| Protein Name |
(S)-8-amino-7-oxononanoate synthase BioU |
| #PDB ID |
2
|
| Organism |
Synechocystis sp. (strain PCC 6803 / Kazusa) |
| Uniprot ID/ACC |
Q55650 (BIOU_SYNY3)
|
| Synonym(s) |
-
|
| Gene Symbol |
bioU
|
| Gene ID |
-
|
| Sequence |
MENNSLAPLRVGILGFGGLGQAAARLLAPKQEMKLVAVADRHGYLYDADGIDVDNAVQAYTQQGSVGKAKKGQMSEQSIEDLIGEGEVDGYFLALPNLPNTFMADVTRQFIASGWQGVLVDALKRTSAVEQLITLREDLAQAGITYMTGCGATPGLLTAAAAIASQSFQEIHQVKITFGVGIANWEAYRATIREDIAHMPGYNVDKAQAMTDAEVAALLDQTNGILALEDMEHADDIMLELAGICHRDQVTVGGVVDTRNPKKPLSTHVKITGRTFEGKISSHTFTLGDETSMAANVCGPAFGYLKAGYGLHRQGLKGLFTAADVMPKFVR |
| Protein Class |
OXIDOREDUCTASE |
| Function |
A 'suicide' enzyme that participates in biotin synthesis. Catalyzes the formation of (S)-8-amino-7-oxononanoate (DAN-carbamic acid) from (7R,8S)-8-amino-7-(carboxyamino)nonanoate (DAN), a function equivalent to the cannonical BioA reaction and the first half-reaction of BioD. The cellular requirement for biotin is thought be low enough that this single turnover enzyme supplies a sufficient amount of the cofactor. Overall it catalyzes three reactions: formation of a covalent linkage with 8-amino-7-oxononanoate to yield a BioU-DAN conjugate at the epsilon-amino group of Lys124 of BioU using NAD(P)H, carboxylation of the conjugate to form BioU-DAN-carbamic acid, and release of DAN-carbamic acid using NAD(P)+ (By similarity) (PubMed:32042199). A coupled Synechocystis BioU/BioD assay produces dethiobiotin from DAN. Complements a bioA deletion in E.coli but not a bioD1 deletion (PubMed:32042199).
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