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Entry version 40 (02 Jun 2021)
Sequence version 1 (11 Jul 2006)
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Protein

Adenosine deaminase RL5

Gene

rl5

Organism
Unknown prokaryotic organism
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

Purine nucleoside enzyme that catalyzes the phosphorolysis of adenosine and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine and hypoxanthine (By similarity).

Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate (By similarity).

Also has adenosine deaminase activity (By similarity).

Also acts as a multicopper oxidase able to oxidize a wide variety of polyphenols and related compounds in vitro (PubMed:16740638).

Displays substrate preference as follows: syringaldazine > 2,6-dimethoxyphenol > veratryl alcohol > guaiacol > tetramethylbenzidine > 4-methoxybenzyl alcohol > 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) >> phenol red > 1-hydroxybenzotriazole (PubMed:16740638).

Cannot use 3,4-dimetoxybenzyl alcohol and violuric acid as substrates (PubMed:16740638).

As this enzyme is derived from a rumen microbial community, it may have a role in the digestion of complex plant materials such as ryegrass lignin (PubMed:16740638).

By similarity1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

Cu cation1 PublicationNote: Binds 4 Cu cations per subunit.1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 18 sec(-1) with 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid as substrate. kcat is 660 sec(-1) with syringaldazine as substrate. kcat is 1175 sec(-1) with 2,6-dimethoxyphenol as substrate (at pH 4.5 and 40 degrees Celsius).1 Publication
  1. KM=26 µM for 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid (at pH 4.5 and 40 degrees Celsius)1 Publication
  2. KM=0.43 µM for syringaldazine (at pH 4.5 and 40 degrees Celsius)1 Publication
  3. KM=0.45 µM for 2,6-dimethoxyphenol (at pH 4.5 and 40 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 4.0-5.0. Activity is very high over a broad pH range from 4.0 to 9.0. Exhibits more than 70% activity at pH 3.5 and 9.5.1 Publication

Temperature dependencei

Optimum temperature is about 60 degrees Celsius. Is fully stable at this temperature.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi36Copper 31 Publication1
Metal bindingi40Copper 31 Publication1
Metal bindingi68Copper 31 Publication1
Metal bindingi73Copper 1; catalytic1 Publication1
Metal bindingi75Copper 11 Publication1
Metal bindingi114Copper 31 Publication1
Metal bindingi118Copper 1; catalytic1 Publication1
Metal bindingi135Copper 1; catalytic1 Publication1
Metal bindingi172Copper 21 Publication1
Metal bindingi175Copper 21 Publication1
Metal bindingi234Copper 21 Publication1
Metal bindingi237Copper 21 Publication1

<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>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, Oxidoreductase, Transferase
LigandCopper, Metal-binding, Zinc

Enzyme and pathway databases

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q1EIR0

<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_and_taxonomy_section">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:
Adenosine deaminase RL5 (EC:3.5.4.4By similarity)
Alternative name(s):
Laccase RL51 Publication
Multicopper oxidase RL51 Publication
Polyphenol oxidase1 Publication (EC:1.10.3.-1 Publication)
Purine nucleoside phosphorylase RL5 (EC:2.4.2.1By similarity)
S-methyl-5'-thioadenosine phosphorylase RL5 (EC:2.4.2.28By similarity)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:rl51 PublicationImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiUnknown prokaryotic organism
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri2725 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiBacteriaenvironmental samples

