1H1C
Histidinol-phosphate aminotransferase (HisC) from Thermotoga maritima
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000105 | biological_process | L-histidine biosynthetic process |
| A | 0004400 | molecular_function | histidinol-phosphate transaminase activity |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| B | 0000105 | biological_process | L-histidine biosynthetic process |
| B | 0004400 | molecular_function | histidinol-phosphate transaminase activity |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| C | 0000105 | biological_process | L-histidine biosynthetic process |
| C | 0004400 | molecular_function | histidinol-phosphate transaminase activity |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0009058 | biological_process | biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0042803 | molecular_function | protein homodimerization activity |
| D | 0000105 | biological_process | L-histidine biosynthetic process |
| D | 0004400 | molecular_function | histidinol-phosphate transaminase activity |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0009058 | biological_process | biosynthetic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP A 1202 |
| Chain | Residue |
| A | GLY84 |
| A | THR199 |
| A | SER201 |
| A | LYS202 |
| A | ARG210 |
| B | TYR53 |
| A | ALA85 |
| A | ASP86 |
| A | TYR106 |
| A | PRO145 |
| A | ASN149 |
| A | ASP173 |
| A | ALA175 |
| A | TYR176 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PLP B 1202 |
| Chain | Residue |
| A | TYR53 |
| B | GLY84 |
| B | ALA85 |
| B | ASP86 |
| B | TYR106 |
| B | ASN149 |
| B | ASP173 |
| B | TYR176 |
| B | THR199 |
| B | SER201 |
| B | LYS202 |
| B | ARG210 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PLP C 1202 |
| Chain | Residue |
| C | GLY84 |
| C | ALA85 |
| C | ASP86 |
| C | TYR106 |
| C | ASN149 |
| C | ASP173 |
| C | TYR176 |
| C | THR199 |
| C | SER201 |
| C | LYS202 |
| C | ARG210 |
| D | TYR53 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP D 1202 |
| Chain | Residue |
| C | TYR53 |
| D | GLY84 |
| D | ALA85 |
| D | ASP86 |
| D | TYR106 |
| D | TYR109 |
| D | ASN149 |
| D | ASP173 |
| D | TYR176 |
| D | THR199 |
| D | SER201 |
| D | LYS202 |
| D | ARG210 |
Functional Information from PROSITE/UniProt
| site_id | PS00599 |
| Number of Residues | 10 |
| Details | AA_TRANSFER_CLASS_2 Aminotransferases class-II pyridoxal-phosphate attachment site. TFSKAFSLAA |
| Chain | Residue | Details |
| A | THR199-ALA208 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:15007066, ECO:0007744|PDB:1H1C |
| Chain | Residue | Details |
| A | LYS202 | |
| B | LYS202 | |
| C | LYS202 | |
| D | LYS202 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | TYR106 | |
| A | ASP173 | |
| A | LYS202 |
| site_id | CSA10 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | TYR106 | |
| A | ASP173 | |
| B | PRO57 |
| site_id | CSA11 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| C | PRO57 | |
| D | TYR106 | |
| D | ASP173 |
| site_id | CSA12 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| D | PRO57 | |
| C | TYR106 | |
| C | ASP173 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | TYR106 | |
| B | ASP173 | |
| B | LYS202 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| C | TYR106 | |
| C | ASP173 | |
| C | LYS202 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| D | TYR106 | |
| D | ASP173 | |
| D | LYS202 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | PHE102 | |
| A | ASP173 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | PHE102 | |
| B | ASP173 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| C | PHE102 | |
| C | ASP173 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| D | PHE102 | |
| D | ASP173 |
| site_id | CSA9 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | PRO57 | |
| B | TYR106 | |
| B | ASP173 |
