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P80078 (GMSS_CLOCO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 86. 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·Interactions·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
OrganismClostridium cochlearium
Taxonomic identifier1494 [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.1 Ref.2 Ref.3

Catalytic activity

L-threo-3-methylaspartate = L-glutamate. Ref.1 Ref.2

Cofactor

Adenosylcobalamin. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6

Enzyme regulation

Competitively inhibited by (2S,4S)-4-fluoroglutamate, 2-methyleneglutarate, (2R,3RS)-3-fluoroglutamate and (S)-3-methylitaconate. Ref.1 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.1 Ref.2 Ref.3 Ref.5 Ref.6

Sequence similarities

Belongs to the methylaspartate mutase GlmS subunit family.

Contains 1 B12-binding domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

glmEP800772EBI-1028147,EBI-1028142

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 137137Glutamate mutase sigma subunit HAMAP-Rule MF_00526
PRO_0000216443

Regions

Domain3 – 137135B12-binding
Region13 – 175Adenosylcobalamin binding HAMAP-Rule MF_00526
Region61 – 633Adenosylcobalamin binding HAMAP-Rule MF_00526
Region93 – 975Adenosylcobalamin binding HAMAP-Rule MF_00526

Sites

Metal binding161Cobalt (cobalamin axial ligand)

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P80078 [UniParc].

Last modified December 13, 2001. Version 2.
Checksum: D9C5BF8DE5D1E878

FASTA13714,812
        10         20         30         40         50         60 
MEKKTIVLGV IGSDCHAVGN KILDHAFTNA GFNVVNIGVL SPQEVFIKAA IETKADAILL 

        70         80         90        100        110        120 
SSLYGQGEID CKGLRQKCDE AGLEGILLYV GGNIVVGKQH WPDVEKRFKD MGYDRVYAPG 

       130 
TPPEVGIADL KKDLNIE 

« Hide

References

[1]"Characterization of the coenzyme-B12-dependent glutamate mutase from Clostridium cochlearium produced in Escherichia coli."
Zelder O., Beatrix B., Leutbecher U., Buckel W.
Eur. J. Biochem. 226:577-585(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, COFACTOR, SUBUNIT.
Strain: ATCC 17787 / DSM 1285 / NCIB 10633.
[2]"Cloning, sequencing and expression in Escherichia coli of the gene encoding component S of the coenzyme B12-dependent glutamate mutase from Clostridium cochlearium."
Zelder O., Beatrix B., Buckel W.
FEMS Microbiol. Lett. 118:15-21(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT.
Strain: ATCC 17787 / DSM 1285 / NCIB 10633.
[3]"Glutamate mutase from Clostridium cochlearium. Purification, cobamide content and stereospecific inhibitors."
Leutbecher U., Boecher R., Linder D., Buckel W.
Eur. J. Biochem. 205:759-765(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-23, FUNCTION, ENZYME REGULATION, COFACTOR, SUBUNIT.
Strain: ATCC 17787 / DSM 1285 / NCIB 10633.
[4]"Structure and dynamics of the B12-binding subunit of glutamate mutase from Clostridium cochlearium."
Hoffmann B., Konrat R., Bothe H., Buckel W., Krautler B.
Eur. J. Biochem. 263:178-188(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[5]"Glutamate mutase from Clostridium cochlearium: the structure of a coenzyme B12-dependent enzyme provides new mechanistic insights."
Reitzer R., Gruber K., Jogl G., Wagner U.G., Bothe H., Buckel W., Kratky C.
Structure 7:891-902(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH COBALAMIN ANALOGS, COFACTOR, SUBUNIT.
Strain: ATCC 17787 / DSM 1285 / NCIB 10633.
[6]"Radical shuttling in a protein: ribose pseudorotation controls alkyl-radical transfer in the coenzyme B(12) dependent enzyme glutamate mutase."
Gruber K., Reitzer R., Kratky C.
Angew. Chem. Int. Ed. Engl. 40:3377-3380(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH COBALAMIN ANALOGS AND SUBSTRATE, COFACTOR, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X80997 Genomic DNA. Translation: CAA56921.1.
X75890 Genomic DNA. Translation: CAA53484.1.
PIRI40658.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B1ANMR-A1-137[»]
1CB7X-ray2.00A/C1-137[»]
1CCWX-ray1.60A/C1-137[»]
1I9CX-ray1.90A/C1-137[»]
ProteinModelPortalP80078.
SMRP80078. Positions 1-137.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP80078. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP80078.
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

EvolutionaryTraceP80078.

Entry information

Entry nameGMSS_CLOCO
AccessionPrimary (citable) accession number: P80078
Secondary accession number(s): Q60144
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: December 13, 2001
Last modified: July 9, 2014
This is version 86 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways