2NV0
Structure of the glutaminase subunit Pdx2 (YaaE) of PLP synthase from Bacillus subtilis
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004359 | molecular_function | glutaminase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005829 | cellular_component | cytosol |
A | 0006541 | biological_process | glutamine metabolic process |
A | 0006543 | biological_process | glutamine catabolic process |
A | 0008614 | biological_process | pyridoxine metabolic process |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016829 | molecular_function | lyase activity |
A | 0036381 | molecular_function | pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity |
A | 0042802 | molecular_function | identical protein binding |
A | 0042819 | biological_process | vitamin B6 biosynthetic process |
A | 0042823 | biological_process | pyridoxal phosphate biosynthetic process |
A | 1903600 | cellular_component | glutaminase complex |
B | 0004359 | molecular_function | glutaminase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005829 | cellular_component | cytosol |
B | 0006541 | biological_process | glutamine metabolic process |
B | 0006543 | biological_process | glutamine catabolic process |
B | 0008614 | biological_process | pyridoxine metabolic process |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016829 | molecular_function | lyase activity |
B | 0036381 | molecular_function | pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity |
B | 0042802 | molecular_function | identical protein binding |
B | 0042819 | biological_process | vitamin B6 biosynthetic process |
B | 0042823 | biological_process | pyridoxal phosphate biosynthetic process |
B | 1903600 | cellular_component | glutaminase complex |
Functional Information from PROSITE/UniProt
site_id | PS01236 |
Number of Residues | 11 |
Details | PDXT_SNO_1 PdxT/SNO family family signature. GLILPGGESTT |
Chain | Residue | Details |
A | GLY41-THR51 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_01615, ECO:0000305 |
Chain | Residue | Details |
A | CYS79 | |
B | CYS79 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Charge relay system => ECO:0000255|HAMAP-Rule:MF_01615, ECO:0000305 |
Chain | Residue | Details |
A | HIS170 | |
A | GLU172 | |
B | HIS170 | |
B | GLU172 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01615, ECO:0000269|PubMed:17159152 |
Chain | Residue | Details |
A | GLY47 | |
A | ARG106 | |
A | ILE134 | |
B | GLY47 | |
B | ARG106 | |
B | ILE134 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1bxr |
Chain | Residue | Details |
A | GLU172 | |
A | HIS170 | |
A | CYS79 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1bxr |
Chain | Residue | Details |
B | GLU172 | |
B | HIS170 | |
B | CYS79 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1bxr |
Chain | Residue | Details |
A | HIS170 | |
A | CYS79 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1bxr |
Chain | Residue | Details |
B | HIS170 | |
B | CYS79 |