Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004151 | molecular_function | dihydroorotase activity |
| A | 0004152 | molecular_function | dihydroorotate dehydrogenase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005743 | cellular_component | mitochondrial inner membrane |
| A | 0005829 | cellular_component | cytosol |
| A | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| A | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| A | 0006225 | biological_process | UDP biosynthetic process |
| A | 0009220 | biological_process | pyrimidine ribonucleotide biosynthetic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| A | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| A | 0106430 | molecular_function | dihydroorotate dehydrogenase (quinone) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE FMN A 398 |
| Chain | Residue |
| A | ALA95 |
| A | ASN212 |
| A | LYS255 |
| A | THR283 |
| A | ASN284 |
| A | THR285 |
| A | SER305 |
| A | GLY306 |
| A | LEU309 |
| A | GLY334 |
| A | GLY335 |
| A | ALA96 |
| A | LEU355 |
| A | TYR356 |
| A | THR357 |
| A | HOH633 |
| A | HOH653 |
| A | GLY97 |
| A | LYS100 |
| A | GLY119 |
| A | SER120 |
| A | ASN145 |
| A | TYR147 |
| A | ASN181 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ORO A 399 |
| Chain | Residue |
| A | LYS100 |
| A | ASN145 |
| A | TYR147 |
| A | GLY148 |
| A | PHE149 |
| A | ASN212 |
| A | SER215 |
| A | ASN284 |
| A | THR285 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 238 A 400 |
| Chain | Residue |
| A | TYR38 |
| A | MET43 |
| A | GLN47 |
| A | PRO52 |
| A | ALA55 |
| A | HIS56 |
| A | ALA59 |
| A | THR63 |
| A | LEU67 |
| A | LEU68 |
| A | ARG136 |
| A | TYR356 |
| A | THR360 |
| A | PRO364 |
| A | HOH713 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE DDQ A 630 |
| Chain | Residue |
| A | MET30 |
| A | ALA31 |
| A | THR32 |
| A | LEU58 |
| A | PHE62 |
| A | LEU67 |
| A | LEU68 |
Functional Information from PROSITE/UniProt
| site_id | PS00911 |
| Number of Residues | 20 |
| Details | DHODEHASE_1 Dihydroorotate dehydrogenase signature 1. GfveiGSVTpkpQeGNprPR |
| Chain | Residue | Details |
| A | GLY114-ARG133 | |
| site_id | PS00912 |
| Number of Residues | 21 |
| Details | DHODEHASE_2 Dihydroorotate dehydrogenase signature 2. IIGvGGVsSgqdAleKIrAGA |
| Chain | Residue | Details |
| A | ILE330-ALA350 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10673429","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16480261","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1h7x |
| Chain | Residue | Details |
| A | SER215 | |
| A | PHE149 | |
| A | LYS255 | |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1h7x |
| Chain | Residue | Details |
| A | SER215 | |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 109 |
| Chain | Residue | Details |
| A | ASN145 | electrostatic stabiliser |
| A | PHE149 | activator, electrostatic stabiliser, enhance reactivity, polar/non-polar interaction |
| A | SER215 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar/non-polar interaction, proton acceptor, proton donor, proton relay |
| A | LYS255 | electrostatic stabiliser, hydrogen bond donor |
| A | ASN284 | electrostatic stabiliser |
