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Q05488 (GMSS_CLOTT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:mutS
OrganismClostridium tetanomorphum
Taxonomic identifier1553 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length137 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate). Ref.3

Catalytic activity

L-threo-3-methylaspartate = L-glutamate. Ref.3

Cofactor

Adenosylcobalamin. Ref.3

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. Ref.3

Sequence similarities

Belongs to the methylaspartate mutase GlmS subunit family.

Contains 1 B12-binding domain.

Biophysicochemical properties

Kinetic parameters:

Kcat is 20.6 sec(-1) for mutase activity with L-glutamate.

KM=18 µM for adenosylcobalamin Ref.3

KM=1.09 mM for L-glutamate

Vmax=22.8 µmol/min/mg enzyme

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 137137Glutamate mutase sigma subunit HAMAP-Rule MF_00526
PRO_0000216445

Regions

Domain3 – 137135B12-binding
Region13 – 175Adenosylcobalamin binding By similarity
Region61 – 633Adenosylcobalamin binding By similarity
Region93 – 975Adenosylcobalamin binding By similarity

Sites

Metal binding161Cobalt (cobalamin axial ligand)

Secondary structure

.............................. 137
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q05488 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: E71FE55BA8CE3DB3

FASTA13714,748
        10         20         30         40         50         60 
MEKKTIVLGV IGSDCHAVGN KILDHSFTNA GFNVVNIGVL SSQEDFINAA IETKADLICV 

        70         80         90        100        110        120 
SSLYGQGEID CKGLREKCDE AGLKGIKLFV GGNIVVGKQN WPDVEQRFKA MGFDRVYPPG 

       130 
TSPETTIADM KEVLGVE 

« Hide

References

[1]"Cloning and sequencing of glutamate mutase component S from Clostridium tetanomorphum. Homologies with other cobalamin-dependent enzymes."
Marsh E.N.G., Holloway D.E.
FEBS Lett. 310:167-170(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-33.
Strain: NCIMB 11547.
[2]"Cloning and sequencing of glutamate mutase component E from Clostridium tetanomorphum."
Brecht M., Kellermann J., Plueckthun A.
FEBS Lett. 319:84-89(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-24.
Strain: ATCC 15920 / DSM 528 / H1.
[3]"Adenosylcobalamin-dependent glutamate mutase from Clostridium tetanomorphum. Overexpression in Escherichia coli, purification, and characterization of the recombinant enzyme."
Holloway D.E., Marsh E.N.
J. Biol. Chem. 269:20425-20430(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT.
[4]"How a protein prepares for B12 binding: structure and dynamics of the B12-binding subunit of glutamate mutase from Clostridium tetanomorphum."
Tollinger M., Konrat R., Hilbert B.H., Marsh E.N.G., Kraeutler B.
Structure 6:1021-1033(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
Strain: ATCC 15920 / DSM 528 / H1.
[5]"A protein pre-organized to trap the nucleotide moiety of coenzyme B(12): refined solution structure of the B(12)-binding subunit of glutamate mutase from Clostridium tetanomorphum."
Hoffmann B., Tollinger M., Konrat R., Huhta M., Marsh E.N., Krautler B.
ChemBioChem 2:643-655(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[6]"The B(12)-binding subunit of glutamate mutase from Clostridium tetanomorphum traps the nucleotide moiety of coenzyme B(12)."
Tollinger M., Eichmuller C., Konrat R., Huhta M.S., Marsh E.N., Krautler B.
J. Mol. Biol. 309:777-791(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X70499 Genomic DNA. Translation: CAA49908.1.
X68570 Genomic DNA. Translation: CAA48567.1.
PIRS29502.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BE1NMR-A1-137[»]
1FMFNMR-A1-137[»]
1ID8NMR-A1-137[»]
ProteinModelPortalQ05488.
SMRQ05488. Positions 1-137.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKQ05488.
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...

Other

EvolutionaryTraceQ05488.

Entry information

Entry nameGMSS_CLOTT
AccessionPrimary (citable) accession number: Q05488
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 9, 2014
This is version 80 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways