UniProt functional annotation for Q9KL03



	UniProt functional annotation for Q9KL03

UniProt code: Q9KL03.

Organism: Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).

Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae; Vibrio.

Function: Involved in the protection against polyamine toxicity by regulating their concentration. Catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to the primary amino groups of spermidine to yield N(1)- and N(8)-acetylspermidine. It can use polyamines such as spermine and N(1)-acetylspermine, but not putrescine or cadaverine. {ECO:0000269|PubMed:23184347, ECO:0000269|PubMed:25623305}.

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:25623305};

Activity regulation: Allosterically regulated. {ECO:0000269|PubMed:25623305}.

Biophysicochemical properties: Kinetic parameters: KM=99 uM for spermine (in the presence of 100 uM AcCoA at pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:25623305}; KM=554 uM for spermidine (in the presence of 100 uM AcCoA at pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:25623305}; KM=1210 uM for AcCoA (in the presence of 3 mM spermine at pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:25623305}; Vmax=48.1 umol/min/mg enzyme with AcCoA as substrate (in the presence of 500 uM spermine at pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:25623305}; Vmax=19.4 umol/min/mg enzyme with spermine as substrate (in the presence of 100 uM AcCoA at pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:25623305}; Vmax=18.8 umol/min/mg enzyme with spermidine as substrate (in the presence of 100 uM AcCoA at pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:25623305}; Note=Kcat is 16.8 sec(-1) for acetyltransferase activity with AcCoA as substrate (in the presence of 500 uM spermine at pH 9 and 37 degrees Celsius). Kcat is 6.79 sec(-1) for acetyltransferase activity with spermine as substrate (in the presence of 100 uM AcCoA at pH 9 and 37 degrees Celsius). Kcat is 6.58 sec(-1) for acetyltransferase activity with spermidine as substrate (in the presence of 100 uM AcCoA at pH 9 and 37 degrees Celsius). {ECO:0000269|PubMed:25623305};

Subunit: Homododecamer; dimer of hexamers. {ECO:0000269|PubMed:25623305}.

Subcellular location: Cytoplasm {ECO:0000305}.

Similarity: Belongs to the acetyltransferase family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae; Vibrio.



Function:		Involved in the protection against polyamine toxicity by regulating their concentration. Catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to the primary amino groups of spermidine to yield N(1)- and N(8)-acetylspermidine. It can use polyamines such as spermine and N(1)-acetylspermine, but not putrescine or cadaverine. {ECO:0000269\|PubMed:23184347, ECO:0000269\|PubMed:25623305}.


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:25623305};
Activity regulation:		Allosterically regulated. {ECO:0000269\|PubMed:25623305}.
Biophysicochemical properties:		Kinetic parameters: KM=99 uM for spermine (in the presence of 100 uM AcCoA at pH 9 and 37 degrees Celsius) {ECO:0000269\|PubMed:25623305}; KM=554 uM for spermidine (in the presence of 100 uM AcCoA at pH 9 and 37 degrees Celsius) {ECO:0000269\|PubMed:25623305}; KM=1210 uM for AcCoA (in the presence of 3 mM spermine at pH 9 and 37 degrees Celsius) {ECO:0000269\|PubMed:25623305}; Vmax=48.1 umol/min/mg enzyme with AcCoA as substrate (in the presence of 500 uM spermine at pH 9 and 37 degrees Celsius) {ECO:0000269\|PubMed:25623305}; Vmax=19.4 umol/min/mg enzyme with spermine as substrate (in the presence of 100 uM AcCoA at pH 9 and 37 degrees Celsius) {ECO:0000269\|PubMed:25623305}; Vmax=18.8 umol/min/mg enzyme with spermidine as substrate (in the presence of 100 uM AcCoA at pH 9 and 37 degrees Celsius) {ECO:0000269\|PubMed:25623305}; Note=Kcat is 16.8 sec(-1) for acetyltransferase activity with AcCoA as substrate (in the presence of 500 uM spermine at pH 9 and 37 degrees Celsius). Kcat is 6.79 sec(-1) for acetyltransferase activity with spermine as substrate (in the presence of 100 uM AcCoA at pH 9 and 37 degrees Celsius). Kcat is 6.58 sec(-1) for acetyltransferase activity with spermidine as substrate (in the presence of 100 uM AcCoA at pH 9 and 37 degrees Celsius). {ECO:0000269\|PubMed:25623305};
Subunit:		Homododecamer; dimer of hexamers. {ECO:0000269\|PubMed:25623305}.
Subcellular location:		Cytoplasm {ECO:0000305}.
Similarity:		Belongs to the acetyltransferase family. {ECO:0000305}.