We will be switching to the new UniProt website soon. Please explore and share your feedback.
Take me to the new website.
UniProtKB - A1DA59 (FTMA_NEOFI)
Protein
Nonribosomal peptide synthetase 13
Gene
NRPS13
Organism
Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus)
Status
Functioni
Catalyzes the condensation of L-tryptophan and L-proline to produce brevianamide F, the first step of verruculogen biosynthesis pathway. Brevianamide F is the precursor of a variety of fungal prenylated alkaloids with biological activity, including fumitremorgins A, B and C and tryprostatin B. Nonribosomal peptide synthesis (NRPS) is a key mechanism responsible for the biosynthesis of bioactive metabolites which are potentially contributing to organismal virulence (By similarity).
By similarityCatalytic activityi
: Alkaloid biosynthesis Pathwayi
This protein is involved in Alkaloid biosynthesis.View all proteins of this organism that are known to be involved in Alkaloid biosynthesis.
GO - Molecular functioni
- isomerase activity Source: UniProtKB-KW
- ligase activity Source: UniProtKB-KW
GO - Biological processi
- alkaloid metabolic process Source: UniProtKB-KW
Keywordsi
Molecular function | Isomerase, Ligase |
Biological process | Alkaloid metabolism, Virulence |
Names & Taxonomyi
Protein namesi | Recommended name: Nonribosomal peptide synthetase 13 (EC:6.3.3.-)Alternative name(s): Brevianamide F synthase Fumitremorgin biosynthesis protein A |
Gene namesi | Name:NRPS13 Synonyms:ftmA, ftmPS ORF Names:NFIA_093690 |
Organismi | Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus) |
Taxonomic identifieri | 331117 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Aspergillaceae › Aspergillus › Aspergillus subgen. Fumigati › |
Proteomesi |
|
Organism-specific databases
VEuPathDBi | FungiDB:NFIA_093690 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000424110 | 1 – 2212 | Nonribosomal peptide synthetase 13Add BLAST | 2212 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 629 | O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation | 1 | |
Modified residuei | 1715 | O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation | 1 |
Keywords - PTMi
Phosphopantetheine, PhosphoproteinFamily & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 592 – 669 | Carrier 1PROSITE-ProRule annotationAdd BLAST | 78 | |
Domaini | 1678 – 1757 | Carrier 2PROSITE-ProRule annotationAdd BLAST | 80 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 74 – 473 | Adenylation 1By similarityAdd BLAST | 400 | |
Regioni | 708 – 973 | Condensation 1By similarityAdd BLAST | 266 | |
Regioni | 1167 – 1564 | Adenylation 2By similarityAdd BLAST | 398 | |
Regioni | 1815 – 2070 | Condensation 2By similarityAdd BLAST | 256 |
Domaini
NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module. Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product. Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) that releases the newly synthesized peptide from the enzyme. Occasionally, epimerase (E) domains (responsible for l- to d- amino acid conversion) are present within the NRP synthetase. NRPS13 has the following architecture: A-T-C-A-T-C (By similarity).By similarity
Sequence similaritiesi
Belongs to the NRP synthetase family.Curated
Keywords - Domaini
RepeatPhylogenomic databases
eggNOGi | KOG1176, Eukaryota KOG1178, Eukaryota |
HOGENOMi | CLU_000022_60_2_1 |
OMAi | RFHYIST |
OrthoDBi | 4243at2759 |
Family and domain databases
Gene3Di | 1.10.1200.10, 2 hits 3.30.300.30, 2 hits 3.30.559.10, 2 hits 3.40.50.12780, 2 hits |
InterProi | View protein in InterPro IPR010071, AA_adenyl_domain IPR036736, ACP-like_sf IPR045851, AMP-bd_C_sf IPR020845, AMP-binding_CS IPR000873, AMP-dep_Synth/Lig IPR042099, ANL_N_sf IPR023213, CAT-like_dom_sf IPR001242, Condensatn IPR009081, PP-bd_ACP IPR006162, Ppantetheine_attach_site |
Pfami | View protein in Pfam PF00501, AMP-binding, 2 hits PF00668, Condensation, 2 hits PF00550, PP-binding, 2 hits |
SUPFAMi | SSF47336, SSF47336, 2 hits |
TIGRFAMsi | TIGR01733, AA-adenyl-dom, 1 hit |
PROSITEi | View protein in PROSITE PS00455, AMP_BINDING, 2 hits PS50075, CARRIER, 2 hits PS00012, PHOSPHOPANTETHEINE, 2 hits |
i Sequence
Sequence statusi: Complete.
