1C3C
T. MARITIMA ADENYLOSUCCINATE LYASE
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004018 | molecular_function | N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity |
A | 0005829 | cellular_component | cytosol |
A | 0006164 | biological_process | purine nucleotide biosynthetic process |
A | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
A | 0009152 | biological_process | purine ribonucleotide biosynthetic process |
A | 0009168 | biological_process | purine ribonucleoside monophosphate biosynthetic process |
A | 0016829 | molecular_function | lyase activity |
A | 0044208 | biological_process | 'de novo' AMP biosynthetic process |
A | 0070626 | molecular_function | (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity |
B | 0003824 | molecular_function | catalytic activity |
B | 0004018 | molecular_function | N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity |
B | 0005829 | cellular_component | cytosol |
B | 0006164 | biological_process | purine nucleotide biosynthetic process |
B | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
B | 0009152 | biological_process | purine ribonucleotide biosynthetic process |
B | 0009168 | biological_process | purine ribonucleoside monophosphate biosynthetic process |
B | 0016829 | molecular_function | lyase activity |
B | 0044208 | biological_process | 'de novo' AMP biosynthetic process |
B | 0070626 | molecular_function | (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity |
Functional Information from PROSITE/UniProt
site_id | PS00163 |
Number of Residues | 10 |
Details | FUMARATE_LYASES Fumarate lyases signature. GSsaMpHKkN |
Chain | Residue | Details |
A | GLY261-ASN270 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:10673438 |
Chain | Residue | Details |
A | HIS141 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P0AB89 |
Chain | Residue | Details |
A | SER262 |
site_id | SWS_FT_FI3 |
Number of Residues | 7 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P0AB89 |
Chain | Residue | Details |
A | ARG4 | |
A | ASN67 | |
A | THR93 | |
A | GLN212 | |
A | SER263 | |
A | LYS268 | |
A | SER307 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | a catalytic site defined by CSA, PubMed 10673438 |
Chain | Residue | Details |
A | THR140 | |
A | HIS141 | |
B | LYS268 | |
B | GLU275 |
site_id | CSA2 |
Number of Residues | 4 |
Details | a catalytic site defined by CSA, PubMed 10673438 |
Chain | Residue | Details |
A | LYS268 | |
A | GLU275 | |
B | THR140 | |
B | HIS141 |
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 80 |
Chain | Residue | Details |
A | HIS68 | electrostatic stabiliser |
A | THR140 | electrostatic stabiliser |
A | HIS141 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | SER263 | proton acceptor, proton donor |
A | LYS268 | electrostatic stabiliser |
A | GLU275 | activator, hydrogen bond acceptor, increase basicity |