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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: -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

A primary alcohol + NAD+ = an aldehyde + NADH.By similarity
A secondary alcohol + NAD+ = a 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

UniPathwayi
UPA00918

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

Interactioni

Protein-protein interaction databases

STRINGi5057.CADACLAP00008386

Structurei

3D structure databases

ProteinModelPortaliA1CFL1
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000294685
OMAiYAPILCA
OrthoDBiEOG092C2Q8E

Family and domain databases

InterProiView protein in InterPro
IPR013149 ADH_C
IPR013154 ADH_N
IPR011032 GroES-like_sf
IPR036291 NAD(P)-bd_dom_sf
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

EnsemblFungiiEAW11660; EAW11660; ACLA_093590
GeneIDi4704848
KEGGiact:ACLA_093590

Similar proteinsi

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...

Protein-protein interaction databases

STRINGi5057.CADACLAP00008386

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEAW11660; EAW11660; ACLA_093590
GeneIDi4704848
KEGGiact:ACLA_093590

Organism-specific databases

EuPathDBiFungiDB:ACLA_093590

Phylogenomic databases

HOGENOMiHOG000294685
OMAiYAPILCA
OrthoDBiEOG092C2Q8E

Enzyme and pathway databases

UniPathwayi
UPA00918

Family and domain databases

InterProiView protein in InterPro
IPR013149 ADH_C
IPR013154 ADH_N
IPR011032 GroES-like_sf
IPR036291 NAD(P)-bd_dom_sf
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: June 20, 2018
This is version 65 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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