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Entry version 158 (02 Jun 2021)
Sequence version 2 (30 May 2000)
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Protein

Protein/nucleic acid deglycase 3

Gene

yajL

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

Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals (PubMed:26774339, PubMed:28596309).

Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Is able to repair glycated serum albumin, collagen, glyceraldehyde-3-phosphate dehydrogenase, and fructose biphosphate aldolase. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE) that cause irreversible damage (PubMed:25416785, PubMed:26774339).

Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. However, is less efficient than Hsp31 and YhbO, suggesting that YajL might be preferentially dedicated to protein repair (PubMed:28596309).

Displays a covalent chaperone activity with sulfenylated thiol proteins by forming mixed disulfides with members of the thiol proteome, and preferentially with sulfenylated cellular proteins, upon oxidative stress; these mixed disulfides can be subsequently reduced by low-molecular-weight thiols to regenerate YajL and reduced proteins (PubMed:22157000, PubMed:22321799).

Involved in biogenesis of ribosomal proteins, probably as a ribosomal protein-folding chaperone (PubMed:20889753).

Confers resistance to oxidative stress (PubMed:20124404, PubMed:22157000, PubMed:22321799).

Plays an important role in protection against electrophile/carbonyl stress (PubMed:26774339).

The chaperone activity reported for YajL is probably recruited to execute its deglycase activity, to interact with non-native glycated proteins and gain access to partially buried glycated sites (PubMed:25416785, PubMed:26774339).

Also displays an apparent glyoxalase activity that in fact reflects its deglycase activity (PubMed:26774339, PubMed:26678554).

8 Publications

Caution

Was originally (Ref. 1) thought to be involved in thiamine biosynthesis. However, this phenotype was probably due to an artifactual recombination event involving a portion of the adjacent thiI gene.Curated
The protein deglycation activity has been ascribed to a TRIS buffer artifact by a publication (PubMed:27903648), which has then been rebutted by clear biochemical experiments showing that DJ-1 family deglycases are bona fide deglycases (PubMed:28013050). Deglycase activity is even strengthened by a novel article that reports nucleotide deglycation activity (PubMed:28596309).Curated

<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 <a href="http://www.uniprot.org/help/function_section">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

Glyoxalase activity is inhibited by zinc ions (PubMed:26678554). Active as a chaperone in both its reduced and oxidized states, and is more active in its oxidized form (PubMed:20124404).2 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 70.32 min(-1) for glyoxalase activity with glyoxal as substrate (at pH 7.4 and 37 degrees Celsius) (PubMed:26678554). The apparent kcat of methylglyoxal and glyoxal degradation is 0.08 sec(-1), and 0.15 sec(-1), respectively (at 22 degrees Celsius) (PubMed:26774339).2 Publications
  1. KM=2.97 mM for glyoxal (at pH 7.4 and 37 degrees Celsius)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 is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei106NucleophileCurated1

<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 functionChaperone, Hydrolase
Biological processDNA damage, DNA repair, Stress response

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:HMP-KIN-MONOMER
MetaCyc:HMP-KIN-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.5.1.124, 2026
4.2.1.130, 2026

<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:
Protein/nucleic acid deglycase 32 Publications (EC:3.1.2.-1 Publication, EC:3.5.1.-1 Publication, EC:3.5.1.1241 Publication)
Alternative name(s):
Chaperone protein YajL
Maillard deglycase1 Publication
<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:yajL
Synonyms:thiJ
Ordered Locus Names:b0424, JW5057
<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>OrganismiEscherichia coli (strain K12)
<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 identifieri83333 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_manual">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 display highest sensitivity to carbonyl stress. The yajL mutant (but not the parental strain) suffers from a 100-fold decrease in viability after incubation for 48 h in LB medium containing 0.6% glucose, and the mutant is rescued by YajL- and DJ-1-overproducing plasmids. The wild-type strain displays a small quantity of glycated proteins after overnight culture in LB medium supplemented with 0.6% glucose, whereas the yajL mutant displays much higher levels of glycated proteins (PubMed:25416785, PubMed:26774339), and also higher DNA and RNA glycation levels (PubMed:28596309). Moreover, the double and triple mutants lacking yhbO and yajL, and yhbO, yajL and hchA, respectively, display impressive amounts of glycated proteins, suggesting that the YhbO, YajL and Hsp31 deglycases display relatively redundant functions (PubMed:26774339). The triple mutant displays higher glycation levels of free nucleotides (GTP and dGTP) than the parental strain, and shows higher glycation levels of DNA and RNA than those of single mutants (PubMed:28596309). The yajL mutant cells display decreased viability in methylglyoxal- or glucose-containing media (PubMed:26774339). They also display increased protein sulfenic acids levels, both before and after oxidative stress, but similar protein disulfides levels (PubMed:22321799). In aerobiosis, mutants show a protein aggregation phenotype, which is increased by oxidative stress (PubMed:20124404). Mutants show also altered gene expression and display decreased translation accuracy (PubMed:20889753). The yajL deletion mutant shows a negligible NADH dehydrogenase 1 activity and compensates for this low activity by utilizing NADH-independent alternative dehydrogenases, including pyruvate oxidase PoxB and D-aminoacid dehydrogenase DadA, and mixed acid aerobic fermentations characterized by acetate, lactate, succinate and ethanol excretion (PubMed:26377309). It shows up-regulation of genes involved in glycolytic and pentose phosphate pathways and alternative respiratory pathways (PubMed:26377309). Moreover, the yajL mutant preferentially catabolizes pyruvate-forming amino acids over Krebs cycle-related ones, and thus it utilizes pyruvate-centred respiro-fermentative metabolism to compensate for the NADH dehydrogenase 1 defect (PubMed:26377309).7 Publications