A1DA59-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MALAVAAPSE WRGILPYNTS KDSPTVHSMK VATDVKNEQG EFGFWDTCVH
60 70 80 90 100
TVVREHCQRS PDSPAVNAWD GSFTYAELDS LSDAIASVLI LFGVKPESII
110 120 130 140 150
PIYMHKSRWT TVAILGVLKS GGAFTLLDPS HPRSRLEEIC KEIQARFILT
160 170 180 190 200
SEELSKQCSE MSSVLVVEHL SRACLLSPGQ AGQTPSRPEN AAYIAFTSGS
210 220 230 240 250
TGKPKGIVIE HRSYCSGARS HLKVFGIDST SRVLQFASYA FDVSIMETLS
260 270 280 290 300
TLMAGGCLCV MSESERSDPN LFVESYKNFR ISHCFMTPSF ARTVQWTECC
310 320 330 340 350
NPPPTLIVGG ELMRPSDTRA YKAMGICCMN AYGPAECSVN VSVQSRVEDG
360 370 380 390 400
VDPRNIGYTT GATAWIISPE NPEQLMPPGT VGELLVEGPI VGRGYLNDPS
410 420 430 440 450
ATRQAFIDTP GWLRRHRKGT SYQHRVYRTG DLASQDSISG ALLLHGRKDA
460 470 480 490 500
QVKIRGQRVE LPDIEHHLQQ TLPDGDAEVI VEKVTFSDDG AEKLIAFVLI
510 520 530 540 550
PPSSTGFITD NMGDRLFLAP QSQIMEQFAI SKKHLQTNLP SYMVPDIFIP
560 570 580 590 600
ISTIPQTVSG KTDRKALRTR AAALSRRDVQ CYLLSPTGDK RPPSTLKETT
610 620 630 640 650
IRSLYSKVLN LPIDLIGMDD TFLRLGGDSL QAIRLVAAAR TAGLVLHAKD
660 670 680 690 700
ILSSQSTLAE QSQRAGLIQT SDHTGEASTP FALLPVATRH DIVDLAQKQC
710 720 730 740 750
RVSSKLIEDI YPCTALQEGM FMTSLRHPGM YTGQITFDIP DRMELPRLRA
760 770 780 790 800
AWLSVVSKNA ALRTRIIETH EGLMQAVIVD DFAWEEETDE MLPSGRWEVL
810 820 830 840 850
EITKIGVPLV RFRYRPRHRQ LIMTIHHSIW DGWSLRLVHE QLQRAYIGRD
860 870 880 890 900
PLPSTSYRSF IQYGQDLPGA DEFWASELAG VNAPIFPTLP SGNYRPCVNA
910 920 930 940 950
SHRHGVRKLV STGRGEHTAA TYIHLAWSLL VAHYTDADET VYGVTVNGRS
960 970 980 990 1000
ADVPGIENIV GPTIATVPLR IRVNQEDTVK MALDQVQDSL ARMIPYEQAG
1010 1020 1030 1040 1050
LQRISRCSRD ASEACRFQTL LIIEAPADRD VACEKNEAKN FSIIRGTTQT
1060 1070 1080 1090 1100
GMDYTAFSPY AMMLIFRTSA DKSAITLDIT YDAQVIGCVE VERMAHQFEH
1110 1120 1130 1140 1150
VLRHIYKRAT GRIGDISFLG PRDIEQVQQW NSYMPPADNR FLQELIFARC
1160 1170 1180 1190 1200
SRRPQASAII SWDGSWTYRE LWAHSSFFAR QLQRYGVTRG TPVAVCLDRS
1210 1220 1230 1240 1250
RWSIAVILAV LLAGGTCVLI DLLSPRQRVR DILQIVGAGI MVNSHATAPV
1260 1270 1280 1290 1300
TSGLCPTVID VSLLVAQNDD SQTECPFNLD TWERGVGTPE DLAFIMFTSG
1310 1320 1330 1340 1350
STGHPKGIEM PHRTLSTSIY HHSAGMKVKS SSRVLHFSSY AFDVSIYEIF
1360 1370 1380 1390 1400
TTLAAGGTIC VPSEFDRMNN LSGFIQDTQV NWAFLTPSTA RSLDPADVPL
1410 1420 1430 1440 1450
LTTLVLGGEA VTHESVEAWA KGRSLINGYG PAEATICGVG NIPEAGWKSG
1460 1470 1480 1490 1500
VIGQIVGGLG WVTVPSDPNR LAAVGAVGEL LLEGPFLARG YLNLPEVTRA
1510 1520 1530 1540 1550
AFIDPPSWRT QIPAPSPYPF LYRTGDLVQY QPDGSIQYIG RKDSRIKLRG
1560 1570 1580 1590 1600
QLVDLSAVEA SLMRVYPAAI QVVADVLVSE NTTRLIAMMK LGPPVTETHD
1610 1620 1630 1640 1650
DPLFEAPDLA FNEAAASVQA RLRAIVPPYM VPSMFIPLRH IPRTLTGKTD
1660 1670 1680 1690 1700
RRQLRDKLLS LSQSDLQRYI MSSSAKTPMS DDNERRLQEI WAEVLQLPCE
1710 1720 1730 1740 1750
AIGREDSFLL LGGESLATMK MVALARRVGF VFAVADVLNN TSLSTLAQFR
