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). 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 key	Position(s)	DescriptionActions	Graphical view	Length
Active siteⁱ	167	Proton acceptorPROSITE-ProRule annotation		1

Regions

Feature key	Position(s)	DescriptionActions	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

View the complete GO annotation on QuickGO ...

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	cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Aspergillaceae › Aspergillus › Emericella nidulans
Proteomesⁱ	UP000000560 Componentⁱ: Chromosome VI UP000005890 Componentⁱ: Unassembled WGS sequence

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000437617	1 – 271	Short chain dehydrogenase asqEAdd BLAST		271

Interactionⁱ

Protein-protein interaction databases

STRINGⁱ	162425.CADANIAP00009358

STRINGⁱ

162425.CADANIAP00009358

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q5AR48
SMRⁱ	Q5AR48
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the short-chain dehydrogenases/reductases (SDR) family.Curated

Phylogenomic databases

OMAⁱ	MTYGASK
Database of Orthologous Groups More...OrthoDBⁱ	EOG092C3UOD

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

Sequenceⁱ

Sequence statusⁱ: Complete.

Q5AR48-1 [UniParc]FASTA Add 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
NCBI Reference Sequences More...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

50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q5AR48	3-oxoacyl-[acyl-carrier-protein] reductase		COLHI		275	UniRef50_Q5AR48
Short chain oxidoreductase		Colletotrichum tofieldiae		275
3-oxoacyl-(Acyl-carrier-protein) reductase		Colletotrichum incanum		275
Uncharacterized protein		NECH7		276
Putative 3-oxoacyl-(Acyl-carrier-protein) reductase		COLSU		274
+28

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

ProteinModelPortalⁱ	Q5AR48
SMRⁱ	Q5AR48
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

STRINGⁱ	162425.CADANIAP00009358

STRINGⁱ

162425.CADANIAP00009358

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblFungiⁱ	CBF82269; CBF82269; ANIA_09232 EAA61523; EAA61523; AN9232.2
GeneIDⁱ	2868050
KEGGⁱ	ani:AN9232.2

Phylogenomic databases

OMAⁱ	MTYGASK
OrthoDBⁱ	EOG092C3UOD

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
ProtoNetⁱ	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:	June 20, 2018
	This is version 92 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

Complete proteome, Reference proteome

UniProtKB - Q5AR48 (ASQE_EMENI)

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Short chain dehydrogenase asqE

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Functionⁱ

Catalytic activityⁱ

Pathwayⁱ: Secondary metabolite biosynthesis

Sites

Regions

GO - Molecular functionⁱ

Keywordsⁱ

Names & Taxonomyⁱ

PTM / Processingⁱ

Molecule processing

Interactionⁱ

Protein-protein interaction databases

Structureⁱ

3D structure databases

Family & Domainsⁱ

Sequence similaritiesⁱ

Phylogenomic databases

Family and domain databases

Sequenceⁱ

Sequence databases

Genome annotation databases

Similar proteinsⁱ

Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ

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Supporting data

UniProtKB - Q5AR48 (ASQE_EMENI)

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Short chain dehydrogenase asqE

asqE

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: Secondary metabolite biosynthesis

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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Functionⁱ

Pathwayⁱ: Secondary metabolite biosynthesis

GO - Molecular functionⁱ

Names & Taxonomyⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