Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
| A | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
| A | 0004354 | molecular_function | glutamate dehydrogenase (NADP+) activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005525 | molecular_function | GTP binding |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005743 | cellular_component | mitochondrial inner membrane |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0006538 | biological_process | L-glutamate catabolic process |
| A | 0006541 | biological_process | glutamine metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0072350 | biological_process | tricarboxylic acid metabolic process |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
| B | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
| B | 0004354 | molecular_function | glutamate dehydrogenase (NADP+) activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005525 | molecular_function | GTP binding |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005743 | cellular_component | mitochondrial inner membrane |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0006538 | biological_process | L-glutamate catabolic process |
| B | 0006541 | biological_process | glutamine metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0072350 | biological_process | tricarboxylic acid metabolic process |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
| C | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
| C | 0004354 | molecular_function | glutamate dehydrogenase (NADP+) activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005525 | molecular_function | GTP binding |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0005743 | cellular_component | mitochondrial inner membrane |
| C | 0005783 | cellular_component | endoplasmic reticulum |
| C | 0006520 | biological_process | amino acid metabolic process |
| C | 0006538 | biological_process | L-glutamate catabolic process |
| C | 0006541 | biological_process | glutamine metabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0072350 | biological_process | tricarboxylic acid metabolic process |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
| D | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
| D | 0004354 | molecular_function | glutamate dehydrogenase (NADP+) activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005525 | molecular_function | GTP binding |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0005743 | cellular_component | mitochondrial inner membrane |
| D | 0005783 | cellular_component | endoplasmic reticulum |
| D | 0006520 | biological_process | amino acid metabolic process |
| D | 0006538 | biological_process | L-glutamate catabolic process |
| D | 0006541 | biological_process | glutamine metabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0072350 | biological_process | tricarboxylic acid metabolic process |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
| E | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
| E | 0004354 | molecular_function | glutamate dehydrogenase (NADP+) activity |
| E | 0005524 | molecular_function | ATP binding |
| E | 0005525 | molecular_function | GTP binding |
| E | 0005739 | cellular_component | mitochondrion |
| E | 0005743 | cellular_component | mitochondrial inner membrane |
| E | 0005783 | cellular_component | endoplasmic reticulum |
| E | 0006520 | biological_process | amino acid metabolic process |
| E | 0006538 | biological_process | L-glutamate catabolic process |
| E | 0006541 | biological_process | glutamine metabolic process |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
| E | 0042802 | molecular_function | identical protein binding |
| E | 0072350 | biological_process | tricarboxylic acid metabolic process |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
| F | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
| F | 0004354 | molecular_function | glutamate dehydrogenase (NADP+) activity |
| F | 0005524 | molecular_function | ATP binding |
| F | 0005525 | molecular_function | GTP binding |
| F | 0005739 | cellular_component | mitochondrion |
| F | 0005743 | cellular_component | mitochondrial inner membrane |
| F | 0005783 | cellular_component | endoplasmic reticulum |
| F | 0006520 | biological_process | amino acid metabolic process |
| F | 0006538 | biological_process | L-glutamate catabolic process |
| F | 0006541 | biological_process | glutamine metabolic process |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
| F | 0042802 | molecular_function | identical protein binding |
