1AG8
ALDEHYDE DEHYDROGENASE FROM BOVINE MITOCHONDRIA
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
A | 0005739 | cellular_component | mitochondrion |
A | 0005759 | cellular_component | mitochondrial matrix |
A | 0006068 | biological_process | ethanol catabolic process |
A | 0008957 | molecular_function | phenylacetaldehyde dehydrogenase (NAD+) activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
A | 0018937 | biological_process | nitroglycerin metabolic process |
A | 0046185 | biological_process | aldehyde catabolic process |
A | 0051287 | molecular_function | NAD binding |
A | 0106435 | molecular_function | carboxylesterase activity |
A | 1903179 | biological_process | regulation of dopamine biosynthetic process |
A | 1905627 | biological_process | regulation of serotonin biosynthetic process |
B | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
B | 0005739 | cellular_component | mitochondrion |
B | 0005759 | cellular_component | mitochondrial matrix |
B | 0006068 | biological_process | ethanol catabolic process |
B | 0008957 | molecular_function | phenylacetaldehyde dehydrogenase (NAD+) activity |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
B | 0018937 | biological_process | nitroglycerin metabolic process |
B | 0046185 | biological_process | aldehyde catabolic process |
B | 0051287 | molecular_function | NAD binding |
B | 0106435 | molecular_function | carboxylesterase activity |
B | 1903179 | biological_process | regulation of dopamine biosynthetic process |
B | 1905627 | biological_process | regulation of serotonin biosynthetic process |
C | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
C | 0005739 | cellular_component | mitochondrion |
C | 0005759 | cellular_component | mitochondrial matrix |
C | 0006068 | biological_process | ethanol catabolic process |
C | 0008957 | molecular_function | phenylacetaldehyde dehydrogenase (NAD+) activity |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
C | 0018937 | biological_process | nitroglycerin metabolic process |
C | 0046185 | biological_process | aldehyde catabolic process |
C | 0051287 | molecular_function | NAD binding |
C | 0106435 | molecular_function | carboxylesterase activity |
C | 1903179 | biological_process | regulation of dopamine biosynthetic process |
C | 1905627 | biological_process | regulation of serotonin biosynthetic process |
D | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
D | 0005739 | cellular_component | mitochondrion |
D | 0005759 | cellular_component | mitochondrial matrix |
D | 0006068 | biological_process | ethanol catabolic process |
D | 0008957 | molecular_function | phenylacetaldehyde dehydrogenase (NAD+) activity |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
D | 0018937 | biological_process | nitroglycerin metabolic process |
D | 0046185 | biological_process | aldehyde catabolic process |
D | 0051287 | molecular_function | NAD binding |
D | 0106435 | molecular_function | carboxylesterase activity |
D | 1903179 | biological_process | regulation of dopamine biosynthetic process |
D | 1905627 | biological_process | regulation of serotonin biosynthetic process |
Functional Information from PROSITE/UniProt
site_id | PS00070 |
Number of Residues | 12 |
Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FfNQGQCCCAGS |
Chain | Residue | Details |
A | PHE295-SER306 |
site_id | PS00687 |
Number of Residues | 8 |
Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LEIGGKSP |
Chain | Residue | Details |
A | LEU267-PRO274 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:9195888 |
Chain | Residue | Details |
A | GLU268 | |
B | GLU268 | |
C | GLU268 | |
D | GLU268 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:9195888 |
Chain | Residue | Details |
A | CYS302 | |
B | CYS302 | |
C | CYS302 | |
D | CYS302 |
site_id | SWS_FT_FI3 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z |
Chain | Residue | Details |
A | ILE166 | |
B | GLY245 | |
B | GLU268 | |
B | GLU399 | |
C | ILE166 | |
C | LYS192 | |
C | GLY225 | |
C | GLY245 | |
C | GLU268 | |
C | GLU399 | |
D | ILE166 | |
A | LYS192 | |
D | LYS192 | |
D | GLY225 | |
D | GLY245 | |
D | GLU268 | |
D | GLU399 | |
A | GLY225 | |
A | GLY245 | |
A | GLU268 | |
A | GLU399 | |
B | ILE166 | |
B | LYS192 | |
B | GLY225 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | SITE: Transition state stabilizer => ECO:0000269|PubMed:9195888 |
Chain | Residue | Details |
A | ASN169 | |
B | ASN169 | |
C | ASN169 | |
D | ASN169 |
site_id | SWS_FT_FI5 |
Number of Residues | 40 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P47738 |
Chain | Residue | Details |
A | LYS35 | |
A | LYS434 | |
B | LYS35 | |
B | LYS56 | |
B | LYS142 | |
B | LYS351 | |
B | LYS358 | |
B | LYS366 | |
B | LYS409 | |
B | LYS411 | |
B | LYS424 | |
A | LYS56 | |
B | LYS434 | |
C | LYS35 | |
C | LYS56 | |
C | LYS142 | |
C | LYS351 | |
C | LYS358 | |
C | LYS366 | |
C | LYS409 | |
C | LYS411 | |
C | LYS424 | |
A | LYS142 | |
C | LYS434 | |
D | LYS35 | |
D | LYS56 | |
D | LYS142 | |
D | LYS351 | |
D | LYS358 | |
D | LYS366 | |
D | LYS409 | |
D | LYS411 | |
D | LYS424 | |
A | LYS351 | |
D | LYS434 | |
A | LYS358 | |
A | LYS366 | |
A | LYS409 | |
A | LYS411 | |
A | LYS424 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1a4s |
Chain | Residue | Details |
A | CYS302 | |
A | GLU268 | |
A | ASN169 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1a4s |
Chain | Residue | Details |
B | CYS302 | |
B | GLU268 | |
B | ASN169 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1a4s |
Chain | Residue | Details |
C | CYS302 | |
C | GLU268 | |
C | ASN169 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1a4s |
Chain | Residue | Details |
D | CYS302 | |
D | GLU268 | |
D | ASN169 |
site_id | CSA5 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a4s |
Chain | Residue | Details |
A | CYS302 | |
A | LYS192 | |
A | GLU268 | |
A | GLU399 |
site_id | CSA6 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a4s |
Chain | Residue | Details |
B | CYS302 | |
B | LYS192 | |
B | GLU268 | |
B | GLU399 |
site_id | CSA7 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a4s |
Chain | Residue | Details |
C | CYS302 | |
C | LYS192 | |
C | GLU268 | |
C | GLU399 |
site_id | CSA8 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a4s |
Chain | Residue | Details |
D | CYS302 | |
D | LYS192 | |
D | GLU268 | |
D | GLU399 |