UniProt functional annotation for P37610



	UniProt functional annotation for P37610

UniProt code: P37610.

Organism: Escherichia coli (strain K12).

Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.

Function: Catalyzes the alpha-ketoglutarate-dependent hydroxylation of taurine yielding sulfite and aminoacetaldehyde after decomposition of an unstable intermediate (PubMed:9287300). Is required for the utilization of taurine (2-aminoethanesulfonate) as an alternative sulfur source for growth in the absence of sulfate (PubMed:8808933). To a lesser extent, pentanesulfonate, 3-(N-morpholino)propanesulfonate and 1,3-dioxo-2-isoindolineethanesulfonate are also desulfonated by this enzyme in vitro; however, desulfonation by TauD of organosulfonates other than taurine seem to be of little or no importance for sulfur metabolism in vivo (PubMed:9287300). {ECO:0000269|PubMed:8808933, ECO:0000269|PubMed:9287300}.

Catalytic activity: Reaction=2-oxoglutarate + O2 + taurine = aminoacetaldehyde + CO2 + H(+) + succinate + sulfite; Xref=Rhea:RHEA:15909, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:17359, ChEBI:CHEBI:30031, ChEBI:CHEBI:58213, ChEBI:CHEBI:507393; EC=1.14.11.17; Evidence={ECO:0000269|PubMed:11955067, ECO:0000269|PubMed:12741810, ECO:0000269|PubMed:9287300, ECO:0000305|PubMed:8808933}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15910; Evidence={ECO:0000269|PubMed:8808933};

Cofactor: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:11955067, ECO:0000269|PubMed:12741810, ECO:0000269|PubMed:9287300}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:11955067, ECO:0000269|PubMed:12741810};

Activity regulation: Activated by ascorbate and inhibited by divalent metal ions such as zinc, copper and cobalt. {ECO:0000269|PubMed:9287300}.

Biophysicochemical properties: Kinetic parameters: KM=55 uM for taurine (at pH 6.9) {ECO:0000269|PubMed:9287300}; KM=11 uM for 2-oxoglutarate (at pH 6.9) {ECO:0000269|PubMed:9287300}; KM=1490 uM for butanesulfonate (at pH 6.9) {ECO:0000269|PubMed:9287300}; KM=590 uM for pentanesulfonate (at pH 6.9) {ECO:0000269|PubMed:9287300}; KM=1510 uM for hexanesulfonate (at pH 6.9) {ECO:0000269|PubMed:9287300}; KM=145 uM for 3-(N-morpholino)propanesulfonate (at pH 6.9) {ECO:0000269|PubMed:9287300}; KM=485 uM for 1,3-dioxo-2-isoindolineethanesulfonate (at pH 6.9) {ECO:0000269|PubMed:9287300}; Vmax=4.1 umol/min/mg enzyme with taurine as substrate (at pH 6.9) {ECO:0000269|PubMed:9287300}; Vmax=1.3 umol/min/mg enzyme with butanesulfonate as substrate (at pH 6.9) {ECO:0000269|PubMed:9287300}; Vmax=1.9 umol/min/mg enzyme with pentanesulfonate as substrate (at pH 6.9) {ECO:0000269|PubMed:9287300}; Vmax=2.2 umol/min/mg enzyme with hexanesulfonate as substrate (at pH 6.9) {ECO:0000269|PubMed:9287300}; Vmax=2.0 umol/min/mg enzyme with 3-(N-morpholino)propanesulfonate as substrate (at pH 6.9) {ECO:0000269|PubMed:9287300}; Vmax=3.8 umol/min/mg enzyme with 1,3-dioxo-2- isoindolineethanesulfonate as substrate (at pH 6.9) {ECO:0000269|PubMed:9287300}; pH dependence: Optimum pH is 6.9. {ECO:0000269|PubMed:9287300};

Pathway: Organosulfur degradation; taurine degradation via aerobic pathway; aminoacetaldehyde and sulfite from taurine: step 1/1. {ECO:0000269|PubMed:8808933}.

Subunit: Homodimer (PubMed:11955067, PubMed:12741810, PubMed:9287300). Was later shown to be a homotetramer arranged as a dimer of two dimers (PubMed:22221834). {ECO:0000269|PubMed:11955067, ECO:0000269|PubMed:12741810, ECO:0000269|PubMed:22221834, ECO:0000269|PubMed:9287300}.

Induction: Is only expressed during growth in the absence of sulfate or cysteine. {ECO:0000269|PubMed:8808933, ECO:0000269|PubMed:9287300}.

Disruption phenotype: Disruption of this gene leads to a loss of the ability to utilize taurine as a source of sulfur, but does not affect the utilization of a range of other aliphatic sulfonates as sulfur sources. {ECO:0000269|PubMed:8808933}.

Biotechnology: Taurine dioxygenase can be used for enzymatic determination of taurine concentration in food quality control, biological research, and medical diagnosis. {ECO:0000269|PubMed:22595347}.

Similarity: Belongs to the TfdA dioxygenase family. {ECO:0000305}.

Sequence caution: Sequence=M24488; Type=Frameshift; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Escherichia coli (strain K12).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.



