| IED ID | IndEnz0002006205 |
| Enzyme Type ID | protease006205 |
| Protein Name |
Spermidine N 1 -acetyltransferase SAT EC 2.3.1.57 GCN5-related N-acetyltransferase GNAT Protease synthase and sporulation negative regulatory protein PAI 1 |
| Gene Name | paiA Ta0374 |
| Organism | Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) |
| Taxonomic Lineage | cellular organisms Archaea Candidatus Thermoplasmatota Thermoplasmata Thermoplasmatales Thermoplasmataceae Thermoplasma Thermoplasma acidophilum Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) |
| Enzyme Sequence | MSIEIRKLSIEDLETLIEVARESWKWTYAGIYSEEYIESWIREKYSKEKLLNEIVRSQSNLDILFLGAFADSTLIGFIELKIIANKAELLRLYLKPEYTHKKIGKTLLLEAEKIMKKKGILECRLYVHRQNSVGFSFYYKNGFKVEDTDGSDFIMEKKYES |
| Enzyme Length | 161 |
| Uniprot Accession Number | Q9HL57 |
| Absorption | |
| Active Site | ACT_SITE 138; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P0A951 |
| Activity Regulation | |
| Binding Site | BINDING 131; /note=Acetyl-CoA; /evidence=ECO:0000269|PubMed:21633970; BINDING 136; /note=Acetyl-CoA; /evidence=ECO:0000269|PubMed:21633970; BINDING 140; /note=Acetyl-CoA; /evidence=ECO:0000269|PubMed:21633970 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + an alkane-alpha,omega-diamine = an N-acetylalkane-alpha,omega-diamine + CoA + H(+); Xref=Rhea:RHEA:11116, Rhea:RHEA-COMP:9766, Rhea:RHEA-COMP:9767, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:70977, ChEBI:CHEBI:70988; EC=2.3.1.57; Evidence={ECO:0000269|PubMed:21633970}; |
| DNA Binding | |
| EC Number | 2.3.1.57 |
| Enzyme Function | FUNCTION: Involved in the protection against polyamine toxicity by regulating their concentration. Also could be involved in the negative control of sporulation as well as production of degradative enzymes such as alpha-amylase, levansucrase and alkaline phosphatase. Catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to an acceptor substrate and release both CoA and the acetylated product. It can use a variety of substrates including spermidine, L-tryptophan, L-leucine, L-lysine, dopamine and tyramine. {ECO:0000269|PubMed:21633970, ECO:0000269|PubMed:23184347}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (7); Binding site (3); Chain (1); Domain (1); Helix (7); Region (2); Site (1); Turn (1) |
| Keywords | 3D-structure;Acyltransferase;Reference proteome;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 3F0A; 3FIX; 3K9U; 3NE7; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 18,997 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=kcat is 42 min(-1) for acetyltransferase activity with acetylspermidine as substrate (at pH 8.3). kcat is 31 min(-1) for acetyltransferase activity with AcCoA as substrate (at pH 8.3). {ECO:0000269|PubMed:21633970}; |
| Metal Binding | |
| Rhea ID | RHEA:11116 |
| Cross Reference Brenda | 2.3.1.57; |