8SK8

human liver mitochondrial Glutamate dehydrogenase 1

Functional Information from GO Data

Chain	GOid	namespace	contents
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	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005525	molecular_function	GTP binding
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0005783	cellular_component	endoplasmic reticulum
A	0006520	biological_process	amino acid metabolic process
A	0006537	biological_process	glutamate biosynthetic process
A	0006538	biological_process	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	0021762	biological_process	substantia nigra development
A	0032024	biological_process	positive regulation of insulin secretion
A	0042803	molecular_function	protein homodimerization activity
A	0043531	molecular_function	ADP binding
A	0070403	molecular_function	NAD+ binding
A	0070728	molecular_function	L-leucine binding
A	0072350	biological_process	tricarboxylic acid metabolic process
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	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005525	molecular_function	GTP binding
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0005783	cellular_component	endoplasmic reticulum
B	0006520	biological_process	amino acid metabolic process
B	0006537	biological_process	glutamate biosynthetic process
B	0006538	biological_process	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	0021762	biological_process	substantia nigra development
B	0032024	biological_process	positive regulation of insulin secretion
B	0042803	molecular_function	protein homodimerization activity
B	0043531	molecular_function	ADP binding
B	0070403	molecular_function	NAD+ binding
B	0070728	molecular_function	L-leucine binding
B	0072350	biological_process	tricarboxylic acid metabolic process
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	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005525	molecular_function	GTP binding
C	0005737	cellular_component	cytoplasm
C	0005739	cellular_component	mitochondrion
C	0005759	cellular_component	mitochondrial matrix
C	0005783	cellular_component	endoplasmic reticulum
C	0006520	biological_process	amino acid metabolic process
C	0006537	biological_process	glutamate biosynthetic process
C	0006538	biological_process	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	0021762	biological_process	substantia nigra development
C	0032024	biological_process	positive regulation of insulin secretion
C	0042803	molecular_function	protein homodimerization activity
C	0043531	molecular_function	ADP binding
C	0070403	molecular_function	NAD+ binding
C	0070728	molecular_function	L-leucine binding
C	0072350	biological_process	tricarboxylic acid metabolic process
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	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005525	molecular_function	GTP binding
D	0005737	cellular_component	cytoplasm
D	0005739	cellular_component	mitochondrion
D	0005759	cellular_component	mitochondrial matrix
D	0005783	cellular_component	endoplasmic reticulum
D	0006520	biological_process	amino acid metabolic process
D	0006537	biological_process	glutamate biosynthetic process
D	0006538	biological_process	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	0021762	biological_process	substantia nigra development
D	0032024	biological_process	positive regulation of insulin secretion
D	0042803	molecular_function	protein homodimerization activity
D	0043531	molecular_function	ADP binding
D	0070403	molecular_function	NAD+ binding
D	0070728	molecular_function	L-leucine binding
D	0072350	biological_process	tricarboxylic acid metabolic process
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	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005525	molecular_function	GTP binding
E	0005737	cellular_component	cytoplasm
E	0005739	cellular_component	mitochondrion
E	0005759	cellular_component	mitochondrial matrix
E	0005783	cellular_component	endoplasmic reticulum
E	0006520	biological_process	amino acid metabolic process
E	0006537	biological_process	glutamate biosynthetic process
E	0006538	biological_process	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	0021762	biological_process	substantia nigra development
E	0032024	biological_process	positive regulation of insulin secretion
E	0042803	molecular_function	protein homodimerization activity
E	0043531	molecular_function	ADP binding
E	0070403	molecular_function	NAD+ binding
E	0070728	molecular_function	L-leucine binding
E	0072350	biological_process	tricarboxylic acid metabolic process
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	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0005525	molecular_function	GTP binding
F	0005737	cellular_component	cytoplasm
F	0005739	cellular_component	mitochondrion
F	0005759	cellular_component	mitochondrial matrix
F	0005783	cellular_component	endoplasmic reticulum
F	0006520	biological_process	amino acid metabolic process
F	0006537	biological_process	glutamate biosynthetic process
F	0006538	biological_process	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	0021762	biological_process	substantia nigra development
F	0032024	biological_process	positive regulation of insulin secretion
F	0042803	molecular_function	protein homodimerization activity
F	0043531	molecular_function	ADP binding
F	0070403	molecular_function	NAD+ binding
F	0070728	molecular_function	L-leucine binding
F	0072350	biological_process	tricarboxylic acid metabolic process

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	VAL177-PRO190

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10011

Chain	Residue	Details
A	LYS183
B	LYS183
C	LYS183
D	LYS183
E	LYS183
F	LYS183

---

site_id	SWS_FT_FI2
Number of Residues	78
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P00366

Chain	Residue	Details
A	GLN141
A	SER438
A	LYS444
A	SER450
A	ARG516
B	GLN141
B	LYS147
B	LYS171
B	ASP176
B	HIS252
B	HIS266
A	LYS147
B	SER270
B	TYR319
B	ARG322
B	SER438
B	LYS444
B	SER450
B	ARG516
C	GLN141
C	LYS147
C	LYS171
A	LYS171
C	ASP176
C	HIS252
C	HIS266
C	SER270
C	TYR319
C	ARG322
C	SER438
C	LYS444
C	SER450
C	ARG516
A	ASP176
D	GLN141
D	LYS147
D	LYS171
D	ASP176
D	HIS252
D	HIS266
D	SER270
D	TYR319
D	ARG322
D	SER438
A	HIS252
D	LYS444
D	SER450
D	ARG516
E	GLN141
E	LYS147
E	LYS171
E	ASP176
E	HIS252
E	HIS266
E	SER270
A	HIS266
E	TYR319
E	ARG322
E	SER438
E	LYS444
E	SER450
E	ARG516
F	GLN141
F	LYS147
F	LYS171
F	ASP176
A	SER270
F	HIS252
F	HIS266
F	SER270
F	TYR319
F	ARG322
F	SER438
F	LYS444
F	SER450
F	ARG516
A	TYR319
A	ARG322

