1R9G
Three-dimensional Structure of YaaE 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 | 0006543 | biological_process | L-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 | 0006543 | biological_process | L-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 | Active site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_01615","evidenceCode":"ECO:0000255"},{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"HAMAP-Rule","id":"MF_01615","evidenceCode":"ECO:0000255"},{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01615","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17159152","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
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 |
