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Q5V467 (GMSS1_HALMA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 64. 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 1

EC=5.4.99.1
Alternative name(s):
Glutamate mutase S chain 1
Glutamate mutase small subunit 1
Methylaspartate mutase 1
Gene names
Name:glmS1
Synonyms:mamA1
Ordered Locus Names:rrnAC0684
OrganismHaloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui) [Complete proteome] [HAMAP]
Taxonomic identifier272569 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloarcula

Protein attributes

Sequence length151 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) Probable. Ref.2

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 – 151151Glutamate mutase sigma subunit 1 HAMAP-Rule MF_00526
PRO_0000278195

Regions

Domain7 – 140134B12-binding
Region17 – 215Adenosylcobalamin binding By similarity
Region65 – 673Adenosylcobalamin binding By similarity
Region96 – 1005Adenosylcobalamin binding By similarity

Sites

Metal binding201Cobalt (cobalamin axial ligand) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5V467 [UniParc].

Last modified December 7, 2004. Version 1.
Checksum: 3812223A02A9142A

FASTA15116,306
        10         20         30         40         50         60 
MTGKYMPRTV ILGVIGSDAH VVGITILEQA LSAAGFEVIN LGVQTAQDEF VSAAKSHDAE 

        70         80         90        100        110        120 
AVLVSSLYGH ARQDCEGLHD ELDDAGLDVL TYVGGNLAVG QSDFEETQAT FRQMGFDRVF 

       130        140        150 
DAETDPEEAI EMLREDLQLT TTEAEQIRVD G 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY596297 Genomic DNA. Translation: AAV45685.1.
RefSeqYP_135391.1. NC_006396.1.

3D structure databases

ProteinModelPortalQ5V467.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272569.rrnAC0684.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV45685; AAV45685; rrnAC0684.
GeneID3130384.
KEGGhma:rrnAC0684.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2185.
HOGENOMHOG000011065.
KOK01846.
OMATSQEEFA.

Enzyme and pathway databases

BioCycHMAR272569:GJDH-607-MONOMER.
MetaCyc:MONOMER-16253.
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 nameGMSS1_HALMA
AccessionPrimary (citable) accession number: Q5V467
Entry history
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: December 7, 2004
Last modified: July 9, 2014
This is version 64 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