Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
twitter

MetaCyc Enzyme: oxalate decarboxylase

Gene: oxdC Accession Number: BSU33240

Synonyms: yvrK

Species: Bacillus subtilis

Subunit composition of oxalate decarboxylase = [OxdC]6
         oxalate decarboxylase monomer = OxdC

Summary:
Bacillus subtilis expresses a cytosolic oxalate decarboxylase that induced in acidic growth media, particularly at pH 5.0, but not by oxalate. The enzyme was purified, and N-terminal sequencing identified the protein to be encoded by the oxdC gene [Tanner00]. The enzyme preferred acidic conditions, and its pH activity profile yielded a bell-shaped curve with 70% activity at pH 3.0, a maximum at pH 5.0, and zero activity at pH 7.5.

The oxdC gene has been cloned and expressed in Escherichia coli, and the recombinant protein was only active after activation by manganese [Tanner01].

A mechanism for oxalate decarboxylation has been proposed, in which both Mn(II) and O2 are cofactors that act together as a two-electron sink during catalysis [Tanner01].

The structure of the enzyme has been determined at 1.75 Å resolution. The enzyme is a hexamer with 32-point symmetry in which each monomer belongs to the cupin family of proteins. It is classified as a bicupin because it contains two cupin folds. Each oxalate decarboxylase cupin domain contains one manganese binding site, and is structurally similar to oxalate oxidase, an enzyme that catalyzes manganese-dependent oxidative decarboxylation of oxalate to carbon dioxide and hydrogen peroxide [Anand02].

Map Position: [3,410,466 -> 3,411,623]

Molecular Weight of Polypeptide: 43.566 kD (from nucleotide sequence), 44.0 kD (experimental) [Tanner00 ]

Molecular Weight of Multimer: 220.0 kD (experimental) [Tanner00]

pI: 6.1 [Tanner00]

Unification Links: Entrez:2635821 , GenoList (SubtiList):BSU33240 , GOA:O34714 , Protein Model Portal:O34714 , SMR:O34714 , String:224308.BSU33240 , String:BSU33240 , SubtilisWiki:oxdC , SubtiWiki:oxdC , UniProt:O34714

Relationship Links: InterPro:IN-FAMILY:IPR006045 , InterPro:IN-FAMILY:IPR011051 , InterPro:IN-FAMILY:IPR014710 , InterPro:IN-FAMILY:IPR017774 , PDB:Structure:1J58 , PDB:Structure:1L3J , PDB:Structure:1UW8 , PDB:Structure:2UY8 , PDB:Structure:2UY9 , PDB:Structure:2UYA , PDB:Structure:2UYB , PDB:Structure:2V09 , PDB:Structure:3S0M , Pfam:IN-FAMILY:PF00190 , Smart:IN-FAMILY:SM00835

Gene-Reaction Schematic: ?

Credits:
Created 23-Jan-2011 by Caspi R , SRI International


Enzymatic reaction of: oxalate decarboxylase

EC Number: 4.1.1.2

oxalate + H+ <=> formate + CO2

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Reversibility of this reaction is unspecified.

In Pathways: oxalate degradation V

Cofactors or Prosthetic Groups: Mn2+ [Tanner01]

pH(opt): 5 [Tanner00]


References

Anand02: Anand R, Dorrestein PC, Kinsland C, Begley TP, Ealick SE (2002). "Structure of oxalate decarboxylase from Bacillus subtilis at 1.75 A resolution." Biochemistry 41(24);7659-69. PMID: 12056897

Tanner00: Tanner A, Bornemann S (2000). "Bacillus subtilis YvrK is an acid-induced oxalate decarboxylase." J Bacteriol 182(18);5271-3. PMID: 10960116

Tanner01: Tanner A, Bowater L, Fairhurst SA, Bornemann S (2001). "Oxalate decarboxylase requires manganese and dioxygen for activity. Overexpression and characterization of Bacillus subtilis YvrK and YoaN." J Biol Chem 276(47);43627-34. PMID: 11546787


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sat Nov 22, 2014, biocyc13.