UniProt functional annotation for Q9HXE3



	UniProt functional annotation for Q9HXE3

UniProt code: Q9HXE3.

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: DauA is highly expressed within the cystic fibrosis (CF) lung, and it is required for virulence via the optimal production of hydrogen cyanide, pyocyanine, pyoverdine, rhamnolipid and alginate during biofilm formation (PubMed:24011342). Involved in the catabolism of D-lysine and D-arginine. Under aerobic conditions, the arginine succinyltransferase (AST) and arginine transaminase (ATA) pathways are 2 major routes for L-arginine utilization as the sole source of carbon and nitrogen. The D-to-L racemization of arginine by DauA and DauB is necessary, before to be channeled into the AST and/or ATA pathways. DauA catalyzes the flavin-dependent oxidative deamination of D-arginine into 2-ketoarginine (2-KA) and ammonia (PubMed:3141581, PubMed:19139398, PubMed:19850617, PubMed:20809650). It has also dehydrogenase activity towards D-lysine, D-tyrosine, D-methionine, D- phenylalanine, D-ornithine, D-histidine and D-leucine as substrates (PubMed:19850617, PubMed:20809650). {ECO:0000269|PubMed:19139398, ECO:0000269|PubMed:19850617, ECO:0000269|PubMed:20809650, ECO:0000269|PubMed:24011342, ECO:0000269|PubMed:3141581}.

Catalytic activity: Reaction=A + D-arginine + H2O = 5-guanidino-2-oxopentanoate + AH2 + NH4(+); Xref=Rhea:RHEA:43572, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:28938, ChEBI:CHEBI:32689, ChEBI:CHEBI:58489; EC=1.4.99.6; Evidence={ECO:0000269|PubMed:19139398, ECO:0000269|PubMed:19850617, ECO:0000269|PubMed:20809650, ECO:0000269|PubMed:3141581};

Catalytic activity: Reaction=A + a D-alpha-amino acid + H2O = a 2-oxocarboxylate + AH2 + NH4(+); Xref=Rhea:RHEA:18125, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59871; Evidence={ECO:0000269|PubMed:19850617, ECO:0000269|PubMed:20809650};

Cofactor: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:20809650, ECO:0000269|PubMed:21707047};

Activity regulation: Inhibited by D-arginine and D-lysine at high concentration. {ECO:0000269|PubMed:19850617}.

Biophysicochemical properties: Kinetic parameters: KM=0.06 mM for D-arginine (at pH 8.7 and 25 degrees Celsius) {ECO:0000269|PubMed:20809650}; KM=0.08 mM for D-arginine (at pH 8.7 and 37 degrees Celsius) {ECO:0000269|PubMed:19850617}; KM=0.19 mM for D-lysine (at pH 8.7 and 37 degrees Celsius) {ECO:0000269|PubMed:19850617}; KM=0.26 mM for D-lysine (at pH 8.7 and 25 degrees Celsius) {ECO:0000269|PubMed:20809650}; KM=0.4 mM for D-tyrosine (at pH 8.7 and 37 degrees Celsius) {ECO:0000269|PubMed:19850617}; KM=0.8 mM for D-tyrosine (at pH 8.7 and 25 degrees Celsius) {ECO:0000269|PubMed:20809650}; KM=1.13 mM for D-phenylalanine (at pH 8.7 and 37 degrees Celsius) {ECO:0000269|PubMed:19850617}; KM=1.43 mM for D-methionine (at pH 8.7 and 37 degrees Celsius) {ECO:0000269|PubMed:19850617}; KM=1.48 mM for D-ornithine (at pH 8.7 and 37 degrees Celsius) {ECO:0000269|PubMed:19850617}; KM=3.52 mM for D-histidine (at pH 8.7 and 37 degrees Celsius) {ECO:0000269|PubMed:19850617}; KM=10 mM for D-methionine (at pH 8.7 and 25 degrees Celsius) {ECO:0000269|PubMed:20809650}; KM=11 mM for D-phenylalanine (at pH 8.7 and 25 degrees Celsius) {ECO:0000269|PubMed:20809650}; KM=11 mM for D-histidine (at pH 8.7 and 25 degrees Celsius) {ECO:0000269|PubMed:20809650}; KM=12 mM for D-leucine (at pH 8.7 and 25 degrees Celsius) {ECO:0000269|PubMed:20809650}; Note=Kcat is 204 sec(-1) for dehydrogenase activity with D-arginine as substrate (at pH 8.7 and 25 degrees Celsius). Kcat is 154 sec(-1) for dehydrogenase activity with D-methionine as substrate (at pH 8.7 and 25 degrees Celsius). Kcat is 141 sec(-1) for dehydrogenase activity with D-lysine as substrate (at pH 8.7 and 25 degrees Celsius). Kcat is 75 sec(-1) for dehydrogenase activity with D- phenylalanine as substrate (at pH 8.7 and 25 degrees Celsius). Kcat is 35 sec(-1) for dehydrogenase activity with D-histidine as substrate (at pH 8.7 and 25 degrees Celsius). Kcat is 23 sec(-1) for dehydrogenase activity with D-tyrosine as substrate (at pH 8.7 and 25 degrees Celsius). Kcat is 11.1 sec(-1) for dehydrogenase activity with D-arginine as substrate (at pH 8.7 and 37 degrees Celsius). Kcat is 9.2 sec(-1) for dehydrogenase activity with D-lysine as substrate (at pH 8.7 and 37 degrees Celsius). Kcat is 6.8 sec(-1) for dehydrogenase activity with D-methionine as substrate (at pH 8.7 and 37 degrees Celsius). Kcat is 6.4 sec(-1) for dehydrogenase activity with D-leucine as substrate (at pH 8.7 and 25 degrees Celsius). Kcat is 6.2 sec(-1) for dehydrogenase activity with D-ornithine as substrate (at pH 8.7 and 37 degrees Celsius). Kcat is 5.3 sec(-1) for dehydrogenase activity with D-phenylalanine as substrate (at pH 8.7 and 37 degrees Celsius). Kcat is 3.6 sec(-1) for dehydrogenase activity with D-histidine and D-tyrosine as substrates (at pH 8.7 and 37 degrees Celsius). {ECO:0000269|PubMed:19850617, ECO:0000269|PubMed:20809650}; pH dependence: Optimum pH is 8.7. {ECO:0000269|PubMed:19850617}; Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:19850617};