| F | 0072350 | biological_process | tricarboxylic acid metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue GLU A 601 |
| Chain | Residue |
| A | LYS90 |
| A | ASN349 |
| A | GLY377 |
| A | VAL378 |
| A | SER381 |
| A | NAI603 |
| A | GLY91 |
| A | MET111 |
| A | LYS114 |
| A | LYS126 |
| A | ALA166 |
| A | PRO167 |
| A | ASP168 |
| A | ARG211 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue GTP A 602 |
| Chain | Residue |
| A | HIS209 |
| A | GLY210 |
| A | SER213 |
| A | LEU257 |
| A | HIS258 |
| A | ARG261 |
| A | TYR262 |
| A | ARG265 |
| A | GLU292 |
| A | HIS450 |
| site_id | AC3 |
| Number of Residues | 22 |
| Details | binding site for residue NAI A 603 |
| Chain | Residue |
| A | ARG94 |
| A | ASP168 |
| A | MET169 |
| A | SER170 |
| A | ARG211 |
| A | THR215 |
| A | GLN250 |
| A | GLY251 |
| A | PHE252 |
| A | GLY253 |
| A | ASN254 |
| A | VAL255 |
| A | GLU275 |
| A | SER276 |
| A | LYS295 |
| A | ALA325 |
| A | ALA326 |
| A | SER327 |
| A | GLN330 |
| A | ALA348 |
| A | ASN349 |
| A | GLU601 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | binding site for residue NAI A 604 |
| Chain | Residue |
| A | HIS195 |
| A | GLN205 |
| A | GLY206 |
| A | LYS387 |
| A | ASN388 |
| A | SER393 |
| B | HIS85 |
| B | ARG86 |
| B | ASP119 |
| B | PRO121 |
| B | LYS488 |
| B | ARG491 |
| B | VAL492 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | binding site for residue GLU B 601 |
| Chain | Residue |
| B | LYS90 |
| B | GLY91 |
| B | MET111 |
| B | LYS114 |
| B | LYS126 |
| B | ALA166 |
| B | PRO167 |
| B | ASP168 |
| B | ARG211 |
| B | ASN349 |
| B | GLY377 |
| B | VAL378 |
| B | SER381 |
| B | NAI603 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | binding site for residue GTP B 602 |
| Chain | Residue |
| B | GLY210 |
| B | SER213 |
| B | ARG217 |
| B | ARG261 |
| B | TYR262 |
| B | ARG265 |
| B | LYS289 |
| B | GLU292 |
| B | LYS446 |
| B | HIS450 |
| site_id | AC7 |
| Number of Residues | 22 |
| Details | binding site for residue NAI B 603 |
| Chain | Residue |
| B | SER327 |
| B | GLN330 |
| B | ALA348 |
| B | ASN349 |
| B | ASN374 |
| B | GLU601 |
| B | ARG94 |
| B | ASP168 |
| B | MET169 |
| B | SER170 |
| B | ARG211 |
| B | THR215 |
| B | GLN250 |
| B | PHE252 |
| B | GLY253 |
| B | ASN254 |
| B | VAL255 |
| B | GLU275 |
| B | SER276 |
| B | LYS295 |
| B | ALA325 |
| B | ALA326 |
| site_id | AC8 |
| Number of Residues | 16 |
| Details | binding site for residue NAI B 604 |
| Chain | Residue |
| B | HIS195 |
| B | GLN205 |
| B | GLY206 |
| B | LYS387 |
| B | ASN388 |
| B | HIS391 |
| B | VAL392 |
| B | SER393 |
| B | GLU445 |
| C | HIS85 |
| C | ARG86 |
| C | THR87 |
| C | ASP119 |
| C | PRO121 |
| C | LYS488 |
| C | VAL492 |
| site_id | AC9 |
| Number of Residues | 14 |
| Details | binding site for residue GLU C 601 |
| Chain | Residue |
| C | LYS90 |
| C | GLY91 |
| C | MET111 |
| C | LYS114 |
| C | LYS126 |
| C | ALA166 |
| C | PRO167 |
| C | ASP168 |
| C | ARG211 |
| C | ASN349 |
| C | GLY377 |
| C | VAL378 |
| C | SER381 |
| C | NAI604 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue NAI C 603 |
| Chain | Residue |
| A | ARG86 |
| A | ASP119 |
| A | ARG491 |
| C | LYS387 |
| C | HIS391 |
| C | SER393 |
| site_id | AD2 |
| Number of Residues | 22 |
| Details | binding site for residue NAI C 604 |
| Chain | Residue |
| C | ARG94 |
| C | ASP168 |
| C | MET169 |
| C | SER170 |
| C | ARG211 |
| C | THR215 |
| C | GLN250 |
| C | GLY251 |
| C | PHE252 |
| C | GLY253 |
| C | ASN254 |
| C | VAL255 |
| C | GLU275 |
| C | SER276 |
| C | ALA325 |
| C | ALA326 |
| C | GLN330 |
| C | GLY347 |
| C | ALA348 |
| C | ASN349 |
| C | ASN374 |
| C | GLU601 |
| site_id | AD3 |
| Number of Residues | 14 |
| Details | binding site for residue GLU D 601 |
| Chain | Residue |
| D | LYS90 |
| D | GLY91 |
| D | MET111 |
| D | LYS114 |
| D | LYS126 |
| D | ALA166 |
| D | PRO167 |
| D | ASP168 |
| D | ARG211 |
| D | ASN349 |
| D | GLY377 |
| D | VAL378 |
| D | SER381 |
| D | NAI603 |
| site_id | AD4 |
| Number of Residues | 22 |
| Details | binding site for residue NAI D 603 |
| Chain | Residue |
| D | ARG94 |
| D | PRO167 |
| D | ASP168 |
| D | MET169 |
| D | SER170 |
| D | ARG211 |
| D | THR215 |
| D | GLN250 |
| D | GLY251 |
| D | GLY253 |
| D | ASN254 |
| D | VAL255 |
| D | GLU275 |
| D | SER276 |
| D | ALA325 |
| D | ALA326 |
| D | SER327 |
| D | GLN330 |
| D | ALA348 |
| D | ASN349 |
| D | ASN374 |
| D | GLU601 |
| site_id | AD5 |
| Number of Residues | 14 |
| Details | binding site for residue GLU E 601 |
| Chain | Residue |
| E | LYS90 |
| E | GLY91 |
| E | MET111 |
| E | LYS114 |
| E | LYS126 |
| E | ALA166 |
| E | PRO167 |
| E | ASP168 |
| E | ARG211 |
