UniProt functional annotation for Q9I5I6

UniProt code: Q9I5I6.

Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas.
 
Function: NAD-dependent L-serine dehydrogenase that catalyzes the oxidation of L-serine and methyl-L-serine and is possibly involved in serine catabolism. Has low activity toward beta-hydroxyisobutyrate. {ECO:0000269|PubMed:22128181}.
 
Catalytic activity: Reaction=L-serine + NAD(+) = aminoacetaldehyde + CO2 + NADH; Xref=Rhea:RHEA:43628, ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58213; EC=1.1.1.387; Evidence={ECO:0000269|PubMed:22128181};
Biophysicochemical properties: Kinetic parameters: KM=2.5 mM for L-serine {ECO:0000269|PubMed:22128181}; KM=2.4 mM for methyl-DL-serine {ECO:0000269|PubMed:22128181}; KM=19.8 mM for DL-glycerate {ECO:0000269|PubMed:22128181}; KM=17.4 mM for methyl-2,2-dimethyl-3-hydroxypropionate {ECO:0000269|PubMed:22128181}; KM=3.4 mM for NAD {ECO:0000269|PubMed:22128181}; Vmax=18.7 umol/min/mg enzyme with L-serine as substrate {ECO:0000269|PubMed:22128181}; Vmax=17.2 umol/min/mg enzyme with methyl-DL-serine as substrate {ECO:0000269|PubMed:22128181}; Vmax=10.4 umol/min/mg enzyme with DL-glycerate as substrate {ECO:0000269|PubMed:22128181}; Vmax=20.9 umol/min/mg enzyme with methyl-2,2-dimethyl-3- hydroxypropionate as substrate {ECO:0000269|PubMed:22128181}; Vmax=2.8 umol/min/mg enzyme with NAD as substrate {ECO:0000269|PubMed:22128181}; Note=kcat is 10.4 sec(-1) with L-serine as substrate. kcat is 9.6 sec(-1) with methyl-DL-serine as substrate. kcat is 5.8 sec(-1) with DL-glycerate as substrate. kcat is 11.6 sec(-1) with methyl-2,2- dimethyl-3-hydroxypropionate as substrate. kcat is 1.6 sec(-1) with NAD as substrate.;
Pathway: Amino-acid degradation.
Subunit: Homotetramer, dimer of dimers. {ECO:0000269|PubMed:22128181}.
Similarity: Belongs to the HIBADH-related family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.