Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008710 | molecular_function | 8-amino-7-oxononanoate synthase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0009102 | biological_process | biotin biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE LLF A 436 |
| Chain | Residue |
| A | ASN47 |
| A | ASP204 |
| A | ALA206 |
| A | HIS207 |
| A | LYS236 |
| A | TYR264 |
| A | SER265 |
| A | THR266 |
| A | HOH444 |
| A | HOH507 |
| A | HOH565 |
| A | GLY75 |
| A | HOH633 |
| A | SER107 |
| A | GLY108 |
| A | PHE109 |
| A | HIS133 |
| A | SER135 |
| A | GLU175 |
| A | SER179 |
Functional Information from PROSITE/UniProt
| site_id | PS00599 |
| Number of Residues | 10 |
| Details | AA_TRANSFER_CLASS_2 Aminotransferases class-II pyridoxal-phosphate attachment site. TFGKGFGVSG |
| Chain | Residue | Details |
| A | THR233-GLY242 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10642176","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10642176","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16557306","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"10642176","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16557306","evidenceCode":"ECO:0000269"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| A | ASP204 | |
| A | GLU175 | |
| A | LYS236 | |
| A | HIS133 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| A | HIS207 | |
| A | PHE238 | |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| A | HIS207 | |
| A | LYS236 | |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 430 |
| Chain | Residue | Details |
| A | ASN47 | electrostatic stabiliser |
| A | HIS133 | electrostatic stabiliser, proton shuttle (general acid/base) |
| A | GLU175 | electrostatic stabiliser |
| A | SER179 | modifies pKa |
| A | ASP204 | electrostatic stabiliser |
| A | HIS207 | electrostatic stabiliser, proton shuttle (general acid/base) |
| A | LYS236 | covalent catalysis, proton shuttle (general acid/base) |
