Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000032 | biological_process | cell wall mannoprotein biosynthetic process |
| A | 0004476 | molecular_function | mannose-6-phosphate isomerase activity |
| A | 0005575 | cellular_component | cellular_component |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009101 | biological_process | glycoprotein biosynthetic process |
| A | 0009298 | biological_process | GDP-mannose biosynthetic process |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0031505 | biological_process | fungal-type cell wall organization |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 501 |
| Chain | Residue |
| A | GLN111 |
| A | HIS113 |
| A | GLU138 |
| A | HIS285 |
| A | 9C2502 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | binding site for residue 9C2 A 502 |
| Chain | Residue |
| A | LEU108 |
| A | SER109 |
| A | GLN111 |
| A | HIS113 |
| A | LYS136 |
| A | GLU138 |
| A | HIS285 |
| A | TYR287 |
| A | GLU294 |
| A | ARG304 |
| A | LYS310 |
| A | ZN501 |
| A | HOH615 |
| A | HOH648 |
| A | HOH673 |
| A | HOH732 |
| A | TYR16 |
| A | TRP18 |
| A | GLU48 |
| A | LYS100 |
Functional Information from PROSITE/UniProt
| site_id | PS00965 |
| Number of Residues | 9 |
| Details | PMI_I_1 Phosphomannose isomerase type I signature 1. YpDdNHKPE |
| Chain | Residue | Details |
| A | TYR130-GLU138 | |
| site_id | PS00966 |
| Number of Residues | 26 |
| Details | PMI_I_2 Phosphomannose isomerase type I signature 2. HAYIsGdiIEcMAaSDNvVRAGfTPK |
| Chain | Residue | Details |
| A | HIS285-LYS310 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"8180205","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8612079","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Site: {"description":"Its modification inactivates the enzyme"} |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 8 |
| Details | M-CSA 880 |
| Chain | Residue | Details |
| A | SER109 | electrostatic stabiliser |
| A | GLN111 | activator, metal ligand |
| A | HIS113 | metal ligand |
| A | LYS136 | proton acceptor, proton donor |
| A | GLU138 | metal ligand, modifies pKa |
| A | HIS285 | metal ligand |
| A | ARG304 | electrostatic stabiliser |
| A | LYS310 | electrostatic stabiliser |
