MIO-dependent tyrosine 2,3-aminomutase
Details
- Name
- MIO-dependent tyrosine 2,3-aminomutase
- Kind
- protein
- Synonyms
- 5.4.3.6
- Tyrosine ammonia-lyase
- Gene Name
- Not Available
- UniProtKB Entry
- Q8GMG0Swiss-Prot
- Organism
- Streptomyces globisporus
- NCBI Taxonomy ID
- 1908
- Amino acid sequence
>lcl|BSEQ0012622|MIO-dependent tyrosine 2,3-aminomutase MALTQVETEIVPVSVDGETLTVEAVRRVAEERATVDVPAESIAKAQKSREIFEGIAEQNI PIYGVTTGYGEMIYMQVDKSKEVELQTNLVRSHSAGVGPLFAEDEARAIVAARLNTLAKG HSAVRPIILERLAQYLNEGITPAIPEIGSLGASGDLAPLSHVASTLIGEGYVLRDGRPVE TAQVLAERGIEPLELRFKEGLALINGTSGMTGLGSLVVGRALEQAQQAEIVTALLIEAVR GSTSPFLAEGHDIARPHEGQIDTAANMRALMRGSGLTVEHADLRRELQKDKEAGKDVQRS EIYLQKAYSLRAIPQVVGAVRDTLYHARHKLRIELNSANDNPLFFEGKEIFHGANFHGQP IAFAMDFVTIALTQLGVLAERQINRVLNRHLSYGLPEFLVSGDPGLHSGFAGAQYPATAL VAENRTIGPASTQSVPSNGDNQDVVSMGLISARNARRVLSNNNKILAVEYLAAAQAVDIS GRFDGLSPAAKATYEAVRRLVPTLGVDRYMADDIELVADALSRGEFLRAIARETDIQLR
- Number of residues
- 539
- Molecular Weight
- 58138.44
- Theoretical pI
- 5.4
- GO Classification
- Functionstyrosine 2,3-aminomutase activity / tyrosine ammonia-lyase activityProcessesantibiotic biosynthetic process / toxin biosynthetic process
- General Function
- Involved in the biosynthesis of the enediyne antitumor antibiotic C-1027. Catalyzes the MIO-dependent deamination of L-tyrosine generating the corresponding alpha,beta-unsaturated acid, (S)-beta-tyrosine.
- Specific Function
- histidine ammonia-lyase activity
- Pfam Domain Function
- Lyase_aromatic (PF00221)
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm (By similarity)
- Gene sequence
>lcl|BSEQ0007206|1497 bp GTGAGGGCTCTGCCGGGAAGTGGCGGATTGCGCATGGCAGGAGATGCCCCGACAGCGGCC GGGAATCGACGATGTCCCCCGACCCCTATCCAGCGTCCGCTGATCCTCAGGAGGCAGACC TTGCAGGCTCCAGAAGCGAAGAACGGCCGGTCCCCGGAGCAGCCGCAGGAAGAGCGGATC GTCCTGGACGTATGGCTGGCGAACTACCCGTTCCCCACCTATGACGGGCGTGACTTCCTC GCTCCGCTGCGCGAGCGGGCGGCGGAGTTCGAGCGCGCCCACCCCCGATACCGGGTCGAC ATCAACGGCCACGACTTCTGGACCATCCCCGAGAAGGTGGCGCGCGCCACCGCGGAGGGC AGGCCTCCGCACATAGCGGGCTACTACGCCACCGACAGCCAGTTGGCGCGGGACGCGCGC AGGCCCGACGGGAAGCCGGTCTTCACCTCGGTGGAGGCCGCGTTGGCCGGCCGGACGGAG ATACTGGGACACCCGGTGGTGGTGGAGGACCTCGACCCCGTGGTGCGCGACTCCTACTCG TTCGGGGGCGAGTTGGTGTCGCTGCCGCTCACGGTCACCACCATGCTCTGCTACGCCAAC TCCTCCCTCCTCGCGCGCGCCGGTGTTCCGGAGTTGCCCCGTACCTGGGATGAGGTCGAA GCAGCCTGCCAGGCGGTGGCCAGCGTCGACGGGGGGCCCGGTCACGGAATCACCTGGGCC AACGACGGCTGGGTTTTCCAGCAGGCCGTCGCCCTTCAGAACGGGGTGCTGACCGATCAG GACAACGGCCGCTCCGGCTCCGCCACGACGGTGGACGTCACATCGGACGAGATGCTGGAC TGGGTCCGCTGGTGGACGCACCTCCATGAGCGCGGCCATTACCTCTACACGGGCGGGCCC TCGGACTGGGGCGGGGCGTTCGAGGCTTTCGTCCAGCAGAAGGTCGCATTCACCTTCGAC TCGTCCAAGGCCGCCCGGGAACTCATCCAGGCCGGTGCACAGGCCGGTTTCGAGGTCGCG GTGTTCCCGTTGCCCAGGAACGCGAAGGCCCCGGTAGCGGGCCAGCCCGTCTCGGGAGAC TCCCTGTGGCTGGCCGCGGGACTCGACGAGACCACGCAGGACGGGCTGCTCGCTCTCACC CAGTACCTGATCAGCCCGGCCAACGCCGCGGACTGGCACCGCACCAACGGTTTCGTACCG GTGACCGGCGCGGCCGGGGAACTGCTGGAAGCGACAGGCTGGTTCGACCGCCGGCCGCAG CAACGGGTGGCCGGGGAGCAGTTGAAGGCGTCCGACCGGTCACCGGCGGCGCTCGGCGCG CTGCTCGGCGACTTCGCGGCCGTCAACGAGGTCATCACCGCAGCGATGGACGATGTCCTG CGCAGTGGAGCGGACCCCGCGAAGGCCTTCGCCGAAGCCGGCGTGGCCGCCCAGCAACTG CTCGATGCCTACAACGCCCGGAACCGCTCCGGATCCGGGACCCCCTCCGCCGTCTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q8GMG0 UniProtKB Entry Name TAM_STRGL GenBank Protein ID 24575077 GenBank Gene ID AY048670 PDB ID(s) 2OHY, 2QVE, 2RJR, 2RJS, 3KDY, 3KDZ - General References
- Liu W, Christenson SD, Standage S, Shen B: Biosynthesis of the enediyne antitumor antibiotic C-1027. Science. 2002 Aug 16;297(5584):1170-3. [Article]
- Christianson CV, Montavon TJ, Van Lanen SG, Shen B, Bruner SD: The structure of L-tyrosine 2,3-aminomutase from the C-1027 enediyne antitumor antibiotic biosynthetic pathway. Biochemistry. 2007 Jun 19;46(24):7205-14. Epub 2007 May 22. [Article]
- Montavon TJ, Christianson CV, Festin GM, Shen B, Bruner SD: Design and characterization of mechanism-based inhibitors for the tyrosine aminomutase SgTAM. Bioorg Med Chem Lett. 2008 May 15;18(10):3099-102. Epub 2007 Nov 19. [Article]
- Cooke HA, Bruner SD: Probing the active site of MIO-dependent aminomutases, key catalysts in the biosynthesis of beta-amino acids incorporated in secondary metabolites. Biopolymers. 2010 Sep;93(9):802-10. doi: 10.1002/bip.21500. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details (2S,3S)-3-(4-fluorophenyl)-2,3-dihydroxypropanoic acid experimental unknown target Details