Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 155 (26 Feb 2020)
Sequence version 1 (01 Nov 1997)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase

Gene

ADI1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

Catalyzes the formation of formate and 2-keto-4-methylthiobutyrate (KMTB) from 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).UniRule annotation2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Fe cationUniRule annotationNote: Binds 1 Fe cation per monomer. Can also use other divalent metal cations.UniRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-methionine biosynthesis via salvage pathway

This protein is involved in step 5 of the subpathway that synthesizes L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate.UniRule annotation
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. Methylthioribose-1-phosphate isomerase (MRI1)
  2. Methylthioribulose-1-phosphate dehydratase (MDE1)
  3. Enolase-phosphatase E1 (UTR4)
  4. Enolase-phosphatase E1 (UTR4)
  5. 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase (ADI1)
  6. Aromatic amino acid aminotransferase 2 (ARO9), Branched-chain-amino-acid aminotransferase, cytosolic (BAT2), Branched-chain-amino-acid aminotransferase, mitochondrial (BAT1), Aromatic/aminoadipate aminotransferase 1 (ARO8)
This subpathway is part of the pathway L-methionine biosynthesis via salvage pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate, the pathway L-methionine biosynthesis via salvage pathway and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi85Iron or nickelUniRule annotation1
Metal bindingi87Iron or nickelUniRule annotation1
Metal bindingi91Iron or nickelUniRule annotation1
Metal bindingi132Iron or nickelUniRule annotation1

<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

  • acireductone dioxygenase (Ni2+-requiring) activity Source: SGD
  • acireductone dioxygenase [iron(II)-requiring] activity Source: GO_Central
  • iron ion binding Source: UniProtKB-UniRule

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDioxygenase, Oxidoreductase
Biological processAmino-acid biosynthesis, Methionine biosynthesis
LigandIron, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:MONOMER3O-186

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-1237112 Methionine salvage pathway

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00904;UER00878

<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 subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenaseUniRule annotation (EC:1.13.11.54UniRule annotation)
Alternative name(s):
Acireductone dioxygenase (Fe(2+)-requiring)UniRule annotation
Short name:
ARDUniRule annotation
Short name:
Fe-ARDUniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ADI1UniRule annotation
Ordered Locus Names:YMR009W
ORF Names:YM8270.12
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome XIII

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YMR009W

Saccharomyces Genome Database

More...
SGDi
S000004611 ADI1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi24E → A: No loss of acireductone dioxygenase activity. 1 Publication1
Mutagenesisi45E → A: No loss of acireductone dioxygenase activity. 1 Publication1
Mutagenesisi91E → A: Loss of acireductone dioxygenase activity. 1 Publication1
Mutagenesisi151E → A: No loss of acireductone dioxygenase activity. 1 Publication1

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001629461 – 1791,2-dihydroxy-3-keto-5-methylthiopentene dioxygenaseAdd BLAST179

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q03677

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q03677

PRoteomics IDEntifications database

More...
PRIDEi
Q03677

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By heat shock.1 Publication

<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

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
35178, 96 interactors

Database of interacting proteins

More...
DIPi
DIP-877N

Protein interaction database and analysis system

More...
IntActi
Q03677, 1 interactor

STRING: functional protein association networks

More...
STRINGi
4932.YMR009W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q03677 protein

<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

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q03677

Database of comparative protein structure models

More...
ModBasei
Search...

<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

Belongs to the acireductone dioxygenase (ARD) family.UniRule annotation

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_090154_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q03677

KEGG Orthology (KO)

More...
KOi
K08967

Identification of Orthologs from Complete Genome Data

More...
OMAi
KERNYSW

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.120.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_03154 Salvage_MtnD_euk, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR004313 ARD
IPR027496 ARD_euk
IPR014710 RmlC-like_jellyroll
IPR011051 RmlC_Cupin_sf

The PANTHER Classification System

More...
PANTHERi
PTHR23418 PTHR23418, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03079 ARD, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51182 SSF51182, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q03677-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVKVYIHDNK VDSDYRAPHN SGTELSLDEL AKLGVIYKYC ANEEEVNEIA
60 70 80 90 100
RQREYKNRDV VNICEGSFKS EAEFNEKLAT FYQEHLHEDE EIRYCLEGAG
110 120 130 140 150
YFDVRDASTP ENWIRCLVES GDLLILPPGI YHRFTLTTSN HIKALRLFKD
160 170
EPKWQAINRS NQADSLPVRK DYIALINQY
Length:179
Mass (Da):20,879
Last modified:November 1, 1997 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iE6629DC2E17E2109
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
Z48613 Genomic DNA Translation: CAA88525.1
AY558584 Genomic DNA Translation: AAS56910.1
BK006946 Genomic DNA Translation: DAA09907.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S53039

NCBI Reference Sequences

More...
RefSeqi
NP_013722.1, NM_001182505.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YMR009W_mRNA; YMR009W; YMR009W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
855021

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YMR009W

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<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

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48613 Genomic DNA Translation: CAA88525.1
AY558584 Genomic DNA Translation: AAS56910.1
BK006946 Genomic DNA Translation: DAA09907.1
PIRiS53039
RefSeqiNP_013722.1, NM_001182505.1

3D structure databases

SMRiQ03677
ModBaseiSearch...

Protein-protein interaction databases

BioGridi35178, 96 interactors
DIPiDIP-877N
IntActiQ03677, 1 interactor
STRINGi4932.YMR009W

Proteomic databases

MaxQBiQ03677
PaxDbiQ03677
PRIDEiQ03677

Genome annotation databases

EnsemblFungiiYMR009W_mRNA; YMR009W; YMR009W
GeneIDi855021
KEGGisce:YMR009W

Organism-specific databases

EuPathDBiFungiDB:YMR009W
SGDiS000004611 ADI1

Phylogenomic databases

HOGENOMiCLU_090154_1_0_1
InParanoidiQ03677
KOiK08967
OMAiKERNYSW

Enzyme and pathway databases

UniPathwayiUPA00904;UER00878
BioCyciYEAST:MONOMER3O-186
ReactomeiR-SCE-1237112 Methionine salvage pathway

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q03677
RNActiQ03677 protein

Family and domain databases

Gene3Di2.60.120.10, 1 hit
HAMAPiMF_03154 Salvage_MtnD_euk, 1 hit
InterProiView protein in InterPro
IPR004313 ARD
IPR027496 ARD_euk
IPR014710 RmlC-like_jellyroll
IPR011051 RmlC_Cupin_sf
PANTHERiPTHR23418 PTHR23418, 1 hit
PfamiView protein in Pfam
PF03079 ARD, 1 hit
SUPFAMiSSF51182 SSF51182, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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 subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMTND_YEAST
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q03677
Secondary accession number(s): D6VZI3
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: February 26, 2020
This is version 155 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<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

Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again