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Protein

Glutamate mutase epsilon subunit

Gene

glmE

Organism
Clostridium tetanomorphum
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 carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate).UniRule annotation1 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

adenosylcob(III)alaminUniRule annotation1 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 20.6 sec(-1) for mutase activity with L-glutamate.
  1. KM=18 µM for adenosylcobalamin1 Publication
  2. KM=1.09 mM for L-glutamate1 Publication
  1. Vmax=22.8 µmol/min/mg enzyme1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-glutamate degradation via mesaconate pathway

This protein is involved in step 1 of the subpathway that synthesizes acetate and pyruvate from L-glutamate.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Glutamate mutase epsilon subunit (glmE), Glutamate mutase sigma subunit (glmS)
  2. Methylaspartate ammonia-lyase
  3. no protein annotated in this organism
  4. no protein annotated in this organism
This subpathway is part of the pathway L-glutamate degradation via mesaconate pathway, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes acetate and pyruvate from L-glutamate, the pathway L-glutamate degradation via mesaconate pathway and in Amino-acid degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei66L-glutamateUniRule annotation1
Binding sitei68Adenosylcobalamin; via carbonyl oxygenUniRule annotation1
Binding sitei100L-glutamateUniRule annotation1
Binding sitei123AdenosylcobalaminUniRule annotation1
Binding sitei171L-glutamateUniRule annotation1
Binding sitei177L-glutamateUniRule annotation1
Binding sitei180Adenosylcobalamin; via carbonyl oxygenUniRule annotation1
Binding sitei181L-glutamateUniRule annotation1
Binding sitei297Adenosylcobalamin; via amide nitrogenUniRule annotation1
Binding sitei326AdenosylcobalaminUniRule annotation1
Binding sitei330Adenosylcobalamin; via carbonyl oxygenUniRule annotation1
Binding sitei334Adenosylcobalamin; via amide nitrogenUniRule annotation1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionIsomerase
LigandCobalamin, Cobalt

Enzyme and pathway databases

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q05509

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

More...
UniPathwayi
UPA00561;UER00617

<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:
Glutamate mutase epsilon subunitUniRule annotation (EC:5.4.99.1UniRule annotation)
Alternative name(s):
Glutamate mutase E chainUniRule annotation
Glutamate mutase large subunitUniRule annotation
Methylaspartate mutaseUniRule annotation
<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:glmEUniRule annotation
Synonyms:mutE
<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>OrganismiClostridium tetanomorphum
<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 identifieri1553 [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 lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000875121 – 485Glutamate mutase epsilon subunitAdd BLAST485

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q05509

<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

Heterotetramer composed of 2 epsilon subunits (GlmE) and 2 sigma subunits (GlmS). GlmE exists as a homodimer and GlmS as a monomer (Probable).1 Publication

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q05509

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

More...
SMRi
Q05509

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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

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>Regioni149 – 150L-glutamate 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 methylaspartate mutase GlmE subunit family.UniRule annotation

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00245 Glm_e, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.90.970.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01923 Me_Asp_mutase_E, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR016176 Cbl-dep_enz_cat
IPR006396 Glu_mut_E
IPR014714 Glu_mut_E_C_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF06368 Met_asp_mut_E, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF001495 Met_asp_mut_epsi, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51703 SSF51703, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01503 MthylAspMut_E, 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>.<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.

Q05509-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MELKNKKWTD EEFFKQREEV LKQWPTGKEV DLQEAVDYLK KVPTEKNFAD
60 70 80 90 100
KLVRAKEAGI TLAQPRAGVA LLDEHINLLR YLQDEGGADL LPSTIDAYTR
110 120 130 140 150
QNRYEECEIG IKESEKAGRS LLNGFPGVNH GVKGCRKVLE SVNLPLQARH
160 170 180 190 200
GTPDSRLLAE IIHAGGWTSN EGGGISYNIP YAKSVPIDKC LKDWQYCDRL
210 220 230 240 250
VGFYEEQGVH INREPFGPLT GTLVPPSMSN AVGITEALLA AEQGVKNITV
260 270 280 290 300
GYGECGNMLQ DIAALRCLEE QTNEYLKAYG YNDVFVTTVF HQWMGGFPQD
310 320 330 340 350
ESKAFGVIVT ATTIASLAGA TKVIVKTPHE AIGIPTKEAN ASGIKATKMA
360 370 380 390 400
LNMLEGQRMP MSKELETEMA IIKAETKCIL DKMFELGKGD LAVGTVKAFE
410 420 430 440 450
TGVMDIPFGP SKYNAGKMMP VRDNLGCVRY LEFGNVPFTE ELKNYNRERL
460 470 480
AERAKFEGRE VSFQMVIDDI FAVGKGRLIG RPENK
Length:485
Mass (Da):53,741
Last modified:February 1, 1995 - 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:i131792A392CACCC0
GO

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 conflicti8W → L AA sequence (PubMed:1397267).Curated1
Sequence conflicti12E → G AA sequence (PubMed:1397267).Curated1
Sequence conflicti17R → A AA sequence (PubMed:1397267).Curated1
Sequence conflicti19E → G AA sequence (PubMed:1397267).Curated1

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
X70499 Genomic DNA Translation: CAA49910.1
X70695 Genomic DNA Translation: CAA50026.1
S48141 Genomic DNA Translation: AAB24069.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S32433

<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
X70499 Genomic DNA Translation: CAA49910.1
X70695 Genomic DNA Translation: CAA50026.1
S48141 Genomic DNA Translation: AAB24069.1
PIRiS32433

3D structure databases

ProteinModelPortaliQ05509
SMRiQ05509
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ05509

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayi
UPA00561;UER00617

SABIO-RKiQ05509

Family and domain databases

CDDicd00245 Glm_e, 1 hit
Gene3Di3.90.970.10, 1 hit
HAMAPiMF_01923 Me_Asp_mutase_E, 1 hit
InterProiView protein in InterPro
IPR016176 Cbl-dep_enz_cat
IPR006396 Glu_mut_E
IPR014714 Glu_mut_E_C_dom_sf
PfamiView protein in Pfam
PF06368 Met_asp_mut_E, 1 hit
PIRSFiPIRSF001495 Met_asp_mut_epsi, 1 hit
SUPFAMiSSF51703 SSF51703, 1 hit
TIGRFAMsiTIGR01503 MthylAspMut_E, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiGLME_CLOTT
<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: Q05509
<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: February 1, 1995
Last sequence update: February 1, 1995
Last modified: December 5, 2018
This is version 85 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

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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