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UniProtKB - P0AF12 (MTNN_ECOLI)

Entry version 133 (23 Feb 2022)
Sequence version 1 (20 Dec 2005)
Previous versions | rss
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Protein

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase

Gene

mtnN

Organism
Escherichia coli (strain K12)
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 irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively (PubMed:3911944, PubMed:16101288).

Also cleaves 5'-deoxyadenosine, a toxic by-product of radical S-adenosylmethionine (SAM) enzymes, into 5-deoxyribose and adenine. Thus, is required for in vivo function of the radical SAM enzymes biotin synthase and lipoic acid synthase, that are inhibited by 5'-deoxyadenosine accumulation (PubMed:15911379).

Can also use 5'-isobutylthioadenosine, 5'-n-butylthioadenosine, S-adenosyl-D-homocysteine, decarboxylated adenosylhomocysteine, deaminated adenosylhomocysteine and S-2-aza-adenosylhomocysteine as substrates in vitro (PubMed:3911944).

3 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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Strongly inhibited by aryl-substituted MTA analogs, alkyl-substituted MTA analogs, 5'-methylthioformycin, 5'-chloroformycin, S-formycinylhomocysteine, 5'-methylthiotubercidin, S-tubercidinylhomocysteine and S-8-aza-adenosylhomocysteine. Poorly inhibited by 5'-isobutylthioinosine, 5'-n-butylthioinosine, 5'-methylthio-3-deaza-adenosine, 5'-isobutylthio-3-deaza-adenosine, S-n-6-methyl-3-deaza-adenosylhomocysteine, S-adenosylhomocysteine sulphoxide and Sinefungin.4 Publications

<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 3.0 sec(-1) and 2.6 sec(-1) with 5'-methylthioadenosine and S-adenosylhomocysteine as substrate, respectively.1 Publication
  1. KM=0.4 µM for 5'-methylthioadenosine (at pH 7 and 37 degrees Celsius)1 Publication
  2. KM=0.8 µM for 5'-methylthioadenosine (at pH 7 and 22 degrees Celsius)1 Publication
  3. KM=4.3 µM for S-adenosylhomocysteine (at pH 7 and 37 degrees Celsius)1 Publication
  4. KM=1.3 µM for S-adenosylhomocysteine (at pH 7 and 22 degrees Celsius)1 Publication

pH dependencei

Exhibits activity across a broad pH range. Enzyme activity is moderately improved under acidic conditions.1 Publication

Temperature dependencei

Optimum temperature is 37-45 degrees Celsius. Rapidly inactivated after exposure for 10 minutes at 55 degrees Celsius.1 Publication

<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 1 of the subpathway that synthesizes S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route).UniRule annotation 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 S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route), 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 is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei12Proton acceptorUniRule annotation1 Publication1
<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 sitei78Substrate; via amide nitrogenUniRule annotation1 Publication1
Binding sitei152Substrate; via amide nitrogen and carbonyl oxygenUniRule annotation1 Publication1
Active sitei197Proton donorUniRule annotation1 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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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
Biological processAmino-acid biosynthesis, Methionine biosynthesis

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:EG11090-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.2.2.16, 2026
3.2.2.30, 2026
3.2.2.9, 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P0AF12

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

More...UniPathwayi		UPA00904;UER00871

<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'-methylthioadenosine/S-adenosylhomocysteine nucleosidase1 PublicationUniRule annotation (EC:3.2.2.9UniRule annotation3 Publications)
Short name:
MTA/SAH nucleosidaseUniRule annotation
Short name:
MTAN1 PublicationUniRule annotation
Alternative name(s):
5'-deoxyadenosine nucleosidaseUniRule annotation1 Publication
Short name:
DOA nucleosidaseUniRule annotation1 Publication
Short name:
dAdo nucleosidaseUniRule annotation1 Publication
5'-methylthioadenosine nucleosidaseUniRule annotation
Short name:
MTA nucleosidaseUniRule annotation
S-adenosylhomocysteine nucleosidaseUniRule annotation
Short name:
AdoHcy nucleosidaseUniRule annotation
Short name:
SAH nucleosidaseUniRule annotation
Short name:
SRH nucleosidaseUniRule 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:mtnNUniRule annotation
Synonyms:mtn, pfs, yadA
Ordered Locus Names:b0159, JW0155
<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>OrganismiEscherichia coli (strain K12)
<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 identifieri83333 [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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<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
  • UP000000318 <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
  • UP000000625 Componenti: Chromosome

