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Entry version 109 (02 Jun 2021)
Sequence version 2 (04 Dec 2007)
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Protein

5'-deoxyadenosine deaminase

Gene

dadD

Organism
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia)
Status
Reviewed-Annotation score:

Annotation score:4 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>
-Protein inferred from homologyi <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 deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-methylthioadenosine, to produce the inosine analogs. Can also deaminate adenosine. The preferred substrate for this enzyme is 5'-deoxyadenosine, but all these substrates are efficiently deaminated. Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions. May also be involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens.

UniRule annotation

Miscellaneous

SAH is a product of SAM methyltransferases and is known to be a feedback inhibitor of these enzymes. As a result of this inhibition, organisms have evolved efficient enzymes to metabolize SAH via different pathways. The pathway found in methanogens differs from the canonical pathway, it uses the deamination of S-adenosyl-L-homocysteine to form S-inosyl-L-homocysteine for the regeneration of SAM from S-adenosyl-L-homocysteine. 5'-deoxyadenosine is a radical SAM enzyme reaction product which strongly inhibits radical SAM enzymes. A pathway for removing this product must be present in methanogens where the MTA/SAH nucleosidase which normally metabolizes this compound is absent.UniRule annotation

<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

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.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: S-adenosyl-L-methionine biosynthesis

This protein is involved in the pathway S-adenosyl-L-methionine biosynthesis, which is part of Amino-acid biosynthesis.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway S-adenosyl-L-methionine biosynthesis 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 bindingi63Zinc; via tele nitrogenUniRule annotation1
Metal bindingi65Zinc; via tele nitrogenUniRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei92SubstrateUniRule annotation1
Binding sitei184SubstrateUniRule annotation1
Metal bindingi211Zinc; via tele nitrogenUniRule annotation1
Binding sitei214SubstrateUniRule annotation1
Metal bindingi299ZincUniRule annotation1
Binding sitei299SubstrateUniRule 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

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 functionHydrolase
LigandMetal-binding, Zinc

Enzyme and pathway databases

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

More...
UniPathwayi
UPA00315

<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:
5'-deoxyadenosine deaminaseUniRule annotation (EC:3.5.4.41UniRule annotation)
Short name:
5'-dA deaminaseUniRule annotation
Alternative name(s):
5'-methylthioadenosine deaminaseUniRule annotation (EC:3.5.4.31UniRule annotation)
Short name:
MTA deaminaseUniRule annotation
Adenosine deaminaseUniRule annotation (EC:3.5.4.4UniRule annotation)
S-adenosylhomocysteine deaminaseUniRule annotation (EC:3.5.4.28UniRule annotation)
Short name:
SAH deaminaseUniRule 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:dadDUniRule annotation
Ordered Locus Names:MM_2279
<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>OrganismiMethanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia)
<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 identifieri192952 [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 lineageiArchaeaEuryarchaeotaStenosarchaea groupMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina
<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
  • UP000000595 <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

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003124811 – 4325'-deoxyadenosine deaminaseAdd BLAST432

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer.

UniRule annotation

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
192952.MM_2279

<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

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SMRi
Q8PUQ3

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 metallo-dependent hydrolases superfamily. MTA/SAH deaminase family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
arCOG00695, Archaea

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_012358_2_1_2

Identification of Orthologs from Complete Genome Data

More...
OMAi
ASYFATN

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.30.40.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01281, MTA_SAH_deamin, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006680, Amidohydro-rel
IPR023512, Deaminase_MtaD/DadD
IPR011059, Metal-dep_hydrolase_composite
IPR032466, Metal_Hydrolase

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01979, Amidohydro_1, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51338, SSF51338, 1 hit
SSF51556, SSF51556, 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.

Q8PUQ3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MADIIIKNAY VLTMDPDAGD IKKGTVVIED GKITEIGVKT KESADTVIDA
60 70 80 90 100
KGSVVMPGLV NTHTHAAMTL FRGYADDLQL AEWLEKHIWP AEAQLTAEDV
110 120 130 140 150
YRGSLLACLE MIRSGTTSFA DMYFFMDETA KAVEASGLRA SLSHGLIELW
160 170 180 190 200
NEEKGENDLK EGKRFVRAWQ GAAKGRIKTM YGPHAPNTCS DEFLAKVKEA
210 220 230 240 250
ARQDGAGLHI HVLETEAELL AMKERYGKCS VHMLDDIGFF GPDVLAAHCV
260 270 280 290 300
WLSDGDIEVL REKGVNVSHN PISNMKLASG TAPVYKMLER GVNVSLGTDG
310 320 330 340 350
CASNNNLDLF EEMKTAALLH KLSTCNPTAL PARQVLQMAT VNGAKALGTE
360 370 380 390 400
TGMLKTGMKA DMIIVDMKKP HLTPCFDVPS HLVYSAGGSD VRTTIVDGKI
410 420 430
LMQDYRVMVL DEQKVIEEAQ KAAEELVARV NS
Length:432
Mass (Da):47,085
Last modified:December 4, 2007 - v2
<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:i4B7AFB14E93CD9FD
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAM31975 differs from that shown. Reason: Erroneous initiation.Curated

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
AE008384 Genomic DNA Translation: AAM31975.1 Different initiation.

NCBI Reference Sequences

More...
RefSeqi
WP_048037226.1, NC_003901.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAM31975; AAM31975; MM_2279

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
24879011

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mma:MM_2279

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|192952.21.peg.2612

<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
AE008384 Genomic DNA Translation: AAM31975.1 Different initiation.
RefSeqiWP_048037226.1, NC_003901.1

3D structure databases

SMRiQ8PUQ3
ModBaseiSearch...

Protein-protein interaction databases

STRINGi192952.MM_2279

Genome annotation databases

EnsemblBacteriaiAAM31975; AAM31975; MM_2279
GeneIDi24879011
KEGGimma:MM_2279
PATRICifig|192952.21.peg.2612

Phylogenomic databases

eggNOGiarCOG00695, Archaea
HOGENOMiCLU_012358_2_1_2
OMAiASYFATN

Enzyme and pathway databases

UniPathwayiUPA00315

Family and domain databases

Gene3Di2.30.40.10, 1 hit
HAMAPiMF_01281, MTA_SAH_deamin, 1 hit
InterProiView protein in InterPro
IPR006680, Amidohydro-rel
IPR023512, Deaminase_MtaD/DadD
IPR011059, Metal-dep_hydrolase_composite
IPR032466, Metal_Hydrolase
PfamiView protein in Pfam
PF01979, Amidohydro_1, 1 hit
SUPFAMiSSF51338, SSF51338, 1 hit
SSF51556, SSF51556, 1 hit

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 nameiDADD_METMA
<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: Q8PUQ3
<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: December 4, 2007
Last sequence update: December 4, 2007
Last modified: June 2, 2021
This is version 109 of the entry and version 2 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 programProkaryotic 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
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