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Protein

Alcohol dehydrogenase patD

Gene

patD

Organism
Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Alcohol dehydrogenase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:19383676, PubMed:24334092). The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units (PubMed:19383676). PatG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (PubMed:24334092). The cytochrome P450 monooxygenase patH then converts m-cresol to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI (PubMed:19383676). The conversion of gentisyl alcohol to two-ring compound neopatulin remains a matter of speculation, but it involves at least two intermediates, isoepoxydon and phyllostin (PubMed:19383676). PatN catalyzes the transformation of isoepoxydon into phyllostin (PubMed:19383676). The last part of the biosynthetic pathway involves the conversion of neopatulin to ascladiol followed by the transformation of the latter into patulin (PubMed:19383676).2 Publications

Catalytic activityi

An alcohol + NAD+ = an aldehyde or ketone + NADH.By similarity

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Pathwayi: patulin biosynthesis

This protein is involved in the pathway patulin biosynthesis, which is part of Mycotoxin biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway patulin biosynthesis and in Mycotoxin biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi46Zinc 1; catalyticBy similarity1
Binding sitei47NADBy similarity1
Metal bindingi67Zinc 1; catalyticBy similarity1
Binding sitei67SubstrateBy similarity1
Metal bindingi68Zinc 1By similarity1
Metal bindingi101Zinc 2By similarity1
Metal bindingi104Zinc 2By similarity1
Metal bindingi112Zinc 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi198 – 203NADBy similarity6
Nucleotide bindingi295 – 297NADBy similarity3
Nucleotide bindingi320 – 322NADBy similarity3

GO - Molecular functioni

Keywordsi

Molecular functionOxidoreductase
LigandMetal-binding, NAD, NADP, Zinc

Enzyme and pathway databases

UniPathwayiUPA00918.

Names & Taxonomyi

Protein namesi
Recommended name:
Alcohol dehydrogenase patD1 Publication (EC:1.1.1.11 Publication)
Alternative name(s):
Patulin synthesis protein D1 Publication
Gene namesi
Name:patD1 Publication
ORF Names:ACLA_093590
OrganismiAspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
Taxonomic identifieri344612 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000006701 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:ACLA_093590.

Pathology & Biotechi

Biotechnological usei

Patulin was originally used as an antibiotic and specifically trialed to be used against the common cold, but it is no longer used for that purpose since it has been shown to induce immunological, neurological and gastrointestinal effects (PubMed:15082620). Genotoxic effects of patulin with dose-dependent increase in DNA strand breaks in brain, liver and kidneys have been detected in mice (PubMed:22222931). However, more recently, it has been proposed that patulin might also have anti-tumor properties (PubMed:26619846).3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004371141 – 388Alcohol dehydrogenase patDAdd BLAST388

Structurei

3D structure databases

ProteinModelPortaliA1CFL1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000294685.
OMAiVIMSTAP.
OrthoDBiEOG092C2Q8E.

Family and domain databases

Gene3Di3.90.180.10. 1 hit.
InterProiView protein in InterPro
IPR013149. ADH_C.
IPR013154. ADH_N.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR020843. PKS_ER.
PfamiView protein in Pfam
PF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
SMARTiView protein in SMART
SM00829. PKS_ER. 1 hit.
SUPFAMiSSF50129. SSF50129. 1 hit.
SSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

A1CFL1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSTLPTTYK RAFFEKQDAT LTLEEVQLIE PQRGEILVKV EACGVCHSDH
60 70 80 90 100
FAQMNLMGGG FPRVPGHEVV GRVAAVGDGE TYWKIGDRTG AGWHGGHDGT
110 120 130 140 150
CGACKKGLFQ MCDNEQVNGI TRDGGYAEYV LIRSEAAVRI PDHVNAAKYA
160 170 180 190 200
PMLCAGVTVF NSIRQMNIPV GETVVIQGLG GLGHLALQYA NRFGYRVVAL
210 220 230 240 250
SRGAQKEEFA RKLGAHVYID TSKEDPVAAL QKLGGAALIV STAPSPELIN
260 270 280 290 300
PLIEGLGVLG KLLILSIVGG IEVHTGLLVS ERRIAIHRTN SIVRSLLTNS
310 320 330 340 350
KVGKGKSIWS WPSGHATDSE EAIAFAELQG IDCLVEEFPL EKCNEAFGRS
360 370 380
SSTTADRERV FLADFTGLTT TAAMMDGSVR FRAVITME
Length:388
Mass (Da):41,701
Last modified:January 23, 2007 - v1
Checksum:iB198DF097329C0F5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS027052 Genomic DNA. Translation: EAW11660.1.
RefSeqiXP_001273086.1. XM_001273085.1.

Genome annotation databases

EnsemblFungiiCADACLAT00008596; CADACLAP00008386; CADACLAG00008596.
GeneIDi4704848.
KEGGiact:ACLA_093590.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS027052 Genomic DNA. Translation: EAW11660.1.
RefSeqiXP_001273086.1. XM_001273085.1.

3D structure databases

ProteinModelPortaliA1CFL1.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADACLAT00008596; CADACLAP00008386; CADACLAG00008596.
GeneIDi4704848.
KEGGiact:ACLA_093590.

Organism-specific databases

EuPathDBiFungiDB:ACLA_093590.

Phylogenomic databases

HOGENOMiHOG000294685.
OMAiVIMSTAP.
OrthoDBiEOG092C2Q8E.

Enzyme and pathway databases

UniPathwayiUPA00918.

Family and domain databases

Gene3Di3.90.180.10. 1 hit.
InterProiView protein in InterPro
IPR013149. ADH_C.
IPR013154. ADH_N.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR020843. PKS_ER.
PfamiView protein in Pfam
PF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
SMARTiView protein in SMART
SM00829. PKS_ER. 1 hit.
SUPFAMiSSF50129. SSF50129. 1 hit.
SSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPATD_ASPCL
AccessioniPrimary (citable) accession number: A1CFL1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 7, 2016
Last sequence update: January 23, 2007
Last modified: April 12, 2017
This is version 57 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.