1E2T
Arylamine N-acetyltransferase (NAT) from Salmonella typhimurium
External Resource: Annotation
Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage
Domain Annotation: SCOP2 Classification SCOP2 Database Homepage
Chains | Type | Family Name | Domain Identifier | Family Identifier | Provenance Source (Version) |
---|---|---|---|---|---|
A | SCOP2 Family | Arylamine N-acetyltransferase | 8021689 | 4000879 | SCOP2 (2022-06-29) |
A | SCOP2 Superfamily | Cysteine proteinases | 8034069 | 3001808 | SCOP2 (2022-06-29) |
G | SCOP2B Superfamily | Cysteine proteinases | 8034069 | 3001808 | SCOP2B (2022-06-29) |
B | SCOP2B Superfamily | Cysteine proteinases | 8034069 | 3001808 | SCOP2B (2022-06-29) |
C | SCOP2B Superfamily | Cysteine proteinases | 8034069 | 3001808 | SCOP2B (2022-06-29) |
D | SCOP2B Superfamily | Cysteine proteinases | 8034069 | 3001808 | SCOP2B (2022-06-29) |
E | SCOP2B Superfamily | Cysteine proteinases | 8034069 | 3001808 | SCOP2B (2022-06-29) |
F | SCOP2B Superfamily | Cysteine proteinases | 8034069 | 3001808 | SCOP2B (2022-06-29) |
H | SCOP2B Superfamily | Cysteine proteinases | 8034069 | 3001808 | SCOP2B (2022-06-29) |
Domain Annotation: ECOD Classification ECOD Database Homepage
Chains | Family Name | Domain Identifier | Architecture | Possible Homology | Homology | Topology | Family | Provenance Source (Version) |
---|---|---|---|---|---|---|---|---|
A | Acetyltransf_2 | e1e2tA1 | A: a+b complex topology | X: Cysteine proteinases-like | H: Cysteine proteinases (From Topology) | T: Cysteine proteinases | F: Acetyltransf_2 | ECOD (1.6) |
G | Acetyltransf_2 | e1e2tG1 | A: a+b complex topology | X: Cysteine proteinases-like | H: Cysteine proteinases (From Topology) | T: Cysteine proteinases | F: Acetyltransf_2 | ECOD (1.6) |
B | Acetyltransf_2 | e1e2tB1 | A: a+b complex topology | X: Cysteine proteinases-like | H: Cysteine proteinases (From Topology) | T: Cysteine proteinases | F: Acetyltransf_2 | ECOD (1.6) |
C | Acetyltransf_2 | e1e2tC1 | A: a+b complex topology | X: Cysteine proteinases-like | H: Cysteine proteinases (From Topology) | T: Cysteine proteinases | F: Acetyltransf_2 | ECOD (1.6) |
D | Acetyltransf_2 | e1e2tD1 | A: a+b complex topology | X: Cysteine proteinases-like | H: Cysteine proteinases (From Topology) | T: Cysteine proteinases | F: Acetyltransf_2 | ECOD (1.6) |
E | Acetyltransf_2 | e1e2tE1 | A: a+b complex topology | X: Cysteine proteinases-like | H: Cysteine proteinases (From Topology) | T: Cysteine proteinases | F: Acetyltransf_2 | ECOD (1.6) |
F | Acetyltransf_2 | e1e2tF1 | A: a+b complex topology | X: Cysteine proteinases-like | H: Cysteine proteinases (From Topology) | T: Cysteine proteinases | F: Acetyltransf_2 | ECOD (1.6) |
H | Acetyltransf_2 | e1e2tH1 | A: a+b complex topology | X: Cysteine proteinases-like | H: Cysteine proteinases (From Topology) | T: Cysteine proteinases | F: Acetyltransf_2 | ECOD (1.6) |
Domain Annotation: CATH CATH Database Homepage
Protein Family Annotation Pfam Database Homepage
Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage
Chains | Polymer | Molecular Function | Biological Process | Cellular Component |
---|---|---|---|---|
N-HYDROXYARYLAMINE O-ACETYLTRANSFERASE |
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InterPro: Protein Family Classification InterPro Database Homepage
Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage
Chains | Enzyme Name | Description | Catalytic Residues |
---|---|---|---|
N-hydroxyarylamine O-acetyltransferase M-CSA #515 | The N acetyl-transferase (NAT) family of enzymes N-acetylate arlyhydrazines and arylamines. The transfer of an acetyl group from acetyl coenzyme A to a substrate was first noted in the deactivation of the drug isonizid, where the rate of deactivation varied between individuals, as explained by pharmacogenetic variation in the rate of NAT activity. NAT enzymes are also involved in the metabolism and detoxification of arylamine and arylhydroxylamine carcinogenic substrates. | Defined by 5 residues: GLU:A-42 [auth A-39]ARG:A-67 [auth A-64]CYS:A-72 [auth A-69]HIS:A-110 [auth A-107]ASP:A-125 [auth A-122] | EC: 2.3.1.118 (PDB Primary Data) EC: 2.3.1.5 (UniProt) |