2YSW
Crystal Structure of the 3-dehydroquinate dehydratase from Aquifex aeolicus VF5
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003855 | molecular_function | 3-dehydroquinate dehydratase activity |
A | 0008652 | biological_process | amino acid biosynthetic process |
A | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
A | 0009423 | biological_process | chorismate biosynthetic process |
A | 0016829 | molecular_function | lyase activity |
A | 0046279 | biological_process | 3,4-dihydroxybenzoate biosynthetic process |
B | 0003855 | molecular_function | 3-dehydroquinate dehydratase activity |
B | 0008652 | biological_process | amino acid biosynthetic process |
B | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
B | 0009423 | biological_process | chorismate biosynthetic process |
B | 0016829 | molecular_function | lyase activity |
B | 0046279 | biological_process | 3,4-dihydroxybenzoate biosynthetic process |
C | 0003855 | molecular_function | 3-dehydroquinate dehydratase activity |
C | 0008652 | biological_process | amino acid biosynthetic process |
C | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
C | 0009423 | biological_process | chorismate biosynthetic process |
C | 0016829 | molecular_function | lyase activity |
C | 0046279 | biological_process | 3,4-dihydroxybenzoate biosynthetic process |
Functional Information from PROSITE/UniProt
site_id | PS01028 |
Number of Residues | 30 |
Details | DEHYDROQUINASE_I Dehydroquinase class I active site. DIELssrgllvklynitkeagkk.LIiSYHN |
Chain | Residue | Details |
A | ASP88-ASN117 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:23396056 |
Chain | Residue | Details |
A | HIS116 | |
B | HIS116 | |
C | HIS116 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | ACT_SITE: Schiff-base intermediate with substrate => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:23396056 |
Chain | Residue | Details |
A | LYS142 | |
B | LYS142 | |
C | LYS142 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00214 |
Chain | Residue | Details |
A | GLU28 | |
A | GLN203 | |
B | GLU28 | |
B | GLN203 | |
C | GLU28 | |
C | GLN203 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:23396056 |
Chain | Residue | Details |
A | ARG61 | |
A | ARG180 | |
B | ARG61 | |
B | ARG180 | |
C | ARG61 | |
C | ARG180 |