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Q9HN21 (GMSS_HALSA) 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
Synonyms:mamA
Ordered Locus Names:VNG_2286G
OrganismHalobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium) [Reference proteome] [HAMAP]
Taxonomic identifier64091 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHalobacterium

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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 149149Glutamate mutase sigma subunit HAMAP-Rule MF_00526
PRO_0000216449

Regions

Domain5 – 138134B12-binding
Region15 – 195Adenosylcobalamin binding By similarity
Region63 – 653Adenosylcobalamin binding By similarity
Region94 – 985Adenosylcobalamin binding By similarity

Sites

Metal binding181Cobalt (cobalamin axial ligand) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9HN21 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 25A631D386055E29

FASTA14915,390
        10         20         30         40         50         60 
MSATDPTVVL GTIGSDAHAV GITLLDHALR EAGFTVHNLG AQTAKTEFAT AAADHDADAV 

        70         80         90        100        110        120 
LVSSLYGHAQ QDCAGLHDQL AAAGVDATTV VGGNLAVGQT DFETVKQRFE EMGFDRVFSA 

       130        140 
QTGFEAVVDA VKTELDVDER SPTTTTLGA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004437 Genomic DNA. Translation: AAG20400.1.
PIRD84379.
RefSeqNP_280920.1. NC_002607.1.

3D structure databases

ProteinModelPortalQ9HN21.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING64091.VNG2286G.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG20400; AAG20400; VNG_2286G.
GeneID1448702.
KEGGhal:VNG2286G.

Phylogenomic databases

eggNOGCOG2185.
KOK01846.
OMALNGHAYE.
PhylomeDBQ9HN21.

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_HALSA
AccessionPrimary (citable) accession number: Q9HN21
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: March 1, 2001
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