UniProtKB - Q4WZ67 (EASL_ASPFU)
Fumigaclavine A dimethylallyltransferase easL
easL
Functioni
Fumigaclavine A dimethylallyltransferase; part of the gene cluster that mediates the biosynthesis of fumiclavanine C, a fungal ergot alkaloid (PubMed:15933009, PubMed:22453123).
DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:15870460).
The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity).
The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by EasD in the presence of NAD+, resulting in the formation of chanoclavine-I aldehyde (PubMed:20039019, PubMed:20526482, PubMed:21409592).
EasA reduces chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline (PubMed:20526482).
EasG then catalyzes the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine (PubMed:20526482).
Hydrolysis of festuclavine by easM then leads to the formation of fumigaclavine B which is in turn acetylated by easN to fumigaclavine A (PubMed:26972831).
Finally, easL catalyzes the conversion of fumigaclavine A into fumigaclavine C by attaching a dimethylallyl moiety to C-2 of the indole nucleus (PubMed:19672909).
By similarity8 PublicationsCatalytic activityi
- EC:2.5.1.1001 Publication
Kineticsi
- KM=6 µM for fumigaclavine A1 Publication
- KM=13 µM for dimethylallyl diphosphate1 Publication
: ergot alkaloid biosynthesis Pathwayi
This protein is involved in the pathway ergot alkaloid biosynthesis, which is part of Alkaloid biosynthesis.1 PublicationView all proteins of this organism that are known to be involved in the pathway ergot alkaloid biosynthesis and in Alkaloid biosynthesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 112 | L-tryptophanBy similarity | 1 | |
Binding sitei | 126 | SubstrateBy similarity | 1 | |
Binding sitei | 211 | SubstrateBy similarity | 1 | |
Binding sitei | 213 | SubstrateBy similarity | 1 | |
Binding sitei | 281 | SubstrateBy similarity | 1 | |
Binding sitei | 283 | SubstrateBy similarity | 1 | |
Binding sitei | 285 | SubstrateBy similarity | 1 | |
Binding sitei | 357 | SubstrateBy similarity | 1 | |
Binding sitei | 422 | SubstrateBy similarity | 1 | |
Binding sitei | 426 | SubstrateBy similarity | 1 |
GO - Molecular functioni
- dimethylallyltranstransferase activity Source: AspGD
- peptidase activity Source: AspGD
- prenyltransferase activity Source: AspGD
- protein homodimerization activity Source: UniProtKB
- transferase activity, transferring alkyl or aryl (other than methyl) groups Source: UniProtKB
GO - Biological processi
- alkaloid biosynthetic process Source: AspGD
- ergot alkaloid biosynthetic process Source: UniProtKB
- fumigaclavine C biosynthetic process Source: GO_Central
Keywordsi
Molecular function | Transferase |
Biological process | Alkaloid metabolism |
Enzyme and pathway databases
UniPathwayi | UPA00327 |
Protein family/group databases
MEROPSi | M77.002 |
Names & Taxonomyi
Protein namesi | Recommended name: Fumigaclavine A dimethylallyltransferase easLCurated (EC:2.5.1.1001 Publication)Alternative name(s): Ergot alkaloid synthesis protein L1 Publication |
Gene namesi | Name:easL1 Publication Synonyms:fgaPT11 Publication ORF Names:AFUA_2G17990 |
Organismi | Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
Taxonomic identifieri | 330879 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Aspergillaceae › Aspergillus › Aspergillus subgen. Fumigati › |
Proteomesi |
|
Organism-specific databases
VEuPathDBi | FungiDB:Afu2g17990 |
Pathology & Biotechi
Biotechnological usei
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000421749 | 1 – 436 | Fumigaclavine A dimethylallyltransferase easLAdd BLAST | 436 |
Expressioni
Inductioni
Interactioni
Subunit structurei
Homodimer.
