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Q05509 (GLME_CLOTT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 70. 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 epsilon subunit

EC=5.4.99.1
Alternative name(s):
Glutamate mutase E chain
Glutamate mutase large subunit
Methylaspartate mutase
Gene names
Name:glmE
Synonyms:mutE
OrganismClostridium tetanomorphum
Taxonomic identifier1553 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length485 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.5

Catalytic activity

L-threo-3-methylaspartate = L-glutamate. Ref.5

Cofactor

Adenosylcobalamin. Ref.5

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 Probable. Ref.5

Sequence similarities

Belongs to the methylaspartate mutase GlmE subunit family.

Biophysicochemical properties

Kinetic parameters:

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

KM=18 µM for adenosylcobalamin Ref.5

KM=1.09 mM for L-glutamate

Vmax=22.8 µmol/min/mg enzyme

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 485485Glutamate mutase epsilon subunit HAMAP-Rule MF_01923
PRO_0000087512

Regions

Region149 – 1502L-glutamate binding By similarity

Sites

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

Experimental info

Sequence conflict81W → L AA sequence Ref.4
Sequence conflict121E → G AA sequence Ref.4
Sequence conflict171R → A AA sequence Ref.4
Sequence conflict191E → G AA sequence Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q05509 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 131792A392CACCC0

FASTA48553,741
        10         20         30         40         50         60 
MELKNKKWTD EEFFKQREEV LKQWPTGKEV DLQEAVDYLK KVPTEKNFAD KLVRAKEAGI 

        70         80         90        100        110        120 
TLAQPRAGVA LLDEHINLLR YLQDEGGADL LPSTIDAYTR QNRYEECEIG IKESEKAGRS 

       130        140        150        160        170        180 
LLNGFPGVNH GVKGCRKVLE SVNLPLQARH GTPDSRLLAE IIHAGGWTSN EGGGISYNIP 

       190        200        210        220        230        240 
YAKSVPIDKC LKDWQYCDRL VGFYEEQGVH INREPFGPLT GTLVPPSMSN AVGITEALLA 

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

       310        320        330        340        350        360 
ESKAFGVIVT ATTIASLAGA TKVIVKTPHE AIGIPTKEAN ASGIKATKMA LNMLEGQRMP 

       370        380        390        400        410        420 
MSKELETEMA IIKAETKCIL DKMFELGKGD LAVGTVKAFE TGVMDIPFGP SKYNAGKMMP 

       430        440        450        460        470        480 
VRDNLGCVRY LEFGNVPFTE ELKNYNRERL AERAKFEGRE VSFQMVIDDI FAVGKGRLIG 


RPENK 

« Hide

References

[1]"Cloning and sequencing of glutamate mutase component E from Clostridium tetanomorphum. Organization of the mut genes."
Holloway D.E., Marsh E.N.G.
FEBS Lett. 317:44-48(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: ATCC 15920 / DSM 528 / H1.
[3]"Cloning, sequencing, and expression in Escherichia coli of the Clostridium tetanomorphum gene encoding beta-methylaspartase and characterization of the recombinant protein."
Goda S.K., Minton N.P., Botting N.P., Gani D.
Biochemistry 31:10747-10756(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 278-485.
Strain: ATCC 15920 / DSM 528 / H1.
[4]"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: PROTEIN SEQUENCE OF 1-20.
Strain: NCIMB 11547.
[5]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X70499 Genomic DNA. Translation: CAA49910.1.
X70695 Genomic DNA. Translation: CAA50026.1.
S48141 Genomic DNA. Translation: AAB24069.1.
PIRS32433.

3D structure databases

ProteinModelPortalQ05509.
SMRQ05509. Positions 1-483.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKQ05509.
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...

Entry information

Entry nameGLME_CLOTT
AccessionPrimary (citable) accession number: Q05509
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 9, 2014
This is version 70 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