Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004590 | molecular_function | orotidine-5'-phosphate decarboxylase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| A | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| B | 0004590 | molecular_function | orotidine-5'-phosphate decarboxylase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| B | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016831 | molecular_function | carboxy-lyase activity |
| B | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE BMP A 301 |
| Chain | Residue |
| A | ASP20 |
| A | ARG203 |
| A | HOH402 |
| A | HOH403 |
| A | HOH406 |
| A | HOH407 |
| A | HOH408 |
| A | HOH411 |
| A | HOH461 |
| B | ASP75 |
| B | ILE76 |
| A | LYS42 |
| B | THR79 |
| A | ASP70 |
| A | LYS72 |
| A | MET126 |
| A | SER127 |
| A | PRO180 |
| A | GLN185 |
| A | GLY202 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE 6CN A 303 |
| Chain | Residue |
| A | ASP20 |
| A | LYS42 |
| A | ASP70 |
| A | LYS72 |
| A | ILE96 |
| A | MET126 |
| A | SER127 |
| A | PRO180 |
| A | GLN185 |
| A | GLY202 |
| A | ARG203 |
| A | HOH402 |
| A | HOH403 |
| A | HOH406 |
| A | HOH407 |
| A | HOH408 |
| A | HOH411 |
| A | HOH461 |
| B | ASP75 |
| B | ILE76 |
| B | THR79 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 311 |
| Chain | Residue |
| A | GLU33 |
| A | ASN210 |
| A | HOH522 |
| A | HOH528 |
| A | HOH717 |
| B | THR159 |
| B | PRO161 |
| B | GLY186 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 312 |
| Chain | Residue |
| A | THR159 |
| A | PRO161 |
| A | GLY186 |
| B | ASN210 |
| B | HOH519 |
| B | HOH530 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 314 |
| Chain | Residue |
| A | ALA208 |
| A | ASP209 |
| A | ASN210 |
| A | ALA213 |
| A | ALA214 |
| A | HOH565 |
| B | GLU162 |
| site_id | AC6 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE BMP B 302 |
| Chain | Residue |
| A | ASP75 |
| A | ILE76 |
| A | THR79 |
| B | ASP20 |
| B | LYS42 |
| B | ASP70 |
| B | LYS72 |
| B | MET126 |
| B | SER127 |
| B | PRO180 |
| B | GLN185 |
| B | GLY202 |
| B | ARG203 |
| B | HOH422 |
| B | HOH423 |
| B | HOH426 |
| B | HOH427 |
| B | HOH428 |
| B | HOH431 |
| B | HOH462 |
| site_id | AC7 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE 6CN B 304 |
| Chain | Residue |
| B | HOH427 |
| B | HOH428 |
| B | HOH431 |
| B | HOH462 |
| A | ASP75 |
| A | ILE76 |
| A | THR79 |
| B | ASP20 |
| B | LYS42 |
| B | ASP70 |
| B | LYS72 |
| B | ILE96 |
| B | MET126 |
| B | SER127 |
| B | PRO180 |
| B | GLN185 |
| B | GLY202 |
| B | ARG203 |
| B | HOH422 |
| B | HOH423 |
| B | HOH426 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 313 |
| Chain | Residue |
| A | GLU162 |
| B | ALA208 |
| B | ASP209 |
| B | ASN210 |
| B | ALA213 |
| B | ALA214 |
Functional Information from PROSITE/UniProt
| site_id | PS00156 |
| Number of Residues | 14 |
| Details | OMPDECASE Orotidine 5'-phosphate decarboxylase active site. IIaDfKvaDIPeTN |
| Chain | Residue | Details |
| A | ILE67-ASN80 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor |
| Chain | Residue | Details |
| A | LYS72 | |
| B | LYS72 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP20 | |
| B | ASP70 | |
| B | SER127 | |
| B | PRO180 | |
| B | GLY202 | |
| B | ARG203 | |
| A | LYS42 | |
| A | ASP70 | |
| A | SER127 | |
| A | PRO180 | |
| A | GLY202 | |
| A | ARG203 | |
| B | ASP20 | |
| B | LYS42 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dbt |
| Chain | Residue | Details |
| A | LYS72 | |
| A | ASP70 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dbt |
| Chain | Residue | Details |
| B | LYS72 | |
| B | ASP70 | |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1dbt |
| Chain | Residue | Details |
| A | LYS42 | |
| A | ASP75 | |
| A | LYS72 | |
| A | ASP70 | |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1dbt |
| Chain | Residue | Details |
| B | LYS42 | |
| B | ASP75 | |
| B | LYS72 | |
| B | ASP70 | |