1760 1770 1780 1790 1800
HLITEDDIPS PSPSLSLSTI ESQSLQKILR PLQNGGLIQG GNDIAAIHPV
1810 1820 1830 1840 1850
TAAQAFLVQR YPWSHFQFDL SGAISPSKLQ TACTTLMARF TILRTVFVEH
1860 1870 1880 1890 1900
AGHLLQLVLR EVRKCVHEIT TDEPLDDFCN SLCQQQQGVC VVNSTALPTL
1910 1920 1930 1940 1950
FTLVSNRQLN RHRLLLRLAH AQYDLTTIPL IVQALADEYN GTLRAGFSSD
1960 1970 1980 1990 2000
FSYYLNHHMR QTNDDRAHTF WNQYLSGSFM TSTDQTADTT TPQERIFHVT
2010 2020 2030 2040 2050
GSCTVTPASH PLGITTATAV KAAVCLVLAS RTGCTDIVVG QTVDARCSSA
2060 2070 2080 2090 2100
DGTLDQIVGP CTNYIPYRLS VCCSKTALEY LCSAQAQHTT SLRYSSLDLD
2110 2120 2130 2140 2150
QIVAKCTSWP SSTQFGYIVQ HQNTGADLAL SLAGCTTSSP MTSYGHVFPQ
2160 2170 2180 2190 2200
GEVWIGSTPY STGLKIDVIA PSAVLSQEDA QAMAGEVGAA LENLLACGDR
2210
PLSDLIGNTF AT
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | DS027694 Genomic DNA Translation: EAW19749.1 |
RefSeqi | XP_001261646.1, XM_001261645.1 |
Genome annotation databases
EnsemblFungii | EAW19749; EAW19749; NFIA_093690 |
GeneIDi | 4588679 |
KEGGi | nfi:NFIA_093690 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | DS027694 Genomic DNA Translation: EAW19749.1 |
RefSeqi | XP_001261646.1, XM_001261645.1 |
3D structure databases
SMRi | A1DA59 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 36630.CADNFIAP00008991 |
Genome annotation databases
EnsemblFungii | EAW19749; EAW19749; NFIA_093690 |
GeneIDi | 4588679 |
KEGGi | nfi:NFIA_093690 |
Organism-specific databases
VEuPathDBi | FungiDB:NFIA_093690 |
Phylogenomic databases
eggNOGi | KOG1176, Eukaryota KOG1178, Eukaryota |
HOGENOMi | CLU_000022_60_2_1 |
OMAi | RFHYIST |
OrthoDBi | 4243at2759 |
Family and domain databases
Gene3Di | 1.10.1200.10, 2 hits 3.30.300.30, 2 hits 3.30.559.10, 2 hits 3.40.50.12780, 2 hits |
InterProi | View protein in InterPro IPR010071, AA_adenyl_domain IPR036736, ACP-like_sf IPR045851, AMP-bd_C_sf IPR020845, AMP-binding_CS IPR000873, AMP-dep_Synth/Lig IPR042099, ANL_N_sf IPR023213, CAT-like_dom_sf IPR001242, Condensatn IPR009081, PP-bd_ACP IPR006162, Ppantetheine_attach_site |
Pfami | View protein in Pfam PF00501, AMP-binding, 2 hits PF00668, Condensation, 2 hits PF00550, PP-binding, 2 hits |
SUPFAMi | SSF47336, SSF47336, 2 hits |
TIGRFAMsi | TIGR01733, AA-adenyl-dom, 1 hit |
PROSITEi | View protein in PROSITE PS00455, AMP_BINDING, 2 hits PS50075, CARRIER, 2 hits PS00012, PHOSPHOPANTETHEINE, 2 hits |
MobiDBi | Search... |
Entry informationi
Entry namei | FTMA_NEOFI | |
Accessioni | A1DA59Primary (citable) accession number: A1DA59 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 16, 2013 |
Last sequence update: | January 23, 2007 | |
Last modified: | February 23, 2022 | |
This is version 87 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families