| IED ID | IndEnz0002001114 |
| Enzyme Type ID | protease001114 |
| Protein Name |
Spermidine/spermine N 1 -acetyltransferase SSAT Protease synthase and sporulation negative regulatory protein PAI 1 Spermidine N 1 -acetyltransferase SAT EC 2.3.1.57 |
| Gene Name | paiA BSU32150 |
| Organism | Bacillus subtilis (strain 168) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168) |
| Enzyme Sequence | MSVKMKKCSREDLQTLQQLSIETFNDTFKEQNSPENMKAYLESAFNTEQLEKELSNMSSQFFFIYFDHEIAGYVKVNIDDAQSEEMGAESLEIERIYIKNSFQKHGLGKHLLNKAIEIALERNKKNIWLGVWEKNENAIAFYKKMGFVQTGAHSFYMGDEEQTDLIMAKTLI |
| Enzyme Length | 172 |
| Uniprot Accession Number | P21340 |
| Absorption | |
| Active Site | ACT_SITE 142; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P0A951 |
| Activity Regulation | |
| Binding Site | BINDING 144; /note=Acetyl-CoA; /evidence=ECO:0000269|PubMed:16210326 |
| 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:16210326}; |
| 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 releases both CoA and the acetylated product. It possesses N1-acetyltransferase activity toward polyamine substrates including spermidine, spermine, aminopropylcadaverine, norspermidine, homospermidine, N(8)-acetylspermidine, diaminopropane and agmatine. {ECO:0000269|PubMed:16210326, ECO:0000269|PubMed:2108124}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (9); Binding site (1); Chain (1); Domain (1); Helix (8); Initiator methionine (1); Region (3); Sequence conflict (1); Site (1) |
| Keywords | 3D-structure;Acyltransferase;Direct protein sequencing;Reference proteome;Sporulation;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1TIQ; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 20,015 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=31 uM for AcCoA (at pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:16210326}; KM=76 uM for spermine (at pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:16210326}; KM=295 uM for N(1)-acetylspermine (at pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:16210326}; KM=323 uM for spermidine (at pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:16210326}; KM=410 uM for aminopropylcadaverine (at pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:16210326}; Vmax=550 nmol/min/mg enzyme with AcCoA as substrate (at pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:16210326}; Vmax=481 nmol/min/mg enzyme with spermine as substrate (at pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:16210326}; Vmax=178 nmol/min/mg enzyme with N(1)-acetylspermine as substrate (at pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:16210326}; Vmax=154 nmol/min/mg enzyme with aminopropylcadaverine as substrate (at pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:16210326}; Vmax=130 nmol/min/mg enzyme with spermidine as substrate (at pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:16210326}; Note=kcat is 21.9 min(-1) for acetyltransferase activity with AcCoA as substrate (at pH 9 and 37 degrees Celius). kcat is 19.1 min(-1) for acetyltransferase activity with spermine as substrate (at pH 9 and 37 degrees Celius). kcat is 7.1 min(-1) for acetyltransferase activity with N(1)-acetylspermine as substrate (at pH 9 and 37 degrees Celius). kcat is 6.1 min(-1) for acetyltransferase activity with aminopropylcadaverine as substrate (at pH 9 and 37 degrees Celius). kcat is 5.2 min(-1) for acetyltransferase activity with spermidine as substrate (at pH 9 and 37 degrees Celius). {ECO:0000269|PubMed:16210326}; |
| Metal Binding | |
| Rhea ID | RHEA:11116 |
| Cross Reference Brenda |