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P61191 (GMSS_TREDE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate mutase sigma subunit

EC=5.4.99.1
Alternative name(s):
Glutamate mutase S chain
Glutamate mutase small subunit
Methylaspartate mutase
Gene names
Name:glmS
Synonyms:mamA
Ordered Locus Names:TDE_1023
OrganismTreponema denticola (strain ATCC 35405 / CIP 103919 / DSM 14222) [Complete proteome] [HAMAP]
Taxonomic identifier243275 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeTreponema

Protein attributes

Sequence length139 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate) By similarity. HAMAP-Rule MF_00526

Catalytic activity

L-threo-3-methylaspartate = L-glutamate. HAMAP-Rule MF_00526

Cofactor

Adenosylcobalamin By similarity. HAMAP-Rule MF_00526

Pathway

Amino-acid degradation; L-glutamate degradation via mesaconate pathway; acetate and pyruvate from L-glutamate: step 1/4. HAMAP-Rule MF_00526

Subunit structure

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

Sequence similarities

Belongs to the methylaspartate mutase GlmS subunit family.

Contains 1 B12-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 139139Glutamate mutase sigma subunit HAMAP-Rule MF_00526
PRO_0000216448

Regions

Domain4 – 139136B12-binding
Region14 – 185Adenosylcobalamin binding By similarity
Region62 – 643Adenosylcobalamin binding By similarity
Region94 – 985Adenosylcobalamin binding By similarity

Sites

Metal binding171Cobalt (cobalamin axial ligand) By similarity

Sequences

Sequence LengthMass (Da)Tools
P61191 [UniParc].

Last modified May 10, 2004. Version 1.
Checksum: D43FFA8217AA6F15

FASTA13914,988
        10         20         30         40         50         60 
MARKIKLVLG VIGSDCHAVG NKILDYSLTE AGFEVTNIGV LSPQEDFINA ALETNADAIL 

        70         80         90        100        110        120 
VSSLYGQGEL DCKGLREKCD EAGLKGIKLF VGGNIVVGKQ NFDEVHKRFT AMGFDHVYPP 

       130 
GTPVETTIKD LHADFPDHA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017226 Genomic DNA. Translation: AAS11512.1.
RefSeqNP_971631.1. NC_002967.9.

3D structure databases

ProteinModelPortalP61191.
SMRP61191. Positions 4-131.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243275.TDE1023.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS11512; AAS11512; TDE_1023.
GeneID2741502.
KEGGtde:TDE1023.
PATRIC20524254. VBITreDen445_0985.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2185.
KOK01846.
OMALNGHAYE.
OrthoDBEOG6CP428.

Enzyme and pathway databases

BioCycTDEN243275:GJ7G-1037-MONOMER.
UniPathwayUPA00561; UER00617.

Family and domain databases

Gene3D3.40.50.280. 1 hit.
HAMAPMF_00526. Me_Asp_mutase_S.
InterProIPR006159. Acid_CoA_mut_C.
IPR006158. Cobalamin-bd.
IPR006394. Me_Asp_mutase.
[Graphical view]
PfamPF02310. B12-binding. 1 hit.
[Graphical view]
SUPFAMSSF52242. SSF52242. 1 hit.
TIGRFAMsTIGR00640. acid_CoA_mut_C. 1 hit.
TIGR01501. MthylAspMutase. 1 hit.
PROSITEPS51332. B12_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGMSS_TREDE
AccessionPrimary (citable) accession number: P61191
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: July 9, 2014
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways