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Protein

Glutamate mutase sigma subunit

Gene

glmS

Organism
Clostridium tetani (strain Massachusetts / E88)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate).UniRule annotation

Catalytic activityi

L-threo-3-methylaspartate = L-glutamate.UniRule annotation

Cofactori

adenosylcob(III)alaminUniRule annotation

Pathway:iL-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 sigma subunit (glmS), Glutamate mutase epsilon subunit (mutE)
  2. no protein annotated in this organism
  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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi16 – 161Cobalt (cobalamin axial ligand)UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Cobalamin, Cobalt, Metal-binding

Enzyme and pathway databases

BioCyciCTET212717:GJAM-2372-MONOMER.
UniPathwayiUPA00561; UER00617.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate mutase sigma subunitUniRule annotation (EC:5.4.99.1UniRule annotation)
Alternative name(s):
Glutamate mutase S chainUniRule annotation
Glutamate mutase small subunitUniRule annotation
Methylaspartate mutaseUniRule annotation
Gene namesi
Name:glmSUniRule annotation
Synonyms:mutS
Ordered Locus Names:CTC_02568
OrganismiClostridium tetani (strain Massachusetts / E88)
Taxonomic identifieri212717 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
ProteomesiUP000001412 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 137137Glutamate mutase sigma subunitPRO_0000216444Add
BLAST

Interactioni

Subunit structurei

Heterotetramer composed of 2 epsilon subunits (GlmE) and 2 sigma subunits (GlmS). GlmE exists as a homodimer and GlmS as a monomer.UniRule annotation

Protein-protein interaction databases

STRINGi212717.CTC02568.

Structurei

3D structure databases

ProteinModelPortaliQ890S0.
SMRiQ890S0. Positions 1-137.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 137135B12-bindingUniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni13 – 175Adenosylcobalamin bindingUniRule annotation
Regioni61 – 633Adenosylcobalamin bindingUniRule annotation
Regioni93 – 975Adenosylcobalamin bindingUniRule annotation

Sequence similaritiesi

Belongs to the methylaspartate mutase GlmS subunit family.UniRule annotation
Contains 1 B12-binding domain.UniRule annotation

Phylogenomic databases

eggNOGiCOG2185.
KOiK01846.
OMAiGHGEMDC.
OrthoDBiEOG6CP428.

Family and domain databases

Gene3Di3.40.50.280. 1 hit.
HAMAPiMF_00526. Me_Asp_mutase_S.
InterProiIPR006158. Cobalamin-bd.
IPR006394. GlmS.
[Graphical view]
PfamiPF02310. B12-binding. 1 hit.
[Graphical view]
SUPFAMiSSF52242. SSF52242. 1 hit.
TIGRFAMsiTIGR01501. MthylAspMutase. 1 hit.
PROSITEiPS51332. B12_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q890S0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKKTIVLGV IGSDCHAVGN KILDHSFTAA GFNVVNIGVL SPQEDFINAA
60 70 80 90 100
IETKADAILV SSLYGQGEID CKGLRQKCDE AGLEGILLYV GGNIVVGKQH
110 120 130
WPDVEKRFKD MGYDRVYAPG TPPEVGIADL KEDLNIK
Length:137
Mass (Da):14,773
Last modified:May 30, 2003 - v1
Checksum:i9BDE133E7A8D0035
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE015927 Genomic DNA. Translation: AAO37025.1.
RefSeqiWP_011100686.1. NC_004557.1.

Genome annotation databases

EnsemblBacteriaiAAO37025; AAO37025; CTC_02568.
GeneIDi24254649.
KEGGictc:CTC02568.
PATRICi19513251. VBICloTet101274_2656.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE015927 Genomic DNA. Translation: AAO37025.1.
RefSeqiWP_011100686.1. NC_004557.1.

3D structure databases

ProteinModelPortaliQ890S0.
SMRiQ890S0. Positions 1-137.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi212717.CTC02568.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAO37025; AAO37025; CTC_02568.
GeneIDi24254649.
KEGGictc:CTC02568.
PATRICi19513251. VBICloTet101274_2656.

Phylogenomic databases

eggNOGiCOG2185.
KOiK01846.
OMAiGHGEMDC.
OrthoDBiEOG6CP428.

Enzyme and pathway databases

UniPathwayiUPA00561; UER00617.
BioCyciCTET212717:GJAM-2372-MONOMER.

Family and domain databases

Gene3Di3.40.50.280. 1 hit.
HAMAPiMF_00526. Me_Asp_mutase_S.
InterProiIPR006158. Cobalamin-bd.
IPR006394. GlmS.
[Graphical view]
PfamiPF02310. B12-binding. 1 hit.
[Graphical view]
SUPFAMiSSF52242. SSF52242. 1 hit.
TIGRFAMsiTIGR01501. MthylAspMutase. 1 hit.
PROSITEiPS51332. B12_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Massachusetts / E88.

Entry informationi

Entry nameiGMSS_CLOTE
AccessioniPrimary (citable) accession number: Q890S0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2003
Last sequence update: May 30, 2003
Last modified: July 22, 2015
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.