Function:		Catalyzes the alpha-ketoglutarate-dependent hydroxylation of taurine yielding sulfite and aminoacetaldehyde after decomposition of an unstable intermediate (PubMed:9287300). Is required for the utilization of taurine (2-aminoethanesulfonate) as an alternative sulfur source for growth in the absence of sulfate (PubMed:8808933). To a lesser extent, pentanesulfonate, 3-(N-morpholino)propanesulfonate and 1,3-dioxo-2-isoindolineethanesulfonate are also desulfonated by this enzyme in vitro; however, desulfonation by TauD of organosulfonates other than taurine seem to be of little or no importance for sulfur metabolism in vivo (PubMed:9287300). {ECO:0000269\|PubMed:8808933, ECO:0000269\|PubMed:9287300}.


Catalytic activity:		Reaction=2-oxoglutarate + O2 + taurine = aminoacetaldehyde + CO2 + H(+) + succinate + sulfite; Xref=Rhea:RHEA:15909, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:17359, ChEBI:CHEBI:30031, ChEBI:CHEBI:58213, ChEBI:CHEBI:507393; EC=1.14.11.17; Evidence={ECO:0000269\|PubMed:11955067, ECO:0000269\|PubMed:12741810, ECO:0000269\|PubMed:9287300, ECO:0000305\|PubMed:8808933}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15910; Evidence={ECO:0000269\|PubMed:8808933};
Cofactor:		Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269\|PubMed:11955067, ECO:0000269\|PubMed:12741810, ECO:0000269\|PubMed:9287300}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269\|PubMed:11955067, ECO:0000269\|PubMed:12741810};
Activity regulation:		Activated by ascorbate and inhibited by divalent metal ions such as zinc, copper and cobalt. {ECO:0000269\|PubMed:9287300}.
Biophysicochemical properties:		Kinetic parameters: KM=55 uM for taurine (at pH 6.9) {ECO:0000269\|PubMed:9287300}; KM=11 uM for 2-oxoglutarate (at pH 6.9) {ECO:0000269\|PubMed:9287300}; KM=1490 uM for butanesulfonate (at pH 6.9) {ECO:0000269\|PubMed:9287300}; KM=590 uM for pentanesulfonate (at pH 6.9) {ECO:0000269\|PubMed:9287300}; KM=1510 uM for hexanesulfonate (at pH 6.9) {ECO:0000269\|PubMed:9287300}; KM=145 uM for 3-(N-morpholino)propanesulfonate (at pH 6.9) {ECO:0000269\|PubMed:9287300}; KM=485 uM for 1,3-dioxo-2-isoindolineethanesulfonate (at pH 6.9) {ECO:0000269\|PubMed:9287300}; Vmax=4.1 umol/min/mg enzyme with taurine as substrate (at pH 6.9) {ECO:0000269\|PubMed:9287300}; Vmax=1.3 umol/min/mg enzyme with butanesulfonate as substrate (at pH 6.9) {ECO:0000269\|PubMed:9287300}; Vmax=1.9 umol/min/mg enzyme with pentanesulfonate as substrate (at pH 6.9) {ECO:0000269\|PubMed:9287300}; Vmax=2.2 umol/min/mg enzyme with hexanesulfonate as substrate (at pH 6.9) {ECO:0000269\|PubMed:9287300}; Vmax=2.0 umol/min/mg enzyme with 3-(N-morpholino)propanesulfonate as substrate (at pH 6.9) {ECO:0000269\|PubMed:9287300}; Vmax=3.8 umol/min/mg enzyme with 1,3-dioxo-2- isoindolineethanesulfonate as substrate (at pH 6.9) {ECO:0000269\|PubMed:9287300}; pH dependence: Optimum pH is 6.9. {ECO:0000269\|PubMed:9287300};
Pathway:		Organosulfur degradation; taurine degradation via aerobic pathway; aminoacetaldehyde and sulfite from taurine: step 1/1. {ECO:0000269\|PubMed:8808933}.
Subunit:		Homodimer (PubMed:11955067, PubMed:12741810, PubMed:9287300). Was later shown to be a homotetramer arranged as a dimer of two dimers (PubMed:22221834). {ECO:0000269\|PubMed:11955067, ECO:0000269\|PubMed:12741810, ECO:0000269\|PubMed:22221834, ECO:0000269\|PubMed:9287300}.
Induction:		Is only expressed during growth in the absence of sulfate or cysteine. {ECO:0000269\|PubMed:8808933, ECO:0000269\|PubMed:9287300}.
Disruption phenotype:		Disruption of this gene leads to a loss of the ability to utilize taurine as a source of sulfur, but does not affect the utilization of a range of other aliphatic sulfonates as sulfur sources. {ECO:0000269\|PubMed:8808933}.
Biotechnology:		Taurine dioxygenase can be used for enzymatic determination of taurine concentration in food quality control, biological research, and medical diagnosis. {ECO:0000269\|PubMed:22595347}.
Similarity:		Belongs to the TfdA dioxygenase family. {ECO:0000305}.
Sequence caution:		Sequence=M24488; Type=Frameshift; Evidence={ECO:0000305};