Subunit: Monomer. {ECO:0000269|PubMed:19139398}.

Induction: Induced by growth on D-arginine, D-lysine and 2-ketoarginine (2-KA), but not on L-arginine (PubMed:3141581, PubMed:19139398). Repressed by DauR. ArgR could be a transcriptional activator of the dauBAR operon in response to the presence of L-Arg (PubMed:19850617). {ECO:0000269|PubMed:19139398, ECO:0000269|PubMed:19850617, ECO:0000269|PubMed:3141581}.

Disruption phenotype: Cells lacking this gene are unable to grow on D- arginine or D-lysine as sole nitrogen source. {ECO:0000269|PubMed:19139398, ECO:0000269|PubMed:19850617}.

Miscellaneous: In vitro, it is essential to include phenazine methosulfate (PMS) or iodonitrotetrazolium chloride (INT) as the artificial electron acceptor in the reaction to ensure DauA remains active with FAD. {ECO:0000269|PubMed:19139398, ECO:0000269|PubMed:3141581}.

Similarity: Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


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:		DauA is highly expressed within the cystic fibrosis (CF) lung, and it is required for virulence via the optimal production of hydrogen cyanide, pyocyanine, pyoverdine, rhamnolipid and alginate during biofilm formation (PubMed:24011342). Involved in the catabolism of D-lysine and D-arginine. Under aerobic conditions, the arginine succinyltransferase (AST) and arginine transaminase (ATA) pathways are 2 major routes for L-arginine utilization as the sole source of carbon and nitrogen. The D-to-L racemization of arginine by DauA and DauB is necessary, before to be channeled into the AST and/or ATA pathways. DauA catalyzes the flavin-dependent oxidative deamination of D-arginine into 2-ketoarginine (2-KA) and ammonia (PubMed:3141581, PubMed:19139398, PubMed:19850617, PubMed:20809650). It has also dehydrogenase activity towards D-lysine, D-tyrosine, D-methionine, D- phenylalanine, D-ornithine, D-histidine and D-leucine as substrates (PubMed:19850617, PubMed:20809650). {ECO:0000269\|PubMed:19139398, ECO:0000269\|PubMed:19850617, ECO:0000269\|PubMed:20809650, ECO:0000269\|PubMed:24011342, ECO:0000269\|PubMed:3141581}.


