Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
We are aiming to switch to the new UniProt website on Monday, May 9. Please explore and share your feedback. Take me to the new website.

UniProtKB - Q9WXM1 (AEEP_THEMA)

Entry version 109 (02 Jun 2021)
Sequence version 1 (01 Nov 1999)
Previous versions | rss
Add a publicationFeedback
Protein

L-Ala-D/L-Glu epimerase

Gene

TM_0006

Organism
Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
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>-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 epimerization of L-Ala-D-Glu to L-Ala-L-Glu and has probably a role in the metabolism of the murein peptide, of which L-Ala-D-Glu is a component. Is also able to catalyze the reverse reaction and the epimerization of a broad range of other dipeptides; is most efficient with L-Ala-D/L-Phe, L-Ala-D/L-Tyr, and L-Ala-D/L-His.

1 Publication

<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

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

<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

  1. KM=2.8 mM for L-Ala-L-Glu (at pH 7.5 and 28 degrees Celsius)1 Publication
  2. KM=1.3 mM for L-Ala-L-Phe (at pH 7.5 and 28 degrees Celsius)1 Publication
  3. KM=0.71 mM for L-Ala-L-Tyr (at pH 7.5 and 28 degrees Celsius)1 Publication
  4. KM=5.3 mM for L-Ala-L-His (at pH 7.5 and 28 degrees Celsius)1 Publication
  5. KM=2.9 mM for L-Ala-L-Leu (at pH 7.5 and 28 degrees Celsius)1 Publication
  6. KM=4.7 mM for L-Ile-L-Phe (at pH 7.5 and 28 degrees Celsius)1 Publication
  7. KM=3.9 mM for L-Lys-L-Phe (at pH 7.5 and 28 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: peptidoglycan degradation

This protein is involved in the pathway peptidoglycan degradation, which is part of Cell wall degradation.
View all proteins of this organism that are known to be involved in the pathway peptidoglycan degradation and in Cell wall degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei134Substrate1
Binding sitei159Substrate1
<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 sitei161Proton acceptor; specific for (R)-substrate epimerizationBy similarity1
<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 bindingi188Magnesium1
Binding sitei190Substrate1
Metal bindingi216Magnesium1
Metal bindingi241Magnesium1
Active sitei265Proton acceptor; specific for (S)-substrate epimerizationBy similarity1
Binding sitei292Substrate; via carbonyl oxygen1
Binding sitei317Substrate1
Binding sitei319Substrate1

<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 functionIsomerase
Biological processCell wall biogenesis/degradation
LigandMagnesium, Metal-binding

Enzyme and pathway databases

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		Q9WXM1

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

More...UniPathwayi		UPA00549

<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:
L-Ala-D/L-Glu epimerase (EC:5.1.1.202 Publications)
Short name:
AE epimerase
Short name:
AEE
<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
Ordered Locus Names:TM_0006
<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>OrganismiThermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
<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 identifieri243274 [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 › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga ›
<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
  • UP000008183 <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_00003889721 – 345L-Ala-D/L-Glu epimeraseAdd BLAST345

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		243274.THEMA_04770

<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

1345
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		Q9WXM1

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		Q9WXM1

<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 mandelate racemase/muconate lactonizing enzyme family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG4948, Bacteria

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9WXM1

Identification of Orthologs from Complete Genome Data

More...OMAi		MFGCYSD

Database of Orthologous Groups

More...OrthoDBi		951991at2

Family and domain databases

Conserved Domains Database

More...CDDi		cd03319, L-Ala-DL-Glu_epimerase, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.20.20.120, 1 hit
3.30.390.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR034603, Dipeptide_epimerase
IPR036849, Enolase-like_C_sf
IPR029017, Enolase-like_N
IPR029065, Enolase_C-like
IPR013342, Mandelate_racemase_C
IPR013341, Mandelate_racemase_N_dom

Pfam protein domain database

More...Pfami		View protein in Pfam
PF13378, MR_MLE_C, 1 hit
PF02746, MR_MLE_N, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00922, MR_MLE, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF51604, SSF51604, 1 hit
SSF54826, SSF54826, 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.

Q9WXM1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSRIVNVKLS LKRYEYEKPF HITGSVSSES RNVEVEIVLE SGVKGYGEAS 
        60         70         80         90        100
PSFRVNGERV EALLAIENAV REMITGIDVR NYARIFEITD RLFGFPSLKA 
       110        120        130        140        150
AVQFATLDAL SQELGTQVCY LLGGKRDEIE TDKTVGIDTV ENRVKEAKKI 
       160        170        180        190        200
FEEGFRVIKI KVGENLKEDI EAVEEIAKVT RGAKYIVDAN MGYTQKEAVE 
       210        220        230        240        250
FARAVYQKGI DIAVYEQPVR REDIEGLKFV RFHSPFPVAA DESARTKFDV 
       260        270        280        290        300
MRLVKEEAVD YVNIKLMKSG ISDALAIVEI AESSGLKLMI GCMGESSLGI 
       310        320        330        340 
NQSVHFALGT GAFEFHDLDS HLMLKEEVFR GKFIQDGPRM RVKDQ
Length:345
Mass (Da):38,664
Last modified:November 1, 1999 - 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:i587BDE71BB1E777B
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
AE000512 Genomic DNA Translation: AAD35100.1

Protein sequence database of the Protein Information Resource

More...PIRi		H72429

NCBI Reference Sequences

More...RefSeqi		NP_227822.1, NC_000853.1
WP_004082436.1, NZ_CP011107.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAD35100; AAD35100; TM_0006

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		tma:TM0006

<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
AE000512 Genomic DNA Translation: AAD35100.1
PIRiH72429
RefSeqiNP_227822.1, NC_000853.1
WP_004082436.1, NZ_CP011107.1

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
2ZADX-ray1.60A/B/C/D1-345[»]
3DEQX-ray2.10A/B/C/D1-345[»]
3DERX-ray1.90A/B/C/D1-345[»]
3DESX-ray2.30A/B/C/D1-345[»]
3DFYX-ray2.10A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-345[»]
SMRiQ9WXM1
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi243274.THEMA_04770

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		896814

Genome annotation databases

EnsemblBacteriaiAAD35100; AAD35100; TM_0006
KEGGitma:TM0006

Phylogenomic databases

eggNOGiCOG4948, Bacteria
InParanoidiQ9WXM1
OMAiMFGCYSD
OrthoDBi951991at2

Enzyme and pathway databases

UniPathwayiUPA00549
SABIO-RKiQ9WXM1

Miscellaneous databases

EvolutionaryTraceiQ9WXM1

Family and domain databases

CDDicd03319, L-Ala-DL-Glu_epimerase, 1 hit
Gene3Di3.20.20.120, 1 hit
3.30.390.10, 1 hit
InterProiView protein in InterPro
IPR034603, Dipeptide_epimerase
IPR036849, Enolase-like_C_sf
IPR029017, Enolase-like_N
IPR029065, Enolase_C-like
IPR013342, Mandelate_racemase_C
IPR013341, Mandelate_racemase_N_dom
PfamiView protein in Pfam
PF13378, MR_MLE_C, 1 hit
PF02746, MR_MLE_N, 1 hit
SMARTiView protein in SMART
SM00922, MR_MLE, 1 hit
SUPFAMiSSF51604, SSF51604, 1 hit
SSF54826, SSF54826, 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 nameiAEEP_THEMA
<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: Q9WXM1
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 24, 2009
Last sequence update: November 1, 1999
Last modified: June 2, 2021
This is version 109 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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

Do not show this banner again