| IED ID | IndEnz0018000445 |
| Enzyme Type ID | peroxidase000445 |
| Protein Name |
Methylamine utilization protein MauG EC 1.-.-.- |
| Gene Name | mauG Pden_4736 |
| Organism | Paracoccus denitrificans (strain Pd 1222) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Alphaproteobacteria Rhodobacterales Rhodobacteraceae Paracoccus Paracoccus denitrificans Paracoccus denitrificans (strain Pd 1222) |
| Enzyme Sequence | MLRLACLAPLAILIPAAGTAEQARPADDALAALGAQLFVDPALSRNATQSCATCHDPARAFTDPREGKAGLAVSVGDDGQSHGDRNTPTLGYAALVPAFHRDANGKYKGGQFWDGRADDLKQQAGQPMLNPVEMAMPDRAAVAARLRDDPAYRTGFEALFGKGVLDDPERAFDAAAEALAAYQATGEFSPFDSKYDRVMRGEEKFTPLEEFGYTVFITWNCRLCHMQRKQGVAERETFTNFEYHNIGLPVNETAREASGLGADHVDHGLLARPGIEDPAQSGRFKVPSLRNVAVTGPYMHNGVFTDLRTAILFYNKYTSRRPEAKINPETGAPWGEPEVARNLSLAELQSGLMLDDGRVDALVAFLETLTDRRYEPLLEESRAAQKD |
| Enzyme Length | 387 |
| Uniprot Accession Number | Q51658 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 51; /note=Heme c 1; covalent; /evidence=ECO:0000255|PROSITE-ProRule:PRU00433; BINDING 54; /note=Heme c 1; covalent; /evidence=ECO:0000255|PROSITE-ProRule:PRU00433; BINDING 221; /note=Heme c 2; covalent; /evidence=ECO:0000255|PROSITE-ProRule:PRU00433; BINDING 224; /note=Heme c 2; covalent; /evidence=ECO:0000255|PROSITE-ProRule:PRU00433 |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 1.-.-.- |
| Enzyme Function | FUNCTION: Involved in methylamine metabolism. Essential for the maturation of the beta subunit of MADH, presumably via a step in the biosynthesis of tryptophan tryptophylquinone (TTQ), the cofactor of MADH. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: One-carbon metabolism; methylamine degradation. |
| nucleotide Binding | |
| Features | Beta strand (9); Binding site (4); Chain (1); Helix (24); Metal binding (3); Signal peptide (1); Turn (2) |
| Keywords | 3D-structure;Electron transport;Heme;Iron;Metal-binding;Oxidoreductase;Periplasm;Plasmid;Reference proteome;Signal;Transport |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Periplasm. |
| Modified Residue | |
| Post Translational Modification | PTM: Binds 2 heme c groups covalently per subunit. {ECO:0000305}. |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (28) |
| Cross Reference PDB | 3L4M; 3L4O; 3ORV; 3PXS; 3PXT; 3PXW; 3RLM; 3RMZ; 3RN0; 3RN1; 3SJL; 3SLE; 3SVW; 3SWS; 3SXT; 4FA1; 4FA4; 4FA5; 4FA9; 4FAN; 4FAV; 4FB1; 4K3I; 4L1Q; 4L3G; 4L3H; 4O1Q; 4Y5R; |
| Mapped Pubmed ID | 20223990; 20929212; 21355604; 21969534; 22299652; 23487750; 23669364; 23832199; 23952537; 24517455; 25896561; |
| Motif | |
| Gene Encoded By | Plasmid pPD1222 |
| Mass | 42,230 |
| Kinetics | |
| Metal Binding | METAL 55; /note=Iron (heme c 1 axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00433; METAL 225; /note=Iron (heme c 2 axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00433; METAL 300; /note=Iron (heme c 1 axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00433 |
| Rhea ID | |
| Cross Reference Brenda | 1.4.9.1; |