4OBV
Ruminococcus gnavus tryptophan decarboxylase RUMGNA_01526 (alpha-FMT)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004058 | molecular_function | aromatic-L-amino-acid decarboxylase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0006568 | biological_process | L-tryptophan metabolic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016830 | molecular_function | carbon-carbon lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0019752 | biological_process | carboxylic acid metabolic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0036469 | molecular_function | L-tryptophan decarboxylase activity |
| B | 0004058 | molecular_function | aromatic-L-amino-acid decarboxylase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0006568 | biological_process | L-tryptophan metabolic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016830 | molecular_function | carbon-carbon lyase activity |
| B | 0016831 | molecular_function | carboxy-lyase activity |
| B | 0019752 | biological_process | carboxylic acid metabolic process |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0036469 | molecular_function | L-tryptophan decarboxylase activity |
| C | 0004058 | molecular_function | aromatic-L-amino-acid decarboxylase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006520 | biological_process | amino acid metabolic process |
| C | 0006568 | biological_process | L-tryptophan metabolic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016830 | molecular_function | carbon-carbon lyase activity |
| C | 0016831 | molecular_function | carboxy-lyase activity |
| C | 0019752 | biological_process | carboxylic acid metabolic process |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0036469 | molecular_function | L-tryptophan decarboxylase activity |
| D | 0004058 | molecular_function | aromatic-L-amino-acid decarboxylase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006520 | biological_process | amino acid metabolic process |
| D | 0006568 | biological_process | L-tryptophan metabolic process |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016830 | molecular_function | carbon-carbon lyase activity |
| D | 0016831 | molecular_function | carboxy-lyase activity |
| D | 0019752 | biological_process | carboxylic acid metabolic process |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0036469 | molecular_function | L-tryptophan decarboxylase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 2SU D 501 |
| Chain | Residue |
| B | ILE19 |
| D | LYS40 |
| D | PRO102 |
| D | ALA103 |
| D | SER104 |
| D | SER105 |
| D | PHE309 |
| D | PRO462 |
| D | GLU463 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 3SO D 502 |
| Chain | Residue |
| B | HIS120 |
| B | LEU336 |
| B | TRP349 |
| B | THR356 |
| D | VAL99 |
| D | GLY159 |
| D | SER160 |
| D | HIS192 |
| D | SER194 |
| D | THR249 |
| D | ASP274 |
| D | ALA276 |
| D | ASP303 |
| D | HIS305 |
| D | LYS306 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE 2SU C 501 |
| Chain | Residue |
| A | ILE19 |
| C | PRO102 |
| C | ALA103 |
| C | SER104 |
| C | SER105 |
| C | PHE309 |
| C | PRO462 |
| C | GLU463 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE 2SU B 501 |
| Chain | Residue |
| B | PRO102 |
| B | ALA103 |
| B | SER105 |
| B | PHE309 |
| B | PRO462 |
| B | GLU463 |
| D | ILE19 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 3SO B 502 |
| Chain | Residue |
| B | PHE98 |
| B | VAL99 |
| B | GLY159 |
| B | SER160 |
| B | HIS192 |
| B | SER194 |
| B | THR249 |
| B | ASP274 |
| B | ALA276 |
| B | ASP303 |
| B | LYS306 |
| D | HIS120 |
| D | TRP349 |
| D | THR356 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 3SO A 501 |
| Chain | Residue |
| A | HIS120 |
| A | TRP349 |
| A | THR356 |
| C | PHE98 |
| C | VAL99 |
| C | GLY159 |
| C | SER160 |
| C | HIS192 |
| C | SER194 |
| C | THR249 |
| C | ASP274 |
| C | ALA276 |
| C | ASP303 |
| C | LYS306 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE 2SU A 502 |
| Chain | Residue |
| A | PRO102 |
| A | ALA103 |
| A | SER104 |
| A | SER105 |
| A | PHE309 |
| A | PRO462 |
| A | GLU463 |
| site_id | AC8 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE 3SO A 503 |
| Chain | Residue |
| A | PHE98 |
| A | VAL99 |
| A | GLY159 |
| A | SER160 |
| A | HIS192 |
| A | THR249 |
| A | ASP274 |
| A | ALA276 |
| A | ASP303 |
| A | HIS305 |
| A | LYS306 |
| C | HIS120 |
| C | LEU336 |
| C | LEU339 |
| C | TRP349 |
| C | THR356 |
Functional Information from PROSITE/UniProt
| site_id | PS00392 |
| Number of Residues | 22 |
| Details | DDC_GAD_HDC_YDC DDC / GAD / HDC / TyrDC pyridoxal-phosphate attachment site. SIsWdahKWLfQtYGCamVLvK |
| Chain | Residue | Details |
| D | SER299-LYS320 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"25263219","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