<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

<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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Cells lacking this gene are deficient in biotin synthase (BioB) activity in vivo due to accumulation of 5'-deoxyadenosine.1 Publication

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>Mutagenesisi9M → A: 13-19% of wild-type catalytic efficiency. 1 Publication1
Mutagenesisi12E → A or Q: Loss of catalytic activity. 1 Publication1
Mutagenesisi50I → A: 12-23% of wild-type catalytic efficiency. 1 Publication1
Mutagenesisi76S → A: 13-23% of wild-type catalytic efficiency. 1 Publication1
Mutagenesisi151F → A: 0.5% of wild-type catalytic efficiency. 1 Publication1
Mutagenesisi173M → A: 0.5% of wild-type catalytic efficiency. 1 Publication1
Mutagenesisi174E → A or Q: Loss of catalytic activity. 1 Publication1
Mutagenesisi193R → A: 13-28% of wild-type catalytic efficiency. 1 Publication1
Mutagenesisi196S → A: 2-4% of wild-type catalytic efficiency. 1 Publication1
Mutagenesisi197D → A or N: Loss of catalytic activity. 1 Publication1
Mutagenesisi207F → A: 2% of wild-type catalytic efficiency. 1 Publication1

Chemistry databases

Drug and drug target database

More...DrugBanki		DB02158, (2S,3S,4R,5S)-2-(4-Amino-4,5-dihydro-1H-pyrrolo[3,2-d]pyrimidin-7-yl)-5-[(methylsulfanyl)methyl]-3,4-pyrrolidinediol
DB08606, (3R,4S)-1-[(4-AMINO-5H-PYRROLO[3,2-D]PYRIMIDIN-7-YL)METHYL]-4-[(METHYLSULFANYL)METHYL]PYRROLIDIN-3-OL
DB02933, 5'-Deoxy-5'-(Methylthio)-Tubercidin
DB00173, Adenine
DB02281, Formycin

<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_00001644391 – 2325'-methylthioadenosine/S-adenosylhomocysteine nucleosidaseAdd BLAST232

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P0AF12

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

More...PaxDbi		P0AF12

PRoteomics IDEntifications database

More...PRIDEi		P0AF12

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...SWISS-2DPAGEi		P0AF12

<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

Homodimer.

UniRule annotation4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

P0AF12
With#Exp.IntAct
itself2EBI-1114261,EBI-1114261

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4260991, 38 interactors
852836, 1 interactor

Database of interacting proteins

More...DIPi		DIP-10270N

Protein interaction database and analysis system

More...IntActi		P0AF12, 7 interactors

STRING: functional protein association networks

More...STRINGi		511145.b0159

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P0AF12

<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

Secondary structure

1232
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P0AF12

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P0AF12

<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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni173 – 174Substrate bindingUniRule annotation2

<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 PNP/UDP phosphorylase family. MtnN subfamily.UniRule annotationCurated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG0775, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_031248_2_2_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P0AF12

Database for complete collections of gene phylogenies

More...PhylomeDBi		P0AF12

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.50.1580, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_01684, Salvage_MtnN, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR010049, MTA_SAH_Nsdase
IPR000845, Nucleoside_phosphorylase_d
IPR035994, Nucleoside_phosphorylase_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01048, PNP_UDP_1, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF53167, SSF53167, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR01704, MTA/SAH-Nsdase, 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.

P0AF12-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKIGIIGAME EEVTLLRDKI ENRQTISLGG CEIYTGQLNG TEVALLKSGI 
        60         70         80         90        100
GKVAAALGAT LLLEHCKPDV IINTGSAGGL APTLKVGDIV VSDEARYHDA 
       110        120        130        140        150
DVTAFGYEYG QLPGCPAGFK ADDKLIAAAE ACIAELNLNA VRGLIVSGDA 
       160        170        180        190        200
FINGSVGLAK IRHNFPQAIA VEMEATAIAH VCHNFNVPFV VVRAISDVAD 
       210        220        230 
QQSHLSFDEF LAVAAKQSSL MVESLVQKLA HG
Length:232
Mass (Da):24,354
Last modified:December 20, 2005 - 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:i9B1FF9BEC39D4F2C
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 AAA23678 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti212 – 232AVAAK…KLAHG → LLPLNSPA in AAA23678 (PubMed:2157212).CuratedAdd BLAST21
Sequence conflicti212 – 232AVAAK…KLAHG → LLPLNSPA in AAA24322 (PubMed:2157212).CuratedAdd BLAST21

