ID NRPS6_ASPFU Reviewed; 1290 AA.
AC Q4WYP0;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=Nonribosomal peptide synthetase 6;
DE EC=6.3.2.-;
GN Name=NRPS6; Synonyms=pesG; ORFNames=AFUA_3G13730;
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. NRPS6 has the following
CC architecture: A-T-C. {ECO:0000269|PubMed:17464044}.
CC -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR EMBL; AAHF01000002; EAL92213.1; -; Genomic_DNA.
DR RefSeq; XP_754251.1; XM_749158.1.
DR AlphaFoldDB; Q4WYP0; -.
DR SMR; Q4WYP0; -.
DR STRING; 330879.Q4WYP0; -.
DR EnsemblFungi; EAL92213; EAL92213; AFUA_3G13730.
DR GeneID; 3512418; -.
DR KEGG; afm:AFUA_3G13730; -.
DR VEuPathDB; FungiDB:Afu3g13730; -.
DR eggNOG; KOG1178; Eukaryota.
DR HOGENOM; CLU_000022_60_3_1; -.
DR InParanoid; Q4WYP0; -.
DR OMA; QIENLAW; -.
DR OrthoDB; 1818010at2759; -.
DR Proteomes; UP000002530; Chromosome 3.
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; cd19542; CT_NRPS-like; 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; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR045851; AMP-bd_C_sf.
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 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; 1.
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; 2.
DR PROSITE; PS50075; CARRIER; 1.
PE 3: Inferred from homology;
KW Ligase; Phosphopantetheine; Phosphoprotein; Reference proteome; Repeat;
KW Virulence.
FT CHAIN 1..1290
FT /note="Nonribosomal peptide synthetase 6"
FT /id="PRO_0000416547"
FT DOMAIN 775..851
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..657
FT /note="Adenylation"
FT REGION 846..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 914..1162
FT /note="Condensation"
FT COMPBIAS 13..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..870
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 812
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 1290 AA; 141796 MW; 8E03CF4ABCAC8611 CRC64;
MTAIDVPWLS TPRRDNSHGT RSNSSCQPSC TQRIAVPISP DAVKYPLAVF CFAWAVTLGA
YLDSQELVIG FAFHGWDGDT SIPSAGTCRI RIRPEQEILP ALDEVVADGD KGLRSWVAQG
AGSETDIAIQ RKEVGDSLHP AVHGDEKLSP EIIITPSGNQ GPYHVQGRFD PHIVAPALAH
MMLHQFAFAV QGIVRGQSSI ASSQVKDLQA ISPDGMAQLM RWNRQSAAEE DGACVQDLIQ
RTCQQQPHAM AVCAWDGSWS YQELDCQASH LASQLCDHGI EPEKFVGLLF EKSKWTTVAI
LAVLKAGGAF VLLDPTQPAA YLSAICTMTR TALLLCSSHN QRLAAELRQT TIQVPRDPYH
GAMPTSDFRR QSSPAVQPHH TLYACFTSGS TGRPKGFIID HVAFNSGLQT YAHATGLGCD
SRVFQFASYS FAPSITDQLA SLIVGASICV PAEEELQNDV EGSISQLQAT WLKLTPSVAR
TLDPGRLPCV KTLILVGEEA QVSDVAAWQD HGITVLGLYG QSENAKGTMV SRKSSEDADP
GNIGSPFCAV GWVVDPDDYH RLMPIGATGE LLLESPCLCR GYIDNEDETK LAFVSKPSWL
TQVRGQGTAQ PLLRTGDIVR YNCVDGTFCL VGRKGNRVKL RGQRLELAQV EHHLRSCLSS
THPVLADVVQ PANENGRDPM LVAFVPWADS QSAADATDGF FAPPTKDFQT QARAVLGRLR
HLLPSFMVPS TLLAVRTIPR TGTGKIHRRR LQEAASMLSR KQLMAYISPF IPYRAPETEL
ERKLQRACGR LLNIEADQIS MQDNFFDLGG NSLTARQLVA VARAEGLQVS VAQIFQQPTL
AGLAQTHRHP VRRAEVPRSS HDPDPFGRVR DDVRREGLPH IARGNIEDAL PVLYTQMTTA
RDHCVDFFPL RVIGGQLDPE QLRLAWTRVI QAFPILRTVF PRFRGRFIQL VVRDIGDSNF
YRVVEAPSGQ TAEEWARALC TEAIQFRCPV DRPVAQLTLI QAAGSSALVL RLCHAQYDGS
CLEHLVRSLM MAYHGRPLVV ESDFQAYTRT CLRLRIPEVL DFWRRFLAGS SPTQLASSMT
GDREAARKIN RSFFRREVNS LAAPAGFTLA TVVKAAWSWV LRNETRSEDV VFGQLVSCRG
SVPLPHADTI IGPCMNIIPV RVGRDLLGAV QAQHAQTMEF DMIGMDEIVR HCTSWPAGTE
PDSIIIHENF HVDWEVHDGG VTIQKIAAVF NQQPSSLTFL ITIPTETGLI AVLMAPANMS
STHADRVLDL FCNTLTRLAW SPAAVLRRSE
//
