non-ribosomal peptide synthetases in the genus
RT Aspergillus.";
RL Gene 383:24-32(2006).
RN [3]
RP REVIEW ON FUNCTION, AND DOMAIN.
RX PubMed=17464044; DOI=10.1099/mic.0.2006/006908-0;
RA Stack D., Neville C., Doyle S.;
RT "Nonribosomal peptide synthesis in Aspergillus fumigatus and other fungi.";
RL Microbiology 153:1297-1306(2007).
CC -!- FUNCTION: Nonribosomal peptide synthesis (NRPS) is a key mechanism
CC responsible for the biosynthesis of bioactive metabolites which are
CC potentially contributing to organismal virulence.
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. Each module is responsible for the recognition (via the A
CC domain) and incorporation of a single amino acid into the growing
CC peptide product. Thus, an NRP synthetase is generally composed of one
CC or more modules and can terminate in a thioesterase domain (TE) that
CC releases the newly synthesized peptide from the enzyme. Occasionally,
CC epimerase (E) domains (responsible for l- to d- amino acid conversion)
CC are present within the NRP synthetase. NRPS9 has the following
CC architecture: C-A-T-C. {ECO:0000269|PubMed:17464044}.
CC -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR EMBL; AAHF01000006; EAL88812.1; -; Genomic_DNA.
DR RefSeq; XP_750850.1; XM_745757.1.
DR AlphaFoldDB; Q4WMK2; -.
DR SMR; Q4WMK2; -.
DR STRING; 330879.Q4WMK2; -.
DR EnsemblFungi; EAL88812; EAL88812; AFUA_6G09610.
DR GeneID; 3508148; -.
DR KEGG; afm:AFUA_6G09610; -.
DR VEuPathDB; FungiDB:Afu6g09610; -.
DR eggNOG; KOG1178; Eukaryota.
DR HOGENOM; CLU_000022_60_3_1; -.
DR InParanoid; Q4WMK2; -.
DR OMA; GHIAAHS; -.
DR OrthoDB; 2787863at2759; -.
DR Proteomes; UP000002530; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IBA:GO_Central.
DR GO; GO:0043041; P:amino acid activation for nonribosomal peptide biosynthetic process; IBA:GO_Central.
DR GO; GO:0019184; P:nonribosomal peptide biosynthetic process; ISM:AspGD.
DR GO; GO:0019748; P:secondary metabolic process; NAS:AspGD.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IBA:GO_Central.
DR CDD; cd05918; A_NRPS_SidN3_like; 1.
DR CDD; cd19534; E_NRPS; 1.
DR FunFam; 3.30.559.30:FF:000002; Nonribosomal peptide synthase Pes1; 1.
DR FunFam; 3.30.300.30:FF:000015; Nonribosomal peptide synthase SidD; 1.
DR FunFam; 3.40.50.12780:FF:000110; Nonribosomal peptide synthase, putative; 1.
DR FunFam; 1.10.1200.10:FF:000005; Nonribosomal peptide synthetase 1; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 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 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; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR PANTHER; PTHR45527:SF3; SIDEROPHORE SYNTHETASE (EUROFUNG)-RELATED; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 2.
DR Pfam; PF00550; PP-binding; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 3.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Ligase; Phosphopantetheine; Phosphoprotein; Reference proteome; Repeat;
KW Virulence.
FT CHAIN 1..1135
FT /note="Nonribosomal peptide synthetase 9"
FT /id="PRO_0000416550"
FT DOMAIN 672..748
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 23..77
FT /note="Condensation 1"
FT REGION 177..562
FT /note="Adenylation"
FT REGION 485..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..999
FT /note="Condensation 2"
FT MOD_RES 709
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 1135 AA; 125762 MW; A2603238F2383EFB CRC64;
MPRSTPVASE QVDFVMKLLG NTTKQITTAT YIKLAWAVVI SCNTGSNDTV FGITVNGRGA
PIDGAGEMTG ATIATIPQHG CILRVWSLPR MPAGMISRER VQRLLQHLEL VLQDLMADPS
CKVGDLPRMS RQEWDQIQRW SGTLPPVSRQ CVHEIVNQRS LQFPNACAVS APDGDLSYAE
LIRSANAVAA ELLVHGVERG NYIPVLFEKC KWSPVAMLGV LKAGAAFVLL DSSYPPQRLH
TICGGLKTQI ILCSKDMYAR AASLGPTAIA IHENAAFLAD IPDVTFPVVS PENAAYVVFT
SGSTGTPKGA VIDHQSYCSG ALAHNRAHVL GRNSRVLQYA SYAFDVSIME TLSTLMAGGC
VCILSDLERH DHFANSVQRL AVTHAFLTPS TARLLMQREL PSLCVLVLGG EAMSLADRSY
WMSRVRLMNE YGIAECSVAS TIREVSHVEQ KDIGFPMGVV AWVVDQNDHE KLVAIGATGE
LLLEGPSPPV GRSSSNRAGS GRCAMGSQAG SYKTGDLVRY NEDGSLSFIS RKDSQIKIRG
QRFELEEVEQ HLRRIDEIQE ATTVVAAPSD RPKQPYLVAF IVPRARESFC VCSARALIPH
PTEEFRLQAA TIQTKLHSIL PAHMVPAIYL PVNRMPKTSS DKIDRCRLKE EVGKWSWSDL
RAYSVSSMSH RAPSNRVEQD LQRVWEQILG ILLDSVGVED SFFHLGGDSI IAMQVVAEAR
SRGLDHSVQD INQLKTIKAI ANKIGDVQRA AIKLVQNHAM LRARYVRQKD GAWKQFFTGY
TEQCFRFSVH QVKSAQEMRQ IIGESQTSLN PEHGPVFTVD LFHHGGEQSL LMIGHHLVLD
LVSWRIILAD MEAMILDPQH QPHLTMSFQT WAHLQAEYGT RHLEPPPGQQ PCSIDEPSMR
QFWGAENNAN TGGDSKTRLI RMNDDLTRKL FGPSSQALDV EPVELLHAAI LFSFVNTFPQ
RPALVIFGEA HGRETWDSSV DVTRTIGWFT TLWPVVAQVN PSDSLETVAR TVRQARRAMD
MHGWTHFTSV YHNTRQTKRS AGAHLMEITF NYAGKFQQVE QDGSLFRMEP MAKQNLFDGA
AELGRWAMLE INSVILNGLL EFHVPYNRGT DEARVLTPWM DNLVKCLEGL ASGFA
//
