Glutamate mutase sigma subunit
Details
- Name
- Glutamate mutase sigma subunit
- Synonyms
- 5.4.99.1
- Glutamate mutase S chain
- Glutamate mutase small subunit
- Methylaspartate mutase
- mutS
- Gene Name
- glmS
- Organism
- Clostridium tetanomorphum
- Amino acid sequence
>lcl|BSEQ0016555|Glutamate mutase sigma subunit MEKKTIVLGVIGSDCHAVGNKILDHSFTNAGFNVVNIGVLSSQEDFINAAIETKADLICV SSLYGQGEIDCKGLREKCDEAGLKGIKLFVGGNIVVGKQNWPDVEQRFKAMGFDRVYPPG TSPETTIADMKEVLGVE
- Number of residues
- 137
- Molecular Weight
- 14747.8
- Theoretical pI
- 4.74
- GO Classification
- Functionscobalamin binding / metal ion binding / methylaspartate mutase activityProcessesanaerobic glutamate catabolic process / glutamate catabolic process via L-citramalate
- General Function
- Methylaspartate mutase activity
- Specific Function
- Catalyzes the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate).
- Pfam Domain Function
- B12-binding (PF02310)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0003511|414 bp ATGGAGAAAAAGACTATTGTTCTTGGAGTTATTGGTTCAGACTGTCATGCAGTTGGTAAC AAAATATTAGACCACTCATTTACAAATGCAGGCTTCAATGTTGTTAACATAGGAGTTTTA TCATCACAGGAAGATTTTATAAATGCAGCTATAGAAACTAAAGCAGACCTTATATGTGTT TCTTCATTATATGGACAGGGAGAAATTGACTGTAAAGGATTAAGAGAAAAGTGTGATGAA GCAGGACTTAAAGGAATAAAATTATTTGTTGGCGGAAACATTGTTGTTGGTAAACAAAAC TGGCCAGATGTTGAACAGAGATTTAAAGCAATGGGATTTGATAGAGTATATCCACCAGGA ACATCTCCAGAAACAACAATAGCTGATATGAAAGAAGTTTTAGGAGTAGAATAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q05488 UniProtKB Entry Name GMSS_CLOTT GenBank Protein ID 49240 GenBank Gene ID X70499 - General References
- Marsh EN, Holloway DE: Cloning and sequencing of glutamate mutase component S from Clostridium tetanomorphum. Homologies with other cobalamin-dependent enzymes. FEBS Lett. 1992 Sep 28;310(2):167-70. [Article]
- Brecht M, Kellermann J, Pluckthun A: Cloning and sequencing of glutamate mutase component E from Clostridium tetanomorphum. FEBS Lett. 1993 Mar 15;319(1-2):84-9. [Article]
- Holloway DE, Marsh EN: Adenosylcobalamin-dependent glutamate mutase from Clostridium tetanomorphum. Overexpression in Escherichia coli, purification, and characterization of the recombinant enzyme. J Biol Chem. 1994 Aug 12;269(32):20425-30. [Article]
- Tollinger M, Konrat R, Hilbert BH, Marsh EN, Krautler B: How a protein prepares for B12 binding: structure and dynamics of the B12-binding subunit of glutamate mutase from Clostridium tetanomorphum. Structure. 1998 Aug 15;6(8):1021-33. [Article]
- Hoffmann B, Tollinger M, Konrat R, Huhta M, Marsh EN, Krautler B: A protein pre-organized to trap the nucleotide moiety of coenzyme B(12): refined solution structure of the B(12)-binding subunit of glutamate mutase from Clostridium tetanomorphum. Chembiochem. 2001 Sep 3;2(9):643-55. [Article]
- Tollinger M, Eichmuller C, Konrat R, Huhta MS, Marsh EN, Krautler B: The B(12)-binding subunit of glutamate mutase from Clostridium tetanomorphum traps the nucleotide moiety of coenzyme B(12). J Mol Biol. 2001 Jun 8;309(3):777-91. [Article]