IED ID | IndEnz0002005360 |
Enzyme Type ID | protease005360 |
Protein Name |
Oxamate amidohydrolase proenzyme EC 3.5.1.126 Cleaved into: Oxamate amidohydrolase large chain Oxamate amidohydrolase alpha chain ; Oxamate amidohydrolase small chain Oxamate amidohydrolase beta chain |
Gene Name | hpxW KPN_01768 |
Organism | Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Klebsiella Klebsiella pneumoniae Klebsiella pneumoniae subsp. pneumoniae Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578) |
Enzyme Sequence | MHSSNVSTHGMAVAPHHLASQSALAILREGGSAIEAMVAAAAAIAVVYPHMNGLGGDGFWLIVPPEGDPIAIDASGAAGSLATLEAYAGQRHIPNRGPQAALTVAGTVSGWVEALRISRDLTGRALPVARLLADAIGYAEDGIPVTASQAHATASKLEELRHQPGFSETWLVAGEAPRPGSRFRQPALAGTLRMLASDGLDSFYRGPLAERLAQGMAALGMPITLGDLQAHRARRPGPLTLQHQQGTLWNLAPPTQGLVSLAILGITDRLKMADADDAQTVHRIVEATKRAFALRDAHITDPRHLDVDVQQLLTPEALQPLADSIDDASASPWGGGKGPGDTVWMGVVDNSGLAVSFIQSIYHEFGSGVVLPDTGIVWQNRGAAFSLDPQHLLALAPGKQPFHTLNPAAARLNDGRVMVYGSMGGDGQPQTQAALFTRYILQGVPLQESISRPRWLLGRTWGQSSDSLKLEGRFAPACIARLRELGHDVEVLADFSEAMGHAGAIVRHPNGLLEGATDPRSNGAAAGY |
Enzyme Length | 528 |
Uniprot Accession Number | A6T9C8 |
Absorption | |
Active Site | ACT_SITE 342; /note=Nucleophile; /evidence=ECO:0000305|PubMed:27303801 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=H2O + oxamate = NH4(+) + oxalate; Xref=Rhea:RHEA:51512, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:30623, ChEBI:CHEBI:58363; EC=3.5.1.126; Evidence={ECO:0000269|PubMed:27303801}; |
DNA Binding | |
EC Number | 3.5.1.126 |
Enzyme Function | FUNCTION: Involved in the uric acid degradation pathway. Catalyzes the conversion of oxamate to oxalate. {ECO:0000269|PubMed:27303801}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Beta strand (15); Chain (2); Helix (19); Mutagenesis (2); Region (1); Site (1); Turn (6) |
Keywords | 3D-structure;Hydrolase;Protease;Reference proteome;Zymogen |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | PTM: Cleaved by autocatalysis into a large (alpha) and a small (beta) subunit. {ECO:0000269|PubMed:27303801}. |
Signal Peptide | |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 5HFT; |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 55,542 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=kcat is 5.5 sec(-1) with oxamate as substrate. {ECO:0000269|PubMed:27303801}; |
Metal Binding | |
Rhea ID | RHEA:51512 |
Cross Reference Brenda | 3.5.1.126; |