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 | 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 | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
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 | |
