Methylaspartate ammonia-lyase
Details
- Name
- Methylaspartate ammonia-lyase
- Synonyms
- 3-methylaspartate ammonia-lyase
- 4.3.1.2
- Beta-methylaspartase
- MAL
- Gene Name
- Not Available
- Organism
- Citrobacter amalonaticus
- Amino acid sequence
>lcl|BSEQ0019406|Methylaspartate ammonia-lyase MKIKQALFTAGYSSFYFDDQQAIKNGAGHDGFIYTGDPVTPGFTSVRQAGECVSVQLILE NGAVAVGDCAAVQYSGAGGRDPLFLAEHFIPFLNDHIKPLLEGRDVDAFLPNARFFDKLR IDGNLLHTAVRYGLSQALLDATALASGRLKTEVVCDEWQLPCVPEAIPLFGQSGDDRYIA VDKMILKGVDVLPHALINNVEEKLGFKGEKLREYVRWLSDRILSLRSSPRYHPTLHIDVY GTIGLIFDMDPVRCAEYIASLEKEAQGLPLYIEGPVDAGNKPDQIRMLTAITKELTRLGS GVKIVADEWCNTYQDIVDFTDAGSCHMVQIKTPDLGGIHNIVDAVLYCNKHGMEAYQGGT CNETEISARTCVHVALAARPMRMLIKPGMGFDEGLNIVFNEMNRTIALLQTKD
- Number of residues
- 413
- Molecular Weight
- 45470.68
- Theoretical pI
- 5.15
- GO Classification
- Functionsmetal ion binding / methylaspartate ammonia-lyase activityProcessesglutamate catabolic process via L-citramalate
- General Function
- Methylaspartate ammonia-lyase activity
- Specific Function
- Involved in the methylaspartate cycle. Catalyzes the formation of the alpha,beta-unsaturated bond by the reversible anti elimination of ammonia from L-threo-beta-methylaspartate (L-threo-(2S,3S)-3-methylaspartate) to give mesaconate (By similarity).
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0006486|1242 bp ATGAAAATTAAACAGGCGCTTTTCACCGCTGGCTACTCCTCATTCTATTTTGATGACCAG CAGGCGATCAAAAATGGCGCAGGTCATGACGGGTTTATTTATACCGGCGATCCGGTCACC CCGGGCTTTACTTCTGTGCGCCAGGCCGGCGAGTGCGTTTCCGTACAGCTGATTCTGGAA AATGGTGCGGTGGCGGTGGGTGATTGCGCCGCGGTGCAGTACTCCGGTGCCGGTGGTCGC GATCCGCTGTTCCTGGCTGAACATTTTATTCCGTTCCTCAACGACCACATTAAACCGCTG CTCGAAGGTCGCGACGTGGATGCGTTCCTGCCGAACGCCCGTTTCTTCGACAAACTGCGT ATCGACGGTAATTTGCTGCATACCGCCGTTCGCTACGGTCTGTCACAGGCACTGCTTGAT GCCACCGCGCTGGCCTCGGGCCGCCTGAAAACGGAAGTGGTGTGTGATGAATGGCAACTG CCCTGCGTACCGGAAGCCATTCCATTATTTGGTCAGAGCGGCGACGATCGCTACATCGCC GTCGACAAGATGATCCTCAAAGGGGTTGACGTCCTGCCGCATGCGCTTATCAACAACGTG GAAGAGAAGCTCGGTTTCAAAGGCGAAAAACTGCGTGAGTACGTGCGCTGGTTGTCCGAC CGTATTCTCAGCCTGCGCAGCAGCCCACGCTACCATCCGACGCTGCATATCGATGTGTAT GGCACCATCGGACTGATCTTCGATATGGACCCGGTACGCTGCGCCGAGTACATCGCCAGC CTGGAAAAAGAGGCTCAGGGTCTGCCGCTGTACATTGAAGGCCCGGTTGATGCAGGCAAC AAGCCGGATCAGATCCGCATGCTGACCGCCATCACCAAAGAGCTGACCCGCCTGGGTTCC GGCGTGAAAATTGTCGCAGACGAATGGTGTAACACCTATCAGGACATTGTGGACTTCACC GATGCCGGTAGCTGCCACATGGTGCAGATCAAAACCCCGGATCTCGGTGGCATTCACAAC ATCGTTGACGCGGTGCTGTACTGCAACAAACACGGGATGGAAGCCTACCAGGGCGGTACC TGTAACGAAACCGAAATCAGCGCCCGCACCTGCGTACATGTGGCTCTCGCCGCACGTCCG ATGCGTATGCTGATCAAGCCTGGCATGGGCTTCGATGAAGGTCTCAATATCGTGTTTAAC GAAATGAACCGCACCATCGCGCTGTTGCAGACTAAGGATTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID O66145 UniProtKB Entry Name MAAL_CITAM GenBank Gene ID AB005294 - General References
- Kato Y, Asano Y: Cloning, nucleotide sequencing, and expression of the 3-methylaspartate ammonia-lyase gene from Citrobacter amalonaticus strain YG-1002. Appl Microbiol Biotechnol. 1998 Oct;50(4):468-74. [Article]
- Levy CW, Buckley PA, Sedelnikova S, Kato Y, Asano Y, Rice DW, Baker PJ: Insights into enzyme evolution revealed by the structure of methylaspartate ammonia lyase. Structure. 2002 Jan;10(1):105-13. [Article]