Gene Ontology annotation through association of InterPro records with GO terms
TreeGrafter-generated GO annotations
Combined Automated Annotation using Multiple IEA Methods
UniProtKB entry B9U6P5 (SPCAD_VARPD): 3-sulfinopropanoyl-CoA desulfinase
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UniProtKB B9U6P5 is a reviewed Swiss-Prot entry for the 399-residue Variovorax paradoxus strain TBEA6 3-sulfinopropanoyl-CoA desulfinase (Acd, EC 3.13.1.4).
"CC -!- FUNCTION: Catalyzes the conversion 3-sulfinopropanoyl-CoA (3SP-CoA) to
CC propanoyl-CoA by abstraction of sulfite. Does not show dehydrogenase
CC activity. {ECO:0000269|PubMed:24317404}."
Identification of 3-sulfinopropionyl coenzyme A (CoA) desulfinases within the Acyl-CoA dehydrogenase superfamily.
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Biochemical characterization of recombinant Variovorax paradoxus strain TBEA6 Acd (B9U6P5) proved that it does not possess acyl-CoA dehydrogenase activity toward tested acyl-CoA thioesters, but instead catalyzes the non-oxidative, FAD-dependent desulfination of 3-sulfinopropanoyl-CoA (3SP-CoA) into propanoyl-CoA and sulfite (EC 3.13.1.4).
"Only AcdTBEA6, AcdN-1, and AcdLB400 desulfinated 3SP-CoA and were thus identified as 3SP-CoA desulfinases within the acyl-CoA dehydrogenase family, although none of these three Acds dehydrogenated any of the tested acyl-CoA thioesters."
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Purified V. paradoxus Acd is a homotetrameric flavoprotein that requires a non-covalently bound FAD cofactor for structural integrity and substrate positioning rather than for redox catalysis.
"Due to the fact that the 3SP-CoA desulfination reaction is basically a hydrolysis and occurs in the absence of an additional electron acceptor, it was postulated that the FAD cofactor in Acd DPN7 is not directly involved in the catalytic mechanism. It was proposed that it is necessary for the structural integrity of the enzyme and for the proper positioning of the substrate during catalysis."
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Variovorax paradoxus TBEA6 utilizes 3-sulfinopropionate (3SP) via Acd, and all purified Acd proteins assemble as soluble homotetramers.
"All purified acyl-CoA dehydrogenases appeared as homotetramers, as revealed by size exclusion chromatography."
3-mercaptopropionate dioxygenase, a cysteine dioxygenase homologue, catalyzes the initial step of 3-mercaptopropionate catabolism in the 3,3-thiodipropionic acid-degrading bacterium variovorax paradoxus.
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In Variovorax paradoxus TBEA6, 3,3'-thiodipropionic acid is metabolized via 3-sulfinopropionate to 3-sulfinopropionyl-CoA and subsequently desulfinated to propionyl-CoA.
"Insertion of Tn5::mob in a gene putatively coding for a family III acyl-CoA-transferase resulted in the accumulation of 3-sulfinopropionate during cultivation on 3,3-thiodipropionic acid, indicating that this compound is further metabolized to 3-sulfinopropionyl-CoA and subsequently to propionyl-CoA."