---

site_id	SWS_FT_FI3
Number of Residues	12
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P26443

Chain	Residue	Details
A	LYS68
E	LYS200
F	LYS68
F	LYS200
A	LYS200
B	LYS68
B	LYS200
C	LYS68
C	LYS200
D	LYS68
D	LYS200
E	LYS68

---

site_id	SWS_FT_FI4
Number of Residues	12
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P26443

Chain	Residue	Details
A	SER79
E	SER128
F	SER79
F	SER128
A	SER128
B	SER79
B	SER128
C	SER79
C	SER128
D	SER79
D	SER128
E	SER79

---

site_id	SWS_FT_FI5
Number of Residues	54
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P00366

Chain	Residue	Details
A	LYS84
B	LYS84
B	LYS110
B	LYS162
B	LYS363
B	LYS415
B	LYS457
B	LYS503
B	LYS527
B	LYS545
C	LYS84
A	LYS110
C	LYS110
C	LYS162
C	LYS363
C	LYS415
C	LYS457
C	LYS503
C	LYS527
C	LYS545
D	LYS84
D	LYS110
A	LYS162
D	LYS162
D	LYS363
D	LYS415
D	LYS457
D	LYS503
D	LYS527
D	LYS545
E	LYS84
E	LYS110
E	LYS162
A	LYS363
E	LYS363
E	LYS415
E	LYS457
E	LYS503
E	LYS527
E	LYS545
F	LYS84
F	LYS110
F	LYS162
F	LYS363
A	LYS415
F	LYS415
F	LYS457
F	LYS503
F	LYS527
F	LYS545
A	LYS457
A	LYS503
A	LYS527
A	LYS545

---

site_id	SWS_FT_FI6
Number of Residues	6
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P26443

Chain	Residue	Details
A	TYR135
B	TYR135
C	TYR135
D	TYR135
E	TYR135
F	TYR135

---

site_id	SWS_FT_FI7
Number of Residues	6
Details	MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29192674

Chain	Residue	Details
A	LYS147
B	LYS147
C	LYS147
D	LYS147
E	LYS147
F	LYS147

---

site_id	SWS_FT_FI8
Number of Residues	30
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P26443

Chain	Residue	Details
A	LYS171
B	LYS548
C	LYS171
C	LYS187
C	LYS211
C	LYS326
C	LYS548
D	LYS171
D	LYS187
D	LYS211
D	LYS326
A	LYS187
D	LYS548
E	LYS171
E	LYS187
E	LYS211
E	LYS326
E	LYS548
F	LYS171
F	LYS187
F	LYS211
F	LYS326
A	LYS211
F	LYS548
A	LYS326
A	LYS548
B	LYS171
B	LYS187
B	LYS211
B	LYS326

---

site_id	SWS_FT_FI9
Number of Residues	6
Details	MOD_RES: ADP-ribosylcysteine => ECO:0000269|PubMed:16023112

Chain	Residue	Details
A	CYS172
B	CYS172
C	CYS172
D	CYS172
E	CYS172
F	CYS172

---

site_id	SWS_FT_FI10
Number of Residues	48
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P26443

Chain	Residue	Details
A	LYS183
B	LYS191
B	LYS346
B	LYS352
B	LYS365
B	LYS390
B	LYS477
B	LYS480
C	LYS183
C	LYS191
C	LYS346
A	LYS191
C	LYS352
C	LYS365
C	LYS390
C	LYS477
C	LYS480
D	LYS183
D	LYS191
D	LYS346
D	LYS352
D	LYS365
A	LYS346
D	LYS390
D	LYS477
D	LYS480
E	LYS183
E	LYS191
E	LYS346
E	LYS352
E	LYS365
E	LYS390
E	LYS477
A	LYS352
E	LYS480
F	LYS183
F	LYS191
F	LYS346
F	LYS352
F	LYS365
F	LYS390
F	LYS477
F	LYS480
A	LYS365
A	LYS390
A	LYS477
A	LYS480
B	LYS183

---

site_id	SWS_FT_FI11
Number of Residues	12
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	SER227
E	SER384
F	SER227
F	SER384
A	SER384
B	SER227
B	SER384
C	SER227
C	SER384
D	SER227
D	SER384
E	SER227

---

site_id	SWS_FT_FI12
Number of Residues	12
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P00366

Chain	Residue	Details
A	LYS386
E	LYS399
F	LYS386
F	LYS399
A	LYS399
B	LYS386
B	LYS399
C	LYS386
C	LYS399
D	LYS386
D	LYS399
E	LYS386

---

site_id	SWS_FT_FI13
Number of Residues	6
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P10860

Chain	Residue	Details
A	THR410
B	THR410
C	THR410
D	THR410
E	THR410
F	THR410

---

site_id	SWS_FT_FI14
Number of Residues	6
Details	MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	TYR512
B	TYR512
C	TYR512
D	TYR512
E	TYR512
F	TYR512

---