1EA0
Alpha subunit of A. brasilense glutamate synthase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004355 | molecular_function | glutamate synthase (NADPH) activity |
| A | 0006537 | biological_process | glutamate biosynthetic process |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0015930 | molecular_function | glutamate synthase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016638 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors |
| A | 0019676 | biological_process | ammonia assimilation cycle |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
| A | 0097054 | biological_process | L-glutamate biosynthetic process |
| B | 0004355 | molecular_function | glutamate synthase (NADPH) activity |
| B | 0006537 | biological_process | glutamate biosynthetic process |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0015930 | molecular_function | glutamate synthase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016638 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors |
| B | 0019676 | biological_process | ammonia assimilation cycle |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
| B | 0097054 | biological_process | L-glutamate biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE OMT A 2473 |
| Chain | Residue |
| A | CYS1 |
| A | ARG210 |
| A | TYR211 |
| A | GLN223 |
| A | ASN231 |
| A | GLY232 |
| A | GLU233 |
| A | ASP273 |
| A | SER274 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE FMN A 2474 |
| Chain | Residue |
| A | PRO856 |
| A | GLY857 |
| A | MET858 |
| A | SER859 |
| A | GLY885 |
| A | GLU886 |
| A | GLN909 |
| A | LYS931 |
| A | LYS999 |
| A | GLY1028 |
| A | GLY1029 |
| A | THR1030 |
| A | GLY1031 |
| A | ASP1070 |
| A | GLY1071 |
| A | GLY1072 |
| A | GLY1093 |
| A | THR1094 |
| A | AKG2475 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE AKG A 2475 |
| Chain | Residue |
| A | SER859 |
| A | GLN934 |
| A | LYS937 |
| A | GLY942 |
| A | GLN943 |
| A | ARG957 |
| A | THR1030 |
| A | GLY1031 |
| A | FMN2474 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE F3S A 2476 |
| Chain | Residue |
| A | CYS1102 |
| A | ILE1103 |
| A | MET1104 |
| A | VAL1105 |
| A | ARG1106 |
| A | GLN1107 |
| A | CYS1108 |
| A | CYS1113 |
| A | VAL1117 |
| A | CYS1118 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE OMT B 2473 |
| Chain | Residue |
| B | CYS1 |
| B | GLN209 |
| B | ARG210 |
| B | TYR211 |
| B | GLN223 |
| B | ASN231 |
| B | GLY232 |
| B | GLU233 |
| B | ASP273 |
| B | SER274 |
| site_id | AC6 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE FMN B 2474 |
| Chain | Residue |
| B | PRO856 |
| B | GLY857 |
| B | MET858 |
| B | SER859 |
| B | GLU886 |
| B | GLN909 |
| B | LYS931 |
| B | LYS999 |
| B | GLY1028 |
| B | GLY1029 |
| B | THR1030 |
| B | GLY1031 |
| B | ASP1070 |
| B | GLY1071 |
| B | GLY1072 |
| B | GLY1093 |
| B | THR1094 |
| B | AKG2475 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE AKG B 2475 |
| Chain | Residue |
| B | SER859 |
| B | GLN934 |
| B | LYS937 |
| B | GLY942 |
| B | GLN943 |
| B | ARG957 |
| B | THR1030 |
| B | GLY1031 |
| B | ALA1032 |
| B | FMN2474 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE F3S B 2476 |
| Chain | Residue |
| B | CYS1102 |
| B | ILE1103 |
| B | MET1104 |
| B | VAL1105 |
| B | ARG1106 |
| B | GLN1107 |
| B | CYS1108 |
| B | CYS1113 |
| B | VAL1117 |
| B | CYS1118 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 42 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"For GATase activity","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 232 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1jxa |
| Chain | Residue | Details |
| A | VAL661 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1jxa |
| Chain | Residue | Details |
| B | VAL661 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1jxa |
| Chain | Residue | Details |
| A | LYS937 | |
| A | GLU886 | |
| A | CYS1 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1jxa |
| Chain | Residue | Details |
| B | LYS937 | |
| B | GLU886 | |
| B | CYS1 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 304 |
| Chain | Residue | Details |
| A | CYS1 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | ASN231 | electrostatic stabiliser, hydrogen bond donor |
| A | GLY232 | electrostatic stabiliser, hydrogen bond donor |
| A | MET479 | single electron acceptor, single electron donor, single electron relay |
| A | GLU886 | proton acceptor, proton donor, proton relay |
| A | LYS937 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 304 |
| Chain | Residue | Details |
| B | CYS1 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | ASN231 | electrostatic stabiliser, hydrogen bond donor |
| B | GLY232 | electrostatic stabiliser, hydrogen bond donor |
| B | MET479 | single electron acceptor, single electron donor, single electron relay |
| B | GLU886 | proton acceptor, proton donor, proton relay |
| B | LYS937 | electrostatic stabiliser |
