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Q32IJ3 (GMSS_SHIDS) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 58. 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
Ordered Locus Names:SDY_0676
OrganismShigella dysenteriae serotype 1 (strain Sd197) [Reference proteome] [HAMAP]
Taxonomic identifier300267 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

Protein attributes

Sequence length149 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 caution

The sequence ABB60864.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 149149Glutamate mutase sigma subunit HAMAP-Rule MF_00526
PRO_0000264143

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
Q32IJ3 [UniParc].

Last modified December 12, 2006. Version 2.
Checksum: B785DAE49F27D9D0

FASTA14916,430
        10         20         30         40         50         60 
MKKATLVIGV IGADCHAVGN KVLDRVFSNH DFRVINLGVM VSQDEYIDAA IETGADAIVV 

        70         80         90        100        110        120 
SSIYGHGDID CLGMRERCIE RGLGDILLYV GGNLVVGKHD FADVETKFKE MGFDRVFAPS 

       130        140 
HDLEDVCQLM AHDINQRHDV DTRILEEAI 

« Hide

References

[1]"Genome dynamics and diversity of Shigella species, the etiologic agents of bacillary dysentery."
Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J., Xu J. expand/collapse author list , Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J., Jin Q.
Nucleic Acids Res. 33:6445-6458(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sd197.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000034 Genomic DNA. Translation: ABB60864.1. Different initiation.
RefSeqYP_402353.1. NC_007606.1.

3D structure databases

ProteinModelPortalQ32IJ3.
SMRQ32IJ3. Positions 1-119.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING300267.SDY_0676.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB60864; ABB60864; SDY_0676.
GeneID3799220.
KEGGsdy:SDY_0676.
PATRIC18690633. VBIShiDys99784_0789.

Phylogenomic databases

eggNOGCOG2185.
HOGENOMHOG000011065.
KOK01846.
OrthoDBEOG6CP428.

Enzyme and pathway databases

BioCycSDYS300267:GJEW-672-MONOMER.
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_SHIDS
AccessionPrimary (citable) accession number: Q32IJ3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: December 12, 2006
Last modified: July 9, 2014
This is version 58 of the entry and version 2 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