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Protein

Glutamate mutase sigma subunit

Gene

glmS

Organism
Treponema denticola (strain ATCC 35405 / CIP 103919 / DSM 14222)
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: 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. 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 bindingi17 – 171Cobalt (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

BioCyciTDEN243275:GJ7G-1037-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:mamA
Ordered Locus Names:TDE_1023
OrganismiTreponema denticola (strain ATCC 35405 / CIP 103919 / DSM 14222)
Taxonomic identifieri243275 [NCBI]
Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeTreponema
ProteomesiUP000008212 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 139139Glutamate mutase sigma subunitPRO_0000216448Add
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

STRINGi243275.TDE1023.

Structurei

3D structure databases

ProteinModelPortaliP61191.
SMRiP61191. Positions 4-131.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 139136B12-bindingUniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni14 – 185Adenosylcobalamin bindingUniRule annotation
Regioni62 – 643Adenosylcobalamin bindingUniRule annotation
Regioni94 – 985Adenosylcobalamin 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.
InterProiIPR006159. Acid_CoA_mut_C.
IPR006158. Cobalamin-bd.
IPR006394. GlmS.
[Graphical view]
PfamiPF02310. B12-binding. 1 hit.
[Graphical view]
SUPFAMiSSF52242. SSF52242. 1 hit.
TIGRFAMsiTIGR00640. acid_CoA_mut_C. 1 hit.
TIGR01501. MthylAspMutase. 1 hit.
PROSITEiPS51332. B12_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P61191-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARKIKLVLG VIGSDCHAVG NKILDYSLTE AGFEVTNIGV LSPQEDFINA
60 70 80 90 100
ALETNADAIL VSSLYGQGEL DCKGLREKCD EAGLKGIKLF VGGNIVVGKQ
110 120 130
NFDEVHKRFT AMGFDHVYPP GTPVETTIKD LHADFPDHA
Length:139
Mass (Da):14,988
Last modified:May 10, 2004 - v1
Checksum:iD43FFA8217AA6F15
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017226 Genomic DNA. Translation: AAS11512.1.
RefSeqiNP_971631.1. NC_002967.9.
WP_002670492.1. NC_002967.9.

Genome annotation databases

EnsemblBacteriaiAAS11512; AAS11512; TDE_1023.
GeneIDi2741502.
KEGGitde:TDE1023.
PATRICi20524254. VBITreDen445_0985.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017226 Genomic DNA. Translation: AAS11512.1.
RefSeqiNP_971631.1. NC_002967.9.
WP_002670492.1. NC_002967.9.

3D structure databases

ProteinModelPortaliP61191.
SMRiP61191. Positions 4-131.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243275.TDE1023.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAS11512; AAS11512; TDE_1023.
GeneIDi2741502.
KEGGitde:TDE1023.
PATRICi20524254. VBITreDen445_0985.

Phylogenomic databases

eggNOGiCOG2185.
KOiK01846.
OMAiGHGEMDC.
OrthoDBiEOG6CP428.

Enzyme and pathway databases

UniPathwayiUPA00561; UER00617.
BioCyciTDEN243275:GJ7G-1037-MONOMER.

Family and domain databases

Gene3Di3.40.50.280. 1 hit.
HAMAPiMF_00526. Me_Asp_mutase_S.
InterProiIPR006159. Acid_CoA_mut_C.
IPR006158. Cobalamin-bd.
IPR006394. GlmS.
[Graphical view]
PfamiPF02310. B12-binding. 1 hit.
[Graphical view]
SUPFAMiSSF52242. SSF52242. 1 hit.
TIGRFAMsiTIGR00640. acid_CoA_mut_C. 1 hit.
TIGR01501. MthylAspMutase. 1 hit.
PROSITEiPS51332. B12_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35405 / CIP 103919 / DSM 14222.

Entry informationi

Entry nameiGMSS_TREDE
AccessioniPrimary (citable) accession number: P61191
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: May 27, 2015
This is version 79 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.