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Q8RHY7 (GMSS_FUSNN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 79. 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:FN1853
OrganismFusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131) [Reference proteome] [HAMAP]
Taxonomic identifier190304 [NCBI]
Taxonomic lineageBacteriaFusobacteriaFusobacterialesFusobacteriaceaeFusobacterium

Protein attributes

Sequence length136 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 – 136136Glutamate mutase sigma subunit HAMAP-Rule MF_00526
PRO_0000216447

Regions

Domain3 – 136134B12-binding
Region13 – 175Adenosylcobalamin binding By similarity
Region61 – 633Adenosylcobalamin binding By similarity

Sites

Metal binding161Cobalt (cobalamin axial ligand) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8RHY7 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 934DB52D9D4B382C

FASTA13615,144
        10         20         30         40         50         60 
MAKKKIVIGV IGSDCHTVGN KIIHNKLEES GFDVVNIGAL SPQIDFINAA LETNSDAIIV 

        70         80         90        100        110        120 
SSIYGYGELD CQGIREKCNE YGLKDILLYI GGNIGSSNEK WENTEKRFKE MGFDRIYKPG 

       130 
TPIEETIIDL KKDFKI 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009951 Genomic DNA. Translation: AAL93952.1.
RefSeqNP_602653.1. NC_003454.1.

3D structure databases

ProteinModelPortalQ8RHY7.
SMRQ8RHY7. Positions 1-136.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING190304.FN1853.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL93952; AAL93952; FN1853.
GeneID992530.
KEGGfnu:FN1853.
PATRIC21949229. VBIFusNuc122357_0329.

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.
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_FUSNN
AccessionPrimary (citable) accession number: Q8RHY7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: June 1, 2002
Last modified: July 9, 2014
This is version 79 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