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
M31772 Genomic DNA Translation: AAA23678.1 Different initiation.
U24438 Genomic DNA Translation: AAC38291.1
M83735 Genomic DNA Translation: AAA24322.1
U70214 Genomic DNA Translation: AAB08589.1
U00096 Genomic DNA Translation: AAC73270.1
AP009048 Genomic DNA Translation: BAB96736.1

Protein sequence database of the Protein Information Resource

More...PIRi		S45227

NCBI Reference Sequences

More...RefSeqi		NP_414701.1, NC_000913.3
WP_000689844.1, NZ_SSZK01000004.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC73270; AAC73270; b0159
BAB96736; BAB96736; BAB96736

Database of genes from NCBI RefSeq genomes

More...GeneIDi		66671551
948542

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW0155
eco:b0159

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.2121

<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
M31772 Genomic DNA Translation: AAA23678.1 Different initiation.
U24438 Genomic DNA Translation: AAC38291.1
M83735 Genomic DNA Translation: AAA24322.1
U70214 Genomic DNA Translation: AAB08589.1
U00096 Genomic DNA Translation: AAC73270.1
AP009048 Genomic DNA Translation: BAB96736.1
PIRiS45227
RefSeqiNP_414701.1, NC_000913.3
WP_000689844.1, NZ_SSZK01000004.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JYSX-ray1.90A/B1-232[»]
1NC1X-ray2.00A/B1-232[»]
1NC3X-ray2.20A/B1-232[»]
1Y6QX-ray2.20A/B1-232[»]
1Y6RX-ray2.20A/B1-232[»]
1Z5NX-ray2.10A/B1-232[»]
1Z5OX-ray2.00A/B1-232[»]
1Z5PX-ray2.00A1-232[»]
3O4VX-ray1.75A/B1-232[»]
4WKCX-ray1.64A1-232[»]
4YMLX-ray1.75A1-232[»]
SMRiP0AF12
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4260991, 38 interactors
852836, 1 interactor
DIPiDIP-10270N
IntActiP0AF12, 7 interactors
STRINGi511145.b0159

Chemistry databases

BindingDBiP0AF12
DrugBankiDB02158, (2S,3S,4R,5S)-2-(4-Amino-4,5-dihydro-1H-pyrrolo[3,2-d]pyrimidin-7-yl)-5-[(methylsulfanyl)methyl]-3,4-pyrrolidinediol
DB08606, (3R,4S)-1-[(4-AMINO-5H-PYRROLO[3,2-D]PYRIMIDIN-7-YL)METHYL]-4-[(METHYLSULFANYL)METHYL]PYRROLIDIN-3-OL
DB02933, 5'-Deoxy-5'-(Methylthio)-Tubercidin
DB00173, Adenine
DB02281, Formycin

2D gel databases

SWISS-2DPAGEiP0AF12

Proteomic databases

jPOSTiP0AF12
PaxDbiP0AF12
PRIDEiP0AF12

Genome annotation databases

EnsemblBacteriaiAAC73270; AAC73270; b0159
BAB96736; BAB96736; BAB96736
GeneIDi66671551
948542
KEGGiecj:JW0155
eco:b0159
PATRICifig|1411691.4.peg.2121

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...EchoBASEi		EB1082

Phylogenomic databases

eggNOGiCOG0775, Bacteria
HOGENOMiCLU_031248_2_2_6
InParanoidiP0AF12
PhylomeDBiP0AF12

Enzyme and pathway databases

UniPathwayiUPA00904;UER00871
BioCyciEcoCyc:EG11090-MONOMER
BRENDAi3.2.2.16, 2026
3.2.2.30, 2026
3.2.2.9, 2026
SABIO-RKiP0AF12

Miscellaneous databases

EvolutionaryTraceiP0AF12

Protein Ontology

More...PROi		PR:P0AF12

Family and domain databases

Gene3Di3.40.50.1580, 1 hit
HAMAPiMF_01684, Salvage_MtnN, 1 hit
InterProiView protein in InterPro
IPR010049, MTA_SAH_Nsdase
IPR000845, Nucleoside_phosphorylase_d
IPR035994, Nucleoside_phosphorylase_sf
PfamiView protein in Pfam
PF01048, PNP_UDP_1, 1 hit
SUPFAMiSSF53167, SSF53167, 1 hit
TIGRFAMsiTIGR01704, MTA/SAH-Nsdase, 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 nameiMTNN_ECOLI
<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: P0AF12
Secondary accession number(s): P24247
<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 20, 2005
Last sequence update: December 20, 2005
Last modified: February 23, 2022
This is version 133 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

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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