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>Mutagenesisi47C → A: Is not impaired in the formation of mixed disulfide with a sulfenylated protein. Has a monomeric quaternary structure. 2 Publications1
Mutagenesisi106C → A: Is impaired in the formation of mixed disulfide with cytoplasmic and sulfenylated proteins. Does not complement a disruption mutant. 3 Publications1
Mutagenesisi106C → D: Does not complement a disruption mutant. 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_00001578291 – 196Protein/nucleic acid deglycase 3Add BLAST196

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei106Cysteine sulfinic acid (-SO2H); alternate1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Cys-106 is easily oxidized to sulfinic acid.1 Publication

Keywords - PTMi

Oxidation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q46948

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

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PaxDbi
Q46948

PRoteomics IDEntifications database

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PRIDEi
Q46948

<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.

2 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4263345, 17 interactors
849455, 59 interactors

Protein interaction database and analysis system

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IntActi
Q46948, 17 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b0424

<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

1196
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

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SMRi
Q46948

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q46948

<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 peptidase C56 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0693, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_000445_44_2_6

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q46948

Database for complete collections of gene phylogenies

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PhylomeDBi
Q46948

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.40.50.880, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR029062, Class_I_gatase-like
IPR006287, DJ-1
IPR002818, DJ-1/PfpI

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01965, DJ-1_PfpI, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52317, SSF52317, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01383, not_thiJ, 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.

Q46948-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSASALVCLA PGSEETEAVT TIDLLVRGGI KVTTASVASD GNLAITCSRG
60 70 80 90 100
VKLLADAPLV EVADGEYDVI VLPGGIKGAE CFRDSTLLVE TVKQFHRSGR
110 120 130 140 150
IVAAICAAPA TVLVPHDIFP IGNMTGFPTL KDKIPAEQWL DKRVVWDARV
160 170 180 190
KLLTSQGPGT AIDFGLKIID LLVGREKAHE VASQLVMAAG IYNYYE
Length:196
Mass (Da):20,777
Last modified:May 30, 2000 - 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:i15282395CCF2CE75
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 AAA82704 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
The sequence AAB40180 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
U34923 Genomic DNA Translation: AAA82704.1 Different initiation.
U82664 Genomic DNA Translation: AAB40180.1 Different initiation.
U00096 Genomic DNA Translation: AAC73527.2
AP009048 Genomic DNA Translation: BAE76204.1

Protein sequence database of the Protein Information Resource

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PIRi
H64771

NCBI Reference Sequences

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RefSeqi
NP_414958.4, NC_000913.3
WP_001276305.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC73527; AAC73527; b0424
BAE76204; BAE76204; BAE76204

Database of genes from NCBI RefSeq genomes

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GeneIDi
945066

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW5057
eco:b0424

Pathosystems Resource Integration Center (PATRIC)

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PATRICi
fig|1411691.4.peg.1853

<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
U34923 Genomic DNA Translation: AAA82704.1 Different initiation.
U82664 Genomic DNA Translation: AAB40180.1 Different initiation.
U00096 Genomic DNA Translation: AAC73527.2
AP009048 Genomic DNA Translation: BAE76204.1
PIRiH64771
RefSeqiNP_414958.4, NC_000913.3
WP_001276305.1, NZ_LN832404.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2AB0X-ray1.10A/B1-196[»]
5SY4X-ray0.98A/B1-196[»]
SMRiQ46948
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4263345, 17 interactors
849455, 59 interactors
IntActiQ46948, 17 interactors
STRINGi511145.b0424

Proteomic databases

jPOSTiQ46948
PaxDbiQ46948
PRIDEiQ46948

Genome annotation databases

EnsemblBacteriaiAAC73527; AAC73527; b0424
BAE76204; BAE76204; BAE76204
GeneIDi945066
KEGGiecj:JW5057
eco:b0424
PATRICifig|1411691.4.peg.1853

Organism-specific databases

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

More...
EchoBASEi
EB3057

Phylogenomic databases

eggNOGiCOG0693, Bacteria
HOGENOMiCLU_000445_44_2_6
InParanoidiQ46948
PhylomeDBiQ46948

Enzyme and pathway databases

BioCyciEcoCyc:HMP-KIN-MONOMER
MetaCyc:HMP-KIN-MONOMER
BRENDAi3.5.1.124, 2026
4.2.1.130, 2026

Miscellaneous databases

EvolutionaryTraceiQ46948

Protein Ontology

More...
PROi
PR:Q46948

Family and domain databases

Gene3Di3.40.50.880, 1 hit
InterProiView protein in InterPro
IPR029062, Class_I_gatase-like
IPR006287, DJ-1
IPR002818, DJ-1/PfpI
PfamiView protein in Pfam
PF01965, DJ-1_PfpI, 1 hit
SUPFAMiSSF52317, SSF52317, 1 hit
TIGRFAMsiTIGR01383, not_thiJ, 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 nameiYAJL_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: Q46948
Secondary accession number(s): Q2MC02
<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: November 1, 1997
Last sequence update: May 30, 2000
Last modified: June 2, 2021
This is version 158 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

3D-structure, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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