Oxalate decarboxylase OxdC
Details
- Name
- Oxalate decarboxylase OxdC
- Synonyms
- 4.1.1.2
- yvrK
- Gene Name
- oxdC
- Organism
- Bacillus subtilis (strain 168)
- Amino acid sequence
>lcl|BSEQ0011876|Oxalate decarboxylase OxdC MKKQNDIPQPIRGDKGATVKIPRNIERDRQNPDMLVPPETDHGTVSNMKFSFSDTHNRLE KGGYAREVTVRELPISENLASVNMRLKPGAIRELHWHKEAEWAYMIYGSARVTIVDEKGR SFIDDVGEGDLWYFPSGLPHSIQALEEGAEFLLVFDDGSFSENSTFQLTDWLAHTPKEVI AANFGVTKEEISNLPGKEKYIFENQLPGSLKDDIVEGPNGEVPYPFTYRLLEQEPIESEG GKVYIADSTNFKVSKTIASALVTVEPGAMRELHWHPNTHEWQYYISGKARMTVFASDGHA RTFNYQAGDVGYVPFAMGHYVENIGDEPLVFLEIFKDDHYADVSLNQWLAMLPETFVQAH LDLGKDFTDVLSKEKHPVVKKKCSK
- Number of residues
- 385
- Molecular Weight
- 43565.77
- Theoretical pI
- 5.11
- GO Classification
- Functionsmetal ion binding / nutrient reservoir activity / oxalate decarboxylase activityComponentscytoplasm
- General Function
- Oxalate decarboxylase activity
- Specific Function
- Converts oxalate to formate and CO(2) in an O(2)-dependent reaction. Can also catalyze minor side reactions: oxalate oxidation to produce H(2)O(2), and oxalate-dependent, H(2)O(2)-independent dye oxidations.
- Pfam Domain Function
- Cupin_1 (PF00190)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0011877|Oxalate decarboxylase OxdC (oxdC) ATGAAAAAACAAAATGACATTCCGCAGCCAATTAGAGGAGACAAAGGAGCAACGGTAAAA ATCCCGCGCAATATTGAAAGAGACCGGCAAAACCCTGATATGCTCGTTCCGCCTGAAACC GATCATGGCACCGTCAGCAATATGAAGTTTTCATTCTCTGATACTCATAACCGATTAGAA AAAGGCGGATATGCCCGGGAAGTGACAGTACGTGAATTGCCGATTTCAGAAAACCTTGCA TCCGTAAATATGCGGCTGAAGCCAGGCGCGATTCGCGAGCTTCACTGGCATAAAGAAGCT GAATGGGCTTATATGATTTACGGAAGTGCAAGAGTCACAATTGTAGATGAAAAAGGGCGC AGCTTTATTGACGATGTAGGTGAAGGAGACCTTTGGTACTTCCCGTCAGGCCTGCCGCAC TCCATCCAAGCGCTGGAGGAGGGAGCTGAGTTCCTGCTCGTGTTTGACGATGGATCATTC TCTGAAAACAGCACGTTCCAGCTGACAGATTGGCTGGCCCACACTCCAAAAGAAGTCATT GCTGCGAACTTCGGCGTGACAAAAGAAGAGATTTCCAATTTGCCTGGCAAAGAAAAATAT ATATTTGAAAACCAACTTCCTGGCAGTTTAAAAGATGATATTGTGGAAGGGCCGAATGGC GAAGTGCCTTATCCATTTACTTACCGCCTTCTTGAACAAGAGCCGATCGAATCTGAGGGA GGAAAAGTATACATTGCAGATTCGACAAACTTCAAAGTGTCTAAAACCATCGCATCAGCG CTCGTAACAGTAGAACCCGGCGCCATGAGAGAACTGCACTGGCACCCGAATACCCACGAA TGGCAATACTACATCTCCGGTAAAGCTAGAATGACCGTTTTTGCATCTGACGGCCATGCC AGAACGTTTAATTACCAAGCCGGTGATGTCGGATATGTACCATTTGCAATGGGTCATTAC GTTGAAAACATCGGGGATGAACCGCTTGTCTTTTTAGAAATCTTCAAAGACGACCATTAT GCTGATGTATCTTTAAACCAATGGCTTGCCATGCTTCCTGAAACATTTGTTCAAGCGCAC CTTGACTTGGGCAAAGACTTTACTGATGTGCTTTCAAAAGAAAAGCACCCAGTAGTGAAA AAGAAATGCAGTAAATAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID O34714 UniProtKB Entry Name OXDC_BACSU GenBank Gene ID AJ223978 - General References
- Wipat A, Brignell SC, Guy BJ, Rose M, Emmerson PT, Harwood CR: The yvsA-yvqA (293 degrees-289 degrees) region of the Bacillus subtilis chromosome containing genes involved in metal ion uptake and a putative sigma factor. Microbiology. 1998 Jun;144 ( Pt 6):1593-600. [Article]
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- Tanner A, Bornemann S: Bacillus subtilis YvrK is an acid-induced oxalate decarboxylase. J Bacteriol. 2000 Sep;182(18):5271-3. [Article]
- Tanner A, Bowater L, Fairhurst SA, Bornemann S: Oxalate decarboxylase requires manganese and dioxygen for activity. Overexpression and characterization of Bacillus subtilis YvrK and YoaN. J Biol Chem. 2001 Nov 23;276(47):43627-34. Epub 2001 Aug 23. [Article]
- MacLellan SR, Wecke T, Helmann JD: A previously unidentified sigma factor and two accessory proteins regulate oxalate decarboxylase expression in Bacillus subtilis. Mol Microbiol. 2008 Aug;69(4):954-67. doi: 10.1111/j.1365-2958.2008.06331.x. Epub 2008 Jun 28. [Article]
- Anand R, Dorrestein PC, Kinsland C, Begley TP, Ealick SE: Structure of oxalate decarboxylase from Bacillus subtilis at 1.75 A resolution. Biochemistry. 2002 Jun 18;41(24):7659-69. [Article]