4A0G
Structure of bifunctional DAPA aminotransferase-DTB 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 | 0008152 | biological_process | metabolic process |
| 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 | 0008152 | biological_process | metabolic process |
| 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 |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
| C | 0004141 | molecular_function | dethiobiotin synthase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0005759 | cellular_component | mitochondrial matrix |
| C | 0008152 | biological_process | metabolic process |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0009102 | biological_process | biotin biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016874 | molecular_function | ligase activity |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
| D | 0004141 | molecular_function | dethiobiotin synthase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0005759 | cellular_component | mitochondrial matrix |
| D | 0008152 | biological_process | metabolic process |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0009102 | biological_process | biotin biosynthetic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0016874 | molecular_function | ligase activity |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PLP A 1644 |
| Chain | Residue |
| A | ASN430 |
| A | PHE618 |
| A | LYS644 |
| A | HOH2136 |
| A | HOH2137 |
| A | HOH2159 |
| A | HOH2185 |
| 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 | 17 |
| Details | BINDING SITE FOR RESIDUE PLP B 1644 |
| Chain | Residue |
| A | HIS679 |
| A | SER680 |
| A | HOH2125 |
| A | HOH2164 |
| A | HOH2165 |
| A | HOH2166 |
| B | ASN430 |
| B | GLY431 |
| B | SER432 |
| B | TYR473 |
| B | HIS474 |
| B | GLU581 |
| B | ASP615 |
| B | VAL617 |
| B | PHE618 |
| B | LYS644 |
| B | HOH2098 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP C 1644 |
| Chain | Residue |
| C | ASN430 |
| C | GLY431 |
| C | SER432 |
| C | ILE435 |
| C | TYR473 |
| C | HIS474 |
| C | GLU581 |
| C | ASP615 |
| C | VAL617 |
| C | PHE618 |
| C | LYS644 |
| D | HIS679 |
| D | SER680 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP D 1644 |
| Chain | Residue |
| C | HIS679 |
| C | SER680 |
| D | ASN430 |
| D | GLY431 |
| D | SER432 |
| D | ILE435 |
| D | TYR473 |
| D | GLU581 |
| D | ASP615 |
| D | VAL617 |
| D | PHE618 |
| D | LYS644 |
| D | HOH2055 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1812 |
| Chain | Residue |
| A | THR24 |
| A | LYS28 |
| A | LYS55 |
| A | GLY191 |
| A | SO41814 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1812 |
| Chain | Residue |
| A | SER195 |
| A | PRO196 |
| B | GLY223 |
| B | GLY224 |
| B | ILE225 |
| B | SER226 |
| B | HOH2041 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1813 |
| Chain | Residue |
| A | GLY223 |
| A | GLY224 |
| A | ILE225 |
| A | SER226 |
| B | SER195 |
| B | PRO196 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1813 |
| Chain | Residue |
| B | LYS28 |
| B | LYS55 |
| B | ASP66 |
| B | GLU188 |
| B | ALA190 |
| B | GLY191 |
| B | MG1814 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 C 1807 |
| Chain | Residue |
| C | THR24 |
| C | LYS28 |
| C | LYS55 |
| C | ALA190 |
| C | GLY191 |
| C | SO41809 |
| C | HOH2005 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 D 1808 |
| Chain | Residue |
| C | SER143 |
| C | SER195 |
| C | PRO196 |
| D | GLY223 |
| D | GLY224 |
| D | ILE225 |
| D | SER226 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 C 1808 |
| Chain | Residue |
| C | GLY223 |
| C | GLY224 |
| C | ILE225 |
| C | SER226 |
| D | SER143 |
| D | SER195 |
| D | PRO196 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 D 1809 |
| Chain | Residue |
| D | THR24 |
| D | LYS28 |
| D | LYS55 |
| D | GLY191 |
| D | MG1810 |
| D | HOH2005 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1814 |
| Chain | Residue |
| A | SER25 |
| A | GLY27 |
| A | LYS28 |
| A | THR29 |
| A | SO41812 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 C 1809 |
| Chain | Residue |
| C | SER25 |
| C | LEU26 |
| C | GLY27 |
| C | LYS28 |
| C | THR29 |
| C | LEU30 |
| C | SO41807 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 1814 |
| Chain | Residue |
| B | LYS28 |
| B | THR29 |
| B | ASP66 |
| B | GLU188 |
| B | SO41813 |
| B | HOH2004 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 1810 |
| Chain | Residue |
| D | THR29 |
| D | ASP66 |
| D | GLU188 |
| D | SO41809 |
| D | HOH2005 |
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 | 20 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P13000 |
| Chain | Residue | Details |
| A | SER25 | |
| B | GLU523 | |
| C | SER25 | |
| C | ASP75 | |
| C | GLU248 | |
| C | PRO496 | |
| C | GLU523 | |
| D | SER25 | |
| D | ASP75 | |
| D | GLU248 | |
| D | PRO496 | |
| A | ASP75 | |
| D | GLU523 | |
| A | GLU248 | |
| A | PRO496 | |
| A | GLU523 | |
| B | SER25 | |
| B | ASP75 | |
| B | GLU248 | |
| B | PRO496 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22547782, ECO:0007744|PDB:4A0G |
| Chain | Residue | Details |
| A | THR29 | |
| D | THR29 | |
| D | ASP66 | |
| D | GLU188 | |
| A | ASP66 | |
| A | GLU188 | |
| B | THR29 | |
| B | ASP66 | |
| B | GLU188 | |
| C | THR29 | |
| C | ASP66 | |
| C | GLU188 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22547782, ECO:0007744|PDB:4A0R |
| Chain | Residue | Details |
| A | THR59 | |
| B | THR59 | |
| C | THR59 | |
| D | THR59 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22547782, ECO:0007744|PDB:4A0H |
| Chain | Residue | Details |
| A | TRP369 | |
| B | ARG775 | |
| C | TRP369 | |
| C | TYR473 | |
| C | LYS644 | |
| C | GLY678 | |
| C | ARG775 | |
| D | TRP369 | |
| D | TYR473 | |
| D | LYS644 | |
| D | GLY678 | |
| A | TYR473 | |
| D | ARG775 | |
| A | LYS644 | |
| A | GLY678 | |
| A | ARG775 | |
| B | TRP369 | |
| B | TYR473 | |
| B | LYS644 | |
| B | GLY678 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22547782, ECO:0007744|PDB:4A0G, ECO:0007744|PDB:4A0H, ECO:0007744|PDB:4A0R |
| Chain | Residue | Details |
| A | GLY431 | |
| D | GLY431 | |
| D | ASP615 | |
| D | HIS679 | |
| A | ASP615 | |
| A | HIS679 | |
| B | GLY431 | |
| B | ASP615 | |
| B | HIS679 | |
| C | GLY431 | |
| C | ASP615 | |
| C | HIS679 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| 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 | |
| C | PHE326 | |
| D | PHE326 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| 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 | |
| C | LYS644 | |
| D | LYS644 |
