Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0006779 | biological_process | porphyrin-containing compound biosynthetic process |
A | 0006782 | biological_process | protoporphyrinogen IX biosynthetic process |
A | 0008483 | molecular_function | transaminase activity |
A | 0016853 | molecular_function | isomerase activity |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
A | 0033014 | biological_process | tetrapyrrole biosynthetic process |
A | 0042286 | molecular_function | glutamate-1-semialdehyde 2,1-aminomutase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE PMP A 501 |
Chain | Residue |
A | SER120 |
A | VAL246 |
A | LYS271 |
A | GLY302 |
A | THR303 |
A | PHE304 |
A | HOH520 |
A | HOH551 |
A | HOH602 |
A | HOH714 |
A | HOH749 |
A | GLY121 |
A | THR122 |
A | TYR148 |
A | HIS149 |
A | GLU210 |
A | ASN215 |
A | ASP243 |
A | VAL245 |
Functional Information from PROSITE/UniProt
site_id | PS00600 |
Number of Residues | 37 |
Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIlDEVvt.GF.RlGlegaqgyfnieg....DIIvlGKiigGG |
Chain | Residue | Details |
A | LEU240-GLY276 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250 |
Chain | Residue | Details |
A | LYS271 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
A | ASP243 | |
A | TYR148 | |
A | LYS271 | |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
A | ASP243 | |