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Q05509 (GLME_CLOTT) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Methylaspartate mutase E chain

EC=5.4.99.1
Alternative name(s):
Glutamate mutase subunit epsilon
Gene names
Name:mutE
OrganismClostridium tetanomorphum
Taxonomic identifier1553 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length485 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

Possible heterotetramer, composed of two E chains and two S chains. E exists as a homodimer and S as a monomer.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 485485Methylaspartate mutase E chain
PRO_0000087512

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.

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.
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: October 16, 2013
This is version 68 of the entry and version 1 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