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P80077 (GLME_CLOCO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Methylaspartate mutase E chain
EC=5.4.99.1
Alternative name(s):
Glutamate mutase subunit epsilon
Gene names
Name:glmE
OrganismClostridium cochlearium
Taxonomic identifier1494 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length483 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Adenosylcobalamin.

Pathway

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

Subunit structure

Heterotetramer of 2 E subunits and 2 S subunits.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

mamAP800782EBI-1028142,EBI-1028147

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 483483Methylaspartate mutase E chain
PRO_0000087511

Secondary structure

1 ......................................................................... 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].
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.
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).
Strain: ATCC 17787 / DSM 1285 / NCIB 10633.
+Additional computationally mapped references.

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...

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.
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. Cbl-dep_enz_cat. 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: May 29, 2013
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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