4A0R
Structure of bifunctional DAPA aminotransferase-DTB synthetase from Arabidopsis thaliana bound to dethiobiotin (DTB).
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| 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 | 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 | 0000287 | molecular_function | magnesium ion binding |
| 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 | 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 | 14 |
| Details | BINDING SITE FOR RESIDUE PLP A 1644 |
| Chain | Residue |
| A | ASN430 |
| A | PHE618 |
| A | LYS644 |
| A | HOH2053 |
| B | HIS679 |
| B | SER680 |
| A | GLY431 |
| A | SER432 |
| A | TYR473 |
| A | HIS474 |
| A | GLY475 |
| A | GLU581 |
| A | ASP615 |
| A | VAL617 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE TLA A 1810 |
| Chain | Residue |
| A | THR24 |
| A | SER25 |
| A | GLY27 |
| A | LYS28 |
| A | THR29 |
| A | LYS55 |
| A | ASP66 |
| A | GLU188 |
| A | THR189 |
| A | ALA190 |
| A | GLY191 |
| A | DTB1811 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE DTB A 1811 |
| Chain | Residue |
| A | THR24 |
| A | GLN58 |
| A | THR59 |
| A | SER143 |
| A | SER195 |
| A | TLA1810 |
| B | LEU222 |
| B | GLY223 |
| B | GLY224 |
| B | ILE225 |
| B | SER226 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP B 1644 |
| Chain | Residue |
| A | HIS679 |
| A | SER680 |
| A | HOH2051 |
| A | HOH2069 |
| B | ASN430 |
| B | GLY431 |
| B | SER432 |
| B | TYR473 |
| B | HIS474 |
| B | GLY475 |
| B | GLU581 |
| B | ASP615 |
| B | VAL617 |
| B | PHE618 |
| B | LYS644 |
| B | HOH2045 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE DTB B 1808 |
| Chain | Residue |
| A | LEU222 |
| A | GLY223 |
| A | GLY224 |
| A | ILE225 |
| B | THR24 |
| B | GLN58 |
| B | THR59 |
| B | SER195 |
| B | PRO196 |
| B | TLA1809 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE TLA B 1809 |
| Chain | Residue |
| B | THR24 |
| B | SER25 |
| B | LEU26 |
| B | GLY27 |
| B | LYS28 |
| B | THR29 |
| B | LYS55 |
| B | ASP66 |
| B | THR189 |
| B | ALA190 |
| B | GLY191 |
| B | DTB1808 |
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 | 10 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P13000 |
| Chain | Residue | Details |
| A | SER25 | |
| B | GLU523 | |
| A | ASP75 | |
| A | GLU248 | |
| A | PRO496 | |
| A | GLU523 | |
| B | SER25 | |
| B | ASP75 | |
| B | GLU248 | |
| B | PRO496 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22547782, ECO:0007744|PDB:4A0G |
| Chain | Residue | Details |
| A | THR29 | |
| A | ASP66 | |
| A | GLU188 | |
| B | THR29 | |
| B | ASP66 | |
| B | GLU188 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22547782, ECO:0007744|PDB:4A0R |
| Chain | Residue | Details |
| A | THR59 | |
| B | THR59 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22547782, ECO:0007744|PDB:4A0H |
| Chain | Residue | Details |
| A | TRP369 | |
| B | ARG775 | |
| A | TYR473 | |
| A | LYS644 | |
| A | GLY678 | |
| A | ARG775 | |
| B | TRP369 | |
| B | TYR473 | |
| B | LYS644 | |
| B | GLY678 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22547782, ECO:0007744|PDB:4A0G, ECO:0007744|PDB:4A0H, ECO:0007744|PDB:4A0R |
| Chain | Residue | Details |
| A | GLY431 | |
| A | ASP615 | |
| A | HIS679 | |
| B | GLY431 | |
| B | ASP615 | |
| B | HIS679 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | SITE: Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAM => ECO:0000250|UniProtKB:P12995 |
| Chain | Residue | Details |
| A | PHE326 | |
| B | PHE326 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:22547782, ECO:0007744|PDB:4A0F, ECO:0007744|PDB:4A0G, ECO:0007744|PDB:4A0H, ECO:0007744|PDB:4A0R |
| Chain | Residue | Details |
| A | LYS644 | |
| B | LYS644 |
