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A1JSN5 (GMSS_YERE8) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 49. 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:YE4040
OrganismYersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081) [Complete proteome] [HAMAP]
Taxonomic identifier393305 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length148 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 – 148148Glutamate mutase sigma subunit HAMAP-Rule MF_00526
PRO_0000303108

Regions

Domain3 – 140138B12-binding
Region13 – 175Adenosylcobalamin binding By similarity
Region61 – 633Adenosylcobalamin binding By similarity
Region93 – 975Adenosylcobalamin binding By similarity

Sites

Metal binding161Cobalt (cobalamin axial ligand) By similarity

Sequences

Sequence LengthMass (Da)Tools
A1JSN5 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: CECFB4E74D24FEEE

FASTA14816,196
        10         20         30         40         50         60 
MQNPTIVIGV IGADCHAVGN KVLDRVFTMH NFSVINLGVM VSQDEYIDAA IETGAQAIVV 

        70         80         90        100        110        120 
SSIYGHGEVD CIGMRENCVE RGIGEILLYV GGNLVIGKHD FSEIETKFKG MGFNRVFAPD 

       130        140 
TDLELVCSLM KRDIERVMQS EEAPEGMQ 

« Hide

References

[1]"The complete genome sequence and comparative genome analysis of the high pathogenicity Yersinia enterocolitica strain 8081."
Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L., Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T., Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S., Sanders M., Whitehead S. expand/collapse author list , Quail M.A., Dougan G., Parkhill J., Prentice M.B.
PLoS Genet. 2:2039-2051(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 13174 / 8081.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM286415 Genomic DNA. Translation: CAL14058.1.
RefSeqYP_001008182.1. NC_008800.1.

3D structure databases

ProteinModelPortalA1JSN5.
SMRA1JSN5. Positions 1-136.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING393305.YE4040.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL14058; CAL14058; YE4040.
GeneID4716331.
KEGGyen:YE4040.
PATRIC18567952. VBIYerEnt11519_4301.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2185.
HOGENOMHOG000011065.
KOK01846.
OMAMGFNRVF.
OrthoDBEOG6CP428.

Enzyme and pathway databases

UniPathwayUPA00561; UER00617.

Family and domain databases

Gene3D3.40.50.280. 1 hit.
HAMAPMF_00526. Me_Asp_mutase_S.
InterProIPR006158. Cobalamin-bd.
IPR006394. Me_Asp_mutase.
[Graphical view]
PfamPF02310. B12-binding. 1 hit.
[Graphical view]
SUPFAMSSF52242. SSF52242. 1 hit.
TIGRFAMsTIGR01501. MthylAspMutase. 1 hit.
PROSITEPS51332. B12_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGMSS_YERE8
AccessionPrimary (citable) accession number: A1JSN5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: February 6, 2007
Last modified: July 9, 2014
This is version 49 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