UniProtKB - Q5AR48 (ASQE_EMENI)
Short chain dehydrogenase asqE
asqE
Functioni
Short chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of the aspoquinolone mycotoxins (PubMed:25251934).
The first stage is catalyzed by the nonribosomal pepdide synthetase asqK that condenses anthranilic acid and O-methyl-L-tyrosine to produce 4'-methoxycyclopeptin (PubMed:25251934).
AsqK is also able to use anthranilic acid and L-phenylalanine as substrates to produce cyclopeptin, but at a tenfold lower rate (PubMed:25251934).
4'-methoxycyclopeptin is then converted to 4'-methoxydehydrocyclopeptin by the ketoglutarate-dependent dioxygenase asqJ through dehydrogenation to form a double bond between C-alpha and C-beta of the O-methyltyrosine side chain (PubMed:25251934, PubMed:26553478).
AsqJ also converts its first product 4'-methoxydehydrocyclopeptin to 4'-methoxycyclopenin (PubMed:25251934).
AsqJ is a very unique dioxygenase which is capable of catalyzing radical-mediated dehydrogenation and epoxidation reactions sequentially on a 6,7-benzo-diazepinedione substrate in the 4'-methoxyviridicatin biosynthetic pathway (PubMed:25251934).
AsqJ is also capable of converting cyclopeptin into dehydrocyclopeptin (PubMed:25251934).
The following conversion of 4'-methoxycyclopenin into 4'-methoxyviridicatin is catalyzed by the cyclopenase asqI (PubMed:30026518).
Cyclopenin can also be converted into viridicatin by asqI (PubMed:30026518).
4'-methoxyviridicatin is the precursor of quinolone natural products, and is further converted to quinolinone B (Probable). The prenyltransferase asqH1 then catalyzes the canonical Friedel-Crafts alkylation of quinolinone B with dimethylallyl cation to yield dimethylallyl quinolone, which is subjected to FAD-dependent dehydrogenation by the FAD-linked oxidoreductase asqF to yield conjugated aryl diene (By similarity).
The delta(3') double bond then serves as the site of the second alkylation with DMAPP catalyzed by the prenyltransferase asqH2 to yield a carbenium ion intermediate, which can be attacked by H2O to yield a styrenyl quinolone containing a C3'-hydroxyprenyl chain (By similarity).
The FAD-dependent monooxygenase asqG performs epoxidation of the terminal C7'-C8' olefin (PubMed:30026518).
Finally, after dehydratation of the epoxide at C3 by asqC, the quinolone epoxide rearrangement protein asqO catalyzes an enzymatic 3-exo-tet cyclization to yield the cyclopropyl-THF ring system in aspoquinolone (PubMed:30026518).
By similarity1 Publication3 PublicationsCatalytic activityi
: Secondary metabolite biosynthesis Pathwayi
This protein is involved in Secondary metabolite biosynthesis.1 PublicationView all proteins of this organism that are known to be involved in Secondary metabolite biosynthesis.
Pathwayi: Alkaloid biosynthesis
This protein is involved in Alkaloid biosynthesis.1 PublicationView all proteins of this organism that are known to be involved in Alkaloid biosynthesis.