Catalytic activity:		Reaction=A + D-arginine + H2O = 5-guanidino-2-oxopentanoate + AH2 + NH4(+); Xref=Rhea:RHEA:43572, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:28938, ChEBI:CHEBI:32689, ChEBI:CHEBI:58489; EC=1.4.99.6; Evidence={ECO:0000269\|PubMed:19139398, ECO:0000269\|PubMed:19850617, ECO:0000269\|PubMed:20809650, ECO:0000269\|PubMed:3141581};
Catalytic activity:		Reaction=A + a D-alpha-amino acid + H2O = a 2-oxocarboxylate + AH2 + NH4(+); Xref=Rhea:RHEA:18125, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59871; Evidence={ECO:0000269\|PubMed:19850617, ECO:0000269\|PubMed:20809650};
Cofactor:		Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269\|PubMed:20809650, ECO:0000269\|PubMed:21707047};
Activity regulation:		Inhibited by D-arginine and D-lysine at high concentration. {ECO:0000269\|PubMed:19850617}.
Biophysicochemical properties:		Kinetic parameters: KM=0.06 mM for D-arginine (at pH 8.7 and 25 degrees Celsius) {ECO:0000269\|PubMed:20809650}; KM=0.08 mM for D-arginine (at pH 8.7 and 37 degrees Celsius) {ECO:0000269\|PubMed:19850617}; KM=0.19 mM for D-lysine (at pH 8.7 and 37 degrees Celsius) {ECO:0000269\|PubMed:19850617}; KM=0.26 mM for D-lysine (at pH 8.7 and 25 degrees Celsius) {ECO:0000269\|PubMed:20809650}; KM=0.4 mM for D-tyrosine (at pH 8.7 and 37 degrees Celsius) {ECO:0000269\|PubMed:19850617}; KM=0.8 mM for D-tyrosine (at pH 8.7 and 25 degrees Celsius) {ECO:0000269\|PubMed:20809650}; KM=1.13 mM for D-phenylalanine (at pH 8.7 and 37 degrees Celsius) {ECO:0000269\|PubMed:19850617}; KM=1.43 mM for D-methionine (at pH 8.7 and 37 degrees Celsius) {ECO:0000269\|PubMed:19850617}; KM=1.48 mM for D-ornithine (at pH 8.7 and 37 degrees Celsius) {ECO:0000269\|PubMed:19850617}; KM=3.52 mM for D-histidine (at pH 8.7 and 37 degrees Celsius) {ECO:0000269\|PubMed:19850617}; KM=10 mM for D-methionine (at pH 8.7 and 25 degrees Celsius) {ECO:0000269\|PubMed:20809650}; KM=11 mM for D-phenylalanine (at pH 8.7 and 25 degrees Celsius) {ECO:0000269\|PubMed:20809650}; KM=11 mM for D-histidine (at pH 8.7 and 25 degrees Celsius) {ECO:0000269\|PubMed:20809650}; KM=12 mM for D-leucine (at pH 8.7 and 25 degrees Celsius) {ECO:0000269\|PubMed:20809650}; Note=Kcat is 204 sec(-1) for dehydrogenase activity with D-arginine as substrate (at pH 8.7 and 25 degrees Celsius). Kcat is 154 sec(-1) for dehydrogenase activity with D-methionine as substrate (at pH 8.7 and 25 degrees Celsius). Kcat is 141 sec(-1) for dehydrogenase activity with D-lysine as substrate (at pH 8.7 and 25 degrees Celsius). Kcat is 75 sec(-1) for dehydrogenase activity with D- phenylalanine as substrate (at pH 8.7 and 25 degrees Celsius). Kcat is 35 sec(-1) for dehydrogenase activity with D-histidine as substrate (at pH 8.7 and 25 degrees Celsius). Kcat is 23 sec(-1) for dehydrogenase activity with D-tyrosine as substrate (at pH 8.7 and 25 degrees Celsius). Kcat is 11.1 sec(-1) for dehydrogenase activity with D-arginine as substrate (at pH 8.7 and 37 degrees Celsius). Kcat is 9.2 sec(-1) for dehydrogenase activity with D-lysine as substrate (at pH 8.7 and 37 degrees Celsius). Kcat is 6.8 sec(-1) for dehydrogenase activity with D-methionine as substrate (at pH 8.7 and 37 degrees Celsius). Kcat is 6.4 sec(-1) for dehydrogenase activity with D-leucine as substrate (at pH 8.7 and 25 degrees Celsius). Kcat is 6.2 sec(-1) for dehydrogenase activity with D-ornithine as substrate (at pH 8.7 and 37 degrees Celsius). Kcat is 5.3 sec(-1) for dehydrogenase activity with D-phenylalanine as substrate (at pH 8.7 and 37 degrees Celsius). Kcat is 3.6 sec(-1) for dehydrogenase activity with D-histidine and D-tyrosine as substrates (at pH 8.7 and 37 degrees Celsius). {ECO:0000269\|PubMed:19850617, ECO:0000269\|PubMed:20809650}; pH dependence: Optimum pH is 8.7. {ECO:0000269\|PubMed:19850617}; Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269\|PubMed:19850617};
Subunit:		Monomer. {ECO:0000269\|PubMed:19139398}.
Induction:		Induced by growth on D-arginine, D-lysine and 2-ketoarginine (2-KA), but not on L-arginine (PubMed:3141581, PubMed:19139398). Repressed by DauR. ArgR could be a transcriptional activator of the dauBAR operon in response to the presence of L-Arg (PubMed:19850617). {ECO:0000269\|PubMed:19139398, ECO:0000269\|PubMed:19850617, ECO:0000269\|PubMed:3141581}.
Disruption phenotype:		Cells lacking this gene are unable to grow on D- arginine or D-lysine as sole nitrogen source. {ECO:0000269\|PubMed:19139398, ECO:0000269\|PubMed:19850617}.
Miscellaneous:		In vitro, it is essential to include phenazine methosulfate (PMS) or iodonitrotetrazolium chloride (INT) as the artificial electron acceptor in the reaction to ensure DauA remains active with FAD. {ECO:0000269\|PubMed:19139398, ECO:0000269\|PubMed:3141581}.
Similarity:		Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family. {ECO:0000305}.