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P80077 (GLME_CLOCO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 84. 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 epsilon subunit

EC=5.4.99.1
Alternative name(s):
Glutamate mutase E chain
Glutamate mutase large subunit
Methylaspartate mutase
Gene names
Name:glmE
OrganismClostridium cochlearium
Taxonomic identifier1494 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length483 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

Catalytic activity

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

Cofactor

Adenosylcobalamin. Ref.1 Ref.2 Ref.3 Ref.4

Enzyme regulation

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

Pathway

Amino-acid degradation; L-glutamate degradation via mesaconate pathway; acetate and pyruvate from L-glutamate: step 1/4. HAMAP-Rule MF_01923

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.4

Sequence similarities

Belongs to the methylaspartate mutase GlmE subunit family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

mamAP800782EBI-1028142,EBI-1028147

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 483483Glutamate mutase epsilon subunit HAMAP-Rule MF_01923
PRO_0000087511

Regions

Region149 – 1502L-glutamate binding HAMAP-Rule MF_01923

Sites

Binding site661L-glutamate
Binding site681Adenosylcobalamin; via carbonyl oxygen
Binding site1001L-glutamate
Binding site1231Adenosylcobalamin
Binding site1711L-glutamate
Binding site1771L-glutamate
Binding site1801Adenosylcobalamin; via carbonyl oxygen
Binding site1811L-glutamate
Binding site2971Adenosylcobalamin; via amide nitrogen
Binding site3261Adenosylcobalamin
Binding site3301Adenosylcobalamin; via carbonyl oxygen
Binding site3341Adenosylcobalamin; via amide nitrogen

Secondary structure

......................................................................... 483
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P80077 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 0789965B945B3F5C

FASTA48353,574
        10         20         30         40         50         60 
MELKNKKWTD EEFHKQREEV LQQWPTGKEV DLQEAVDYLK KIPAEKNFAE KLVLAKKKGI 

        70         80         90        100        110        120 
TMAQPRAGVA LLDEHIELLR YLQDEGGADF LPSTIDAYTR QNRYDECENG IKESEKAGRS 

       130        140        150        160        170        180 
LLNGFPGVNY GVKGCRKVLE AVNLPLQARH GTPDSRLLAE IIHAGGWTSN EGGGISYNVP 

       190        200        210        220        230        240 
YAKNVTIEKS LLDWQYCDRL VGFYEEQGVH INREPFGPLT GTLVPPSMSN AVGITEALLA 

       250        260        270        280        290        300 
AEQGVKNITV GYGECGNMIQ DIAALRCLEE QTNEYLKAYG YNDVFVTTVF HQWMGGFPQD 

       310        320        330        340        350        360 
ESKAFGVIVT ATTIAALAGA TKVIVKTPHE AIGIPTKEAN AAGIKATKMA LNMLEGQRMP 

       370        380        390        400        410        420 
MSKELETEMA VIKAETKCIL DKMFELGKGD LAIGTVKAFE TGVMDIPFGP SKYNAGKMMP 

       430        440        450        460        470        480 
VRDNLGCVRY LEFGNVPFTE EIKNYNRERL QERAKFEGRD VSFQMVIDDI FAVGKGRLIG 


RPE 

« 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]"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 1-26, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, COFACTOR, SUBUNIT.
Strain: ATCC 17787 / DSM 1285 / NCIB 10633.
[3]"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.
[4]"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: CAA56923.1.
PIRI40662.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CB7X-ray2.00B/D1-483[»]
1CCWX-ray1.60B/D1-483[»]
1I9CX-ray1.90B/D1-483[»]
ProteinModelPortalP80077.
SMRP80077. Positions 1-483.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP80077. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-1101.
SABIO-RKP80077.
UniPathwayUPA00561; UER00617.

Family and domain databases

Gene3D3.20.20.240. 1 hit.
3.90.970.10. 1 hit.
HAMAPMF_01923. Me_Asp_mutase_E.
InterProIPR016176. Cbl-dep_enz_cat.
IPR014348. Cbl-dep_enz_cat-sub.
IPR006396. Glu_mut_E.
IPR014714. Glu_mut_E_C_dom.
[Graphical view]
PfamPF06368. Met_asp_mut_E. 1 hit.
[Graphical view]
PIRSFPIRSF001495. Met_asp_mut_epsi. 1 hit.
SUPFAMSSF51703. SSF51703. 1 hit.
TIGRFAMsTIGR01503. MthylAspMut_E. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP80077.

Entry information

Entry nameGLME_CLOCO
AccessionPrimary (citable) accession number: P80077
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 84 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