| E | ASN349 |
| E | GLY377 |
| E | VAL378 |
| E | SER381 |
| E | NAI603 |
| site_id | AD6 |
| Number of Residues | 21 |
| Details | binding site for residue NAI E 603 |
| Chain | Residue |
| E | ARG94 |
| E | ASP168 |
| E | MET169 |
| E | SER170 |
| E | ARG211 |
| E | THR215 |
| E | GLN250 |
| E | GLY251 |
| E | GLY253 |
| E | ASN254 |
| E | VAL255 |
| E | GLU275 |
| E | SER276 |
| E | ALA325 |
| E | ALA326 |
| E | SER327 |
| E | GLN330 |
| E | ALA348 |
| E | ASN349 |
| E | ASN374 |
| E | GLU601 |
| site_id | AD7 |
| Number of Residues | 10 |
| Details | binding site for residue NAI F 601 |
| Chain | Residue |
| D | HIS195 |
| D | LYS387 |
| D | ASN388 |
| D | SER393 |
| F | ARG86 |
| F | THR87 |
| F | ASP119 |
| F | PRO121 |
| F | LYS488 |
| F | VAL492 |
| site_id | AD8 |
| Number of Residues | 14 |
| Details | binding site for residue GLU F 602 |
| Chain | Residue |
| F | LYS90 |
| F | GLY91 |
| F | MET111 |
| F | LYS114 |
| F | LYS126 |
| F | ALA166 |
| F | PRO167 |
| F | ASP168 |
| F | ARG211 |
| F | ASN349 |
| F | GLY377 |
| F | VAL378 |
| F | SER381 |
| F | NAI605 |
| site_id | AD9 |
| Number of Residues | 11 |
| Details | binding site for residue NAI F 603 |
| Chain | Residue |
| E | ARG86 |
| E | THR87 |
| E | ASP119 |
| E | VAL120 |
| E | PRO121 |
| F | HIS195 |
| F | ILE203 |
| F | LYS387 |
| F | ASN388 |
| F | HIS391 |
| F | SER393 |
| site_id | AE1 |
| Number of Residues | 10 |
| Details | binding site for residue GTP F 604 |
| Chain | Residue |
| F | HIS209 |
| F | GLY210 |
| F | SER213 |
| F | ARG261 |
| F | TYR262 |
| F | ARG265 |
| F | LYS289 |
| F | GLU292 |
| F | LYS446 |
| F | HIS450 |
| site_id | AE2 |
| Number of Residues | 24 |
| Details | binding site for residue NAI F 605 |
| Chain | Residue |
| F | ARG94 |
| F | PRO167 |
| F | ASP168 |
| F | MET169 |
| F | SER170 |
| F | ARG211 |
| F | THR215 |
| F | GLN250 |
| F | GLY251 |
| F | PHE252 |
| F | GLY253 |
| F | ASN254 |
| F | VAL255 |
| F | GLU275 |
| F | SER276 |
| F | LYS295 |
| F | ALA325 |
| F | ALA326 |
| F | SER327 |
| F | GLY347 |
| F | ALA348 |
| F | ASN349 |
| F | ASN374 |
| F | GLU602 |
| site_id | AE3 |
| Number of Residues | 8 |
| Details | binding site for Di-peptide GTP C 602 and ARG C 265 |
| Chain | Residue |
| C | SER213 |
| C | ARG261 |
| C | TYR262 |
| C | LEU263 |
| C | HIS264 |
| C | PHE266 |
| C | GLY267 |
| C | GLU292 |
| site_id | AE4 |
| Number of Residues | 11 |
| Details | binding site for Di-peptide GTP D 602 and ARG D 265 |
| Chain | Residue |
| D | SER213 |
| D | HIS258 |
| D | ARG261 |
| D | TYR262 |
| D | LEU263 |
| D | HIS264 |
| D | PHE266 |
| D | GLY267 |
| D | LYS289 |
| D | GLU292 |
| D | HIS450 |
| site_id | AE5 |
| Number of Residues | 17 |
| Details | binding site for Di-peptide NAI D 604 and ARG D 86 |
| Chain | Residue |
| D | GLN84 |
| D | HIS85 |
| D | THR87 |
| D | ASP119 |
| D | PRO121 |
| D | PHE122 |
| D | GLY123 |
| D | GLN463 |
| D | LYS488 |
| D | VAL492 |
| E | HIS195 |
| E | SER204 |
| E | LYS387 |
| E | ASN388 |
| E | HIS391 |
| E | SER393 |
| E | GLU445 |
| site_id | AE6 |
| Number of Residues | 9 |
| Details | binding site for Di-peptide GTP E 602 and ARG E 265 |
| Chain | Residue |
| E | HIS209 |
| E | ARG217 |
| E | ARG261 |
| E | TYR262 |
| E | LEU263 |
| E | HIS264 |
| E | PHE266 |
| E | GLY267 |
| E | HIS450 |
Functional Information from PROSITE/UniProt
| site_id | PS00074 |
| Number of Residues | 14 |
| Details | GLFV_DEHYDROGENASE Glu / Leu / Phe / Val dehydrogenases active site. VpfGGAKaGvkiNP |
| Chain | Residue | Details |
| A | VAL120-PRO133 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI3 |
| Number of Residues | 72 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11254391","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12653548","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10011","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 54 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"22076378","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 18 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"22076378","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"UniProtKB","id":"P00367","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 24 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"ADP-ribosylcysteine","evidences":[{"source":"UniProtKB","id":"P00367","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 48 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P00367","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P10860","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P00367","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
