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UniProt functional annotation for K4L7X3 | ||
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| UniProt code: K4L7X3. |
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| Organism: | |
Advenella mimigardefordensis (strain DSM 17166 / LMG 22922 / DPN7). |
| Taxonomy: | |
Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Alcaligenaceae. |
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| Function: | |
Catalyzes the conversion 3-sulfinopropanoyl-CoA (3SP-CoA) to propanoyl-CoA by abstraction of sulfite (PubMed:23354747, PubMed:26057676). Does not show dehydrogenase activity (PubMed:23354747). Involved in the degradation of 3,3'- dithiodipropionate (DTDP), a sulfur-containing precursor substrate for biosynthesis of polythioesters (PTEs) (PubMed:23354747). {ECO:0000269|PubMed:23354747, ECO:0000269|PubMed:26057676}. |
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| Catalytic activity: | |
Reaction=3-sulfinopropanoyl-CoA + H2O = H(+) + propanoyl-CoA + sulfite; Xref=Rhea:RHEA:41624, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:57392, ChEBI:CHEBI:78349; EC=3.13.1.4; Evidence={ECO:0000269|PubMed:23354747, ECO:0000269|PubMed:26057676}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41625; Evidence={ECO:0000269|PubMed:23354747, ECO:0000269|PubMed:26057676}; |
| Cofactor: | |
Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:23354747, ECO:0000269|PubMed:26057676}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:26057676}; |
| Biophysicochemical properties: | |
Kinetic parameters: KM=0.013 mM for 3SP-CoA {ECO:0000269|PubMed:23354747}; Vmax=4.19 umol/min/mg enzyme {ECO:0000269|PubMed:23354747}; Note=kcat is 3.13 sec(-1). {ECO:0000269|PubMed:23354747}; |
| Subunit: | |
Homotetramer. {ECO:0000269|PubMed:23354747, ECO:0000269|PubMed:26057676}. |
| Disruption phenotype: | |
Deletion of the gene completely impairs growth on DTDP or 3-sulfinopropanoyl (3SP) as the sole carbon source. {ECO:0000269|PubMed:23354747}. |
| Miscellaneous: | |
Does not catalyze the dehydrogenation of acyl-CoA thioesters (PubMed:23354747). The absence of dehydrogenase activity is most probably caused by the absence of a catalytic glutamate residue in either of the two positions conserved throughout the acyl-CoA dehydrogenase family (PubMed:23354747). {ECO:0000269|PubMed:23354747}. |
| Similarity: | |
Belongs to the acyl-CoA dehydrogenase family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.