UniProt functional annotation for Q9X034

UniProt code: Q9X034.

Organism:		Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8).
Taxonomy:		Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
Function:		Catalyzes the deamination of 5-methylthioadenosine and S- adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L- homocysteine, respectively. Is also able to deaminate adenosine. Adenosine-5-monophosphate (AMP) and S-adenosyl-L-methionine (SAM) are not enzyme substrates. {ECO:0000269|PubMed:17603473}.
Catalytic activity:		Reaction=H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L- homocysteine; Xref=Rhea:RHEA:20716, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:57856, ChEBI:CHEBI:57985; EC=3.5.4.28; Evidence={ECO:0000269|PubMed:17603473};
Catalytic activity:		Reaction=H(+) + H2O + S-methyl-5'-thioadenosine = NH4(+) + S-methyl-5'- thioinosine; Xref=Rhea:RHEA:25025, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:28938, ChEBI:CHEBI:48595; EC=3.5.4.31; Evidence={ECO:0000269|PubMed:17603473};
Cofactor:		Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:17603473}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:17603473};
Biophysicochemical properties:		Kinetic parameters: KM=210 uM for S-adenosyl-L-homocysteine {ECO:0000269|PubMed:17603473}; KM=44 uM for 5-methyl-thioadenosine {ECO:0000269|PubMed:17603473}; KM=250 uM for adenosine {ECO:0000269|PubMed:17603473};
Similarity:		Belongs to the metallo-dependent hydrolases superfamily. MTA/SAH deaminase family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.