4A0F
Structure of selenomethionine substituted bifunctional DAPA aminotransferase-dethiobiotin synthetase from Arabidopsis thaliana in its apo form.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
| A | 0004141 | molecular_function | dethiobiotin synthase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009102 | biological_process | biotin biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016874 | molecular_function | ligase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
| B | 0004141 | molecular_function | dethiobiotin synthase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009102 | biological_process | biotin biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016874 | molecular_function | ligase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP A 1644 |
| Chain | Residue |
| A | ASN430 |
| A | LYS644 |
| A | HOH2050 |
| B | HIS679 |
| B | SER680 |
| A | GLY431 |
| A | SER432 |
| A | TYR473 |
| A | HIS474 |
| A | GLU581 |
| A | ASP615 |
| A | VAL617 |
| A | PHE618 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP B 1644 |
| Chain | Residue |
| A | HIS679 |
| A | SER680 |
| B | ASN430 |
| B | GLY431 |
| B | SER432 |
| B | TYR473 |
| B | HIS474 |
| B | GLU581 |
| B | ASP615 |
| B | VAL617 |
| B | PHE618 |
| B | LYS644 |
| B | HOH2010 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1809 |
| Chain | Residue |
| A | THR24 |
| A | LYS28 |
| A | LYS55 |
| A | GLY191 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1809 |
| Chain | Residue |
| B | THR24 |
| B | LYS28 |
| B | LYS55 |
| B | ASP66 |
| B | ALA190 |
| B | GLY191 |
| B | SO41810 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1810 |
| Chain | Residue |
| B | SER25 |
| B | LEU26 |
| B | GLY27 |
| B | LYS28 |
| B | THR29 |
| B | SO41809 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1810 |
| Chain | Residue |
| A | GLY223 |
| A | GLY224 |
| A | ILE225 |
| A | SER226 |
| B | SER143 |
| B | SER195 |
| B | PRO196 |
Functional Information from PROSITE/UniProt
| site_id | PS00600 |
| Number of Residues | 38 |
| Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. VIfDEVft.GFwRlGvetttellgckp....DIAcfAKlltGG |
| Chain | Residue | Details |
| A | VAL612-GLY649 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P13000","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22547782","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4A0G","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22547782","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4A0R","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22547782","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4A0H","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22547782","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4A0G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4A0H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4A0R","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Site: {"description":"Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAM","evidences":[{"source":"UniProtKB","id":"P12995","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"22547782","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4A0F","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4A0G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4A0H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4A0R","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