1 PublicationGO - Molecular functioni
- protein homodimerization activity Source: UniProtKB
Protein-protein interaction databases
STRINGi | 746128.CADAFUBP00003301 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 24 | DisorderedSequence analysisAdd BLAST | 24 | |
Regioni | 103 – 104 | L-tryptophan bindingBy similarity | 2 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 7 – 22 | Polar residuesSequence analysisAdd BLAST | 16 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | ENOG502S2XP, Eukaryota |
HOGENOMi | CLU_037431_0_0_1 |
InParanoidi | Q4WZ67 |
OMAi | LFARNHI |
OrthoDBi | 1531660at2759 |
Family and domain databases
CDDi | cd13929, PT-DMATS_CymD, 1 hit |
InterProi | View protein in InterPro IPR033964, Aro_prenylTrfase IPR017795, Aro_prenylTrfase_DMATS IPR012148, DMATS-type_fun |
PANTHERi | PTHR40627, PTHR40627, 1 hit |
Pfami | View protein in Pfam PF11991, Trp_DMAT, 1 hit |
PIRSFi | PIRSF000509, Trp_DMAT, 1 hit |
SFLDi | SFLDS00036, Aromatic_Prenyltransferase, 1 hit |
TIGRFAMsi | TIGR03429, arom_pren_DMATS, 1 hit |
i Sequence
Sequence statusi: Complete.
10 20 30 40 50
MTKTDAQGRH PQETATHAAT TDEEVQDQWR APFEVLSRTL VFQHEDHRLW
60 70 80 90 100
WERAASKLAT YLRLAKYSVG SQYQHLLMFY SVYAPNLGPW PNDKRDNVHW
110 120 130 140 150
VCGICPGGEN LEISMNYQQG AKCTVRIAAE TITPAAGTDK DPFNLTAEKK
160 170 180 190 200
MIEDLKALQP NLNFTWFNHF QREVLVPEEV ALNNDEIISK VPFKNQRLHG
210 220 230 240 250
LDLSEGAFML KSYFMPAIRS AITGVENTQI MFESIRKLNL KNANFISALS
260 270 280 290 300
TLEDWMVPTN GRFMEYWDGI SYDAVDACKA RIKIYTGIRM KSIEHARDVW
310 320 330 340 350
TLGGRLQGED IEKGFDLVAR LWRRLMDEEP STCEMKYWMQ WVWELRTDVP
360 370 380 390 400
FPVPKLYFSV AAAEDHYVSD TVVEILDYLG WDDLVQTHRA LMDEAWSLGQ
410 420 430
TTKSYLAFSY ISVTFHSIKG PYITTYGNPS GPRPVF
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AAHF01000001 Genomic DNA Translation: EAL94098.1 |
RefSeqi | XP_756136.1, XM_751043.1 |
Genome annotation databases
EnsemblFungii | EAL94098; EAL94098; AFUA_2G17990 |
GeneIDi | 3512711 |
KEGGi | afm:AFUA_2G17990 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AAHF01000001 Genomic DNA Translation: EAL94098.1 |
RefSeqi | XP_756136.1, XM_751043.1 |
3D structure databases
AlphaFoldDBi | Q4WZ67 |
SMRi | Q4WZ67 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 746128.CADAFUBP00003301 |
Protein family/group databases
MEROPSi | M77.002 |
Genome annotation databases
EnsemblFungii | EAL94098; EAL94098; AFUA_2G17990 |
GeneIDi | 3512711 |
KEGGi | afm:AFUA_2G17990 |
Organism-specific databases
VEuPathDBi | FungiDB:Afu2g17990 |
Phylogenomic databases
eggNOGi | ENOG502S2XP, Eukaryota |
HOGENOMi | CLU_037431_0_0_1 |
InParanoidi | Q4WZ67 |
OMAi | LFARNHI |
OrthoDBi | 1531660at2759 |
Enzyme and pathway databases
UniPathwayi | UPA00327 |
Family and domain databases
CDDi | cd13929, PT-DMATS_CymD, 1 hit |
InterProi | View protein in InterPro IPR033964, Aro_prenylTrfase IPR017795, Aro_prenylTrfase_DMATS IPR012148, DMATS-type_fun |
PANTHERi | PTHR40627, PTHR40627, 1 hit |
Pfami | View protein in Pfam PF11991, Trp_DMAT, 1 hit |
PIRSFi | PIRSF000509, Trp_DMAT, 1 hit |
SFLDi | SFLDS00036, Aromatic_Prenyltransferase, 1 hit |
TIGRFAMsi | TIGR03429, arom_pren_DMATS, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | EASL_ASPFU | |
Accessioni | Q4WZ67Primary (citable) accession number: Q4WZ67 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | March 6, 2013 |
Last sequence update: | July 5, 2005 | |
Last modified: | May 25, 2022 | |
This is version 82 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