Pathwayi: Mycotoxin biosynthesis
This protein is involved in Mycotoxin biosynthesis.1 PublicationView all proteins of this organism that are known to be involved in Mycotoxin biosynthesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 167 | Proton acceptorPROSITE-ProRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 14 – 22 | NADBy similarity | 9 | |
Nucleotide bindingi | 41 – 42 | NADBy similarity | 2 | |
Nucleotide bindingi | 72 – 74 | NADBy similarity | 3 |
GO - Molecular functioni
- alcohol dehydrogenase (NAD+) activity Source: UniProtKB-EC
Keywordsi
Molecular function | Oxidoreductase |
Ligand | NAD |
Names & Taxonomyi
Protein namesi | Recommended name: Short chain dehydrogenase asqE1 Publication (EC:1.1.1.1PROSITE-ProRule annotation)Alternative name(s): 4'-methoxyviridicatin/aspoquinolone biosynthesis cluster protein asqECurated Aspoquinolone biosynthesis protein E1 Publication |
Gene namesi | Name:asqE1 Publication ORF Names:AN9232 |
Organismi | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
Taxonomic identifieri | 227321 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Aspergillaceae › Aspergillus › Aspergillus subgen. Nidulantes › |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000437617 | 1 – 271 | Short chain dehydrogenase asqEAdd BLAST | 271 |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG0725, Eukaryota |
HOGENOMi | CLU_010194_1_3_1 |
InParanoidi | Q5AR48 |
OMAi | VMQANAF |
OrthoDBi | 913128at2759 |
Family and domain databases
InterProi | View protein in InterPro IPR036291, NAD(P)-bd_dom_sf IPR020904, Sc_DH/Rdtase_CS IPR002347, SDR_fam |
PRINTSi | PR00081, GDHRDH PR00080, SDRFAMILY |
SUPFAMi | SSF51735, SSF51735, 1 hit |
PROSITEi | View protein in PROSITE PS00061, ADH_SHORT, 1 hit |
i Sequence
Sequence statusi: Complete.
10 20 30 40 50
MTQAPWSLAR KTAIVTGGSR GIGRAIAIHL TCKGLSKLAI TYISNLAAAE
60 70 80 90 100
STLDECRKNG LGMGIAIKAD LLDPNIGHGL VQQALAGLET PTIDILVNNA
110 120 130 140 150
AYLDPSEAAS VEELTLPVFQ KVMQANAFAP ISIISATMPH LPVSGGRVIN
160 170 180 190 200
ISSAAAKLAN PGPVMTYGAS KAALDSFTRS LAAEFATDKA ATFNTVCVGP
210 220 230 240 250
TVTDGFHVVG KLYPEGFMEE LAKAFTAAQR VGMPQDIAFI VGFLAGEEAR
260 270
WVNGACMSAN GGFREVLPAL S
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BN001306 Genomic DNA Translation: CBF82269.1 AACD01000170 Genomic DNA Translation: EAA61523.1 |
RefSeqi | XP_682501.1, XM_677409.1 |
Genome annotation databases
EnsemblFungii | CBF82269; CBF82269; ANIA_09232 EAA61523; EAA61523; AN9232.2 |
GeneIDi | 2868050 |
KEGGi | ani:AN9232.2 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BN001306 Genomic DNA Translation: CBF82269.1 AACD01000170 Genomic DNA Translation: EAA61523.1 |
RefSeqi | XP_682501.1, XM_677409.1 |
3D structure databases
AlphaFoldDBi | Q5AR48 |
SMRi | Q5AR48 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 162425.CADANIAP00009358 |
Genome annotation databases
EnsemblFungii | CBF82269; CBF82269; ANIA_09232 EAA61523; EAA61523; AN9232.2 |
GeneIDi | 2868050 |
KEGGi | ani:AN9232.2 |
Phylogenomic databases
eggNOGi | KOG0725, Eukaryota |
HOGENOMi | CLU_010194_1_3_1 |
InParanoidi | Q5AR48 |
OMAi | VMQANAF |
OrthoDBi | 913128at2759 |
Family and domain databases
InterProi | View protein in InterPro IPR036291, NAD(P)-bd_dom_sf IPR020904, Sc_DH/Rdtase_CS IPR002347, SDR_fam |
PRINTSi | PR00081, GDHRDH PR00080, SDRFAMILY |
SUPFAMi | SSF51735, SSF51735, 1 hit |
PROSITEi | View protein in PROSITE PS00061, ADH_SHORT, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | ASQE_EMENI | |
Accessioni | Q5AR48Primary (citable) accession number: Q5AR48 Secondary accession number(s): C8VJP7 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 2, 2016 |
Last sequence update: | April 26, 2005 | |
Last modified: | May 25, 2022 | |
This is version 105 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