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Protein

Short chain dehydrogenase asqE

Gene

asqE

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

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). 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). The following conversion of 4'-methoxycyclopenin into 4'-methoxyviridicatin proceeds non-enzymatically (PubMed:25251934). AsqJ is also capable of converting cyclopeptin into dehydrocyclopeptin and cyclopenin in a sequential fashion (PubMed:25251934). Cyclopenin can be converted into viridicatin non-enzymatically (PubMed:25251934). 4'-methoxyviridicatin likely acts as a precursor of quinolone natural products, such as aspoquinolones, peniprequinolones, penigequinolones, and yaequinolones (PubMed:25251934). Further characterization of the remaining genes in the cluster has still to be done to determine the exact identity of quinolone products this cluster is responsible for biosynthesizing (PubMed:25251934).1 Publication

Catalytic activityi

A primary alcohol + NAD+ = an aldehyde + NADH.PROSITE-ProRule annotation
A secondary alcohol + NAD+ = a ketone + NADH.PROSITE-ProRule annotation

Pathwayi: Secondary metabolite biosynthesis

This protein is involved in Secondary metabolite biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in Secondary metabolite biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei167Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi14 – 22NADBy similarity9
Nucleotide bindingi41 – 42NADBy similarity2
Nucleotide bindingi72 – 74NADBy similarity3

GO - Molecular functioni

Keywordsi

Molecular functionOxidoreductase
LigandNAD

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
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000000560 Componenti: Chromosome VI
  • UP000005890 Componenti: Unassembled WGS sequence

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004376171 – 271Short chain dehydrogenase asqEAdd BLAST271

Interactioni

Protein-protein interaction databases

STRINGi162425.CADANIAP00009358

Structurei

3D structure databases

ProteinModelPortaliQ5AR48
SMRiQ5AR48
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

OMAiMTYGASK
OrthoDBiEOG092C3UOD

Family and domain databases

InterProiView protein in InterPro
IPR036291 NAD(P)-bd_dom_sf
IPR020904 Sc_DH/Rdtase_CS
IPR002347 SDR_fam
PRINTSiPR00081 GDHRDH
PR00080 SDRFAMILY
SUPFAMiSSF51735 SSF51735, 1 hit
PROSITEiView protein in PROSITE
PS00061 ADH_SHORT, 1 hit

Sequencei

Sequence statusi: Complete.

Q5AR48-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:271
Mass (Da):28,147
Last modified:April 26, 2005 - v1
Checksum:iC5E46EE7F47BB471
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BN001306 Genomic DNA Translation: CBF82269.1
AACD01000170 Genomic DNA Translation: EAA61523.1
RefSeqiXP_682501.1, XM_677409.1

Genome annotation databases

EnsemblFungiiCBF82269; CBF82269; ANIA_09232
EAA61523; EAA61523; AN9232.2
GeneIDi2868050
KEGGiani:AN9232.2

Similar proteinsi

Entry informationi

Entry nameiASQE_EMENI
AccessioniPrimary (citable) accession number: Q5AR48
Secondary accession number(s): C8VJP7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 2, 2016
Last sequence update: April 26, 2005
Last modified: June 20, 2018
This is version 92 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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