<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_and_biotech_section">'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>Mutagenesisi36N → A: Loss of 1.0 of Cu/mol of protein. Loss of catalytic activity. 1 Publication1
Mutagenesisi40Y → A: Loss of 1.0 of Cu/mol of protein. Loss of catalytic activity. 1 Publication1
Mutagenesisi68M → A: No effect on Cu content. No effect on catalytic activity. 1 Publication1
Mutagenesisi73H → A: Loss of 1.0 of Cu/mol of protein. No effect on secondary structure. Loss of catalytic activity. 1 Publication1
Mutagenesisi75C → Q: Loss of 1.0 of Cu/mol of protein. No effect on secondary structure. Loss of catalytic activity. 1 Publication1
Mutagenesisi114N → A: Loss of 1.0 of Cu/mol of protein. Loss of catalytic activity. 1 Publication1
Mutagenesisi118C → Q: Loss of 1.0 of Cu/mol of protein. No effect on secondary structure. Loss of catalytic activity. 1 Publication1
Mutagenesisi135H → A: Loss of 1.0 of Cu/mol of protein. No effect on secondary structure. Loss of catalytic activity. 1 Publication1
Mutagenesisi172C → Q: Loss of 1.0 of Cu/mol of protein. Loss of catalytic activity. 1 Publication1
Mutagenesisi175C → Q: Loss of 1.0 of Cu/mol of protein. Loss of catalytic activity. 1 Publication1
Mutagenesisi190H → A: Binds only 1.0 of Cu/mol of protein. Causes major change in secondary structure. Displays about 10% of wild-type catalytic activity. 1 Publication1
Mutagenesisi207H → A: Binds only 1.0 of Cu/mol of protein. Causes major change in secondary structure. Displays about 10% of wild-type catalytic activity. 1 Publication1
Mutagenesisi233H → A: Loss of 1.0 of Cu/mol of protein. No effect on secondary structure. Loss of catalytic activity. 1 Publication1
Mutagenesisi234C → Q: No effect on Cu content. No effect on catalytic activity. 1 Publication1
Mutagenesisi237C → Q: Loss of 1.0 of Cu/mol of protein. Loss of catalytic activity. 1 Publication1
Mutagenesisi239H → A: Binds only 1.0 of Cu/mol of protein. Causes major change in secondary structure. Loss of catalytic 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004407801 – 262Adenosine deaminase RL5Add BLAST262

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q1EIR0

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

1 Publication

GO - Molecular functioni

<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
Q1EIR0

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

Family and domain databases

Conserved Domains Database

More...
CDDi
cd16833, YfiH, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.60.140.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003730, Cu_polyphenol_OxRdtase
IPR038371, Cu_polyphenol_OxRdtase_sf
IPR011324, Cytotoxic_necrot_fac-like_cat

The PANTHER Classification System

More...
PANTHERi
PTHR30616, PTHR30616, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02578, Cu-oxidase_4, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF64438, SSF64438, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00726, TIGR00726, 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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

Q1EIR0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MIELEKLDFA KSVEGVEAFS TTRGQVDGRN AYSGVNLCDY VGDDALRVLD
60 70 80 90 100
ARLTLAMQLG VDLDDLVMPR QTHSCRVAVI DERFRALDID EQEAALEGVD
110 120 130 140 150
ALVTRLQGIV IGVNTADCVP IVLVDSQAGI VAVSHAGWRG TVGRIAKAVV
160 170 180 190 200
EEMCRQGATV DRIQAAMGPS ICQDCFEVGD EVVEAFKKAH FNLNDIVVRN
210 220 230 240 250
PATGKAHIDL RAANRAVLVA AGVPAANIVE SQHCSRCEHT SFFSARRLGI
260
NSGRTFTGIY RK
Length:262
Mass (Da):28,282
Last modified:July 11, 2006 - 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:i326C915E8A48610F
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
AM269758 Genomic DNA Translation: CAK32504.1

<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
AM269758 Genomic DNA Translation: CAK32504.1

3D structure databases

SMRiQ1EIR0
ModBaseiSearch...

Proteomic databases

PRIDEiQ1EIR0

Enzyme and pathway databases

SABIO-RKiQ1EIR0

Family and domain databases

CDDicd16833, YfiH, 1 hit
Gene3Di3.60.140.10, 1 hit
InterProiView protein in InterPro
IPR003730, Cu_polyphenol_OxRdtase
IPR038371, Cu_polyphenol_OxRdtase_sf
IPR011324, Cytotoxic_necrot_fac-like_cat
PANTHERiPTHR30616, PTHR30616, 1 hit
PfamiView protein in Pfam
PF02578, Cu-oxidase_4, 1 hit
SUPFAMiSSF64438, SSF64438, 1 hit
TIGRFAMsiTIGR00726, TIGR00726, 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 nameiPURNU_UNKP
<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: Q1EIR0
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 5, 2017
Last sequence update: July 11, 2006
Last modified: June 2, 2021
This is version 40 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 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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