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UniProt functional annotation for Q55650 | ||
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| UniProt code: Q55650. |
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| Organism: | |
Synechocystis sp. (strain PCC 6803 / Kazusa). |
| Taxonomy: | |
Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis; unclassified Synechocystis. |
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| 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). {ECO:0000255|HAMAP-Rule:MF_00852, ECO:0000269|PubMed:32042199}. |
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| Catalytic activity: | |
Reaction=(S)-8-amino-7-oxononanoate + CO2 + L-lysyl-[protein] = (7R,8S)-8-amino-7-(carboxyamino)nonanoate + (S)-2-amino-6- oxohexanoyl-[protein] + 2 H(+); Xref=Rhea:RHEA:63660, Rhea:RHEA- COMP:9752, Rhea:RHEA-COMP:12448, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:29969, ChEBI:CHEBI:131803, ChEBI:CHEBI:149468, ChEBI:CHEBI:149470; Evidence={ECO:0000255|HAMAP- Rule:MF_00852, ECO:0000269|PubMed:32042199}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63661; Evidence={ECO:0000255|HAMAP-Rule:MF_00852, ECO:0000269|PubMed:32042199}; |
| Catalytic activity: | |
Reaction=(S)-8-amino-7-oxononanoate + H(+) + L-lysyl-[protein] + NADPH = H2O + N(6)-[(2S,3R)-2-amino-8-carboxyoctan-3-yl]-L-lysyl-[protein] + NADP(+); Xref=Rhea:RHEA:63664, Rhea:RHEA-COMP:9752, Rhea:RHEA- COMP:16405, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:149468, ChEBI:CHEBI:149472; Evidence={ECO:0000255|HAMAP-Rule:MF_00852, ECO:0000305|PubMed:32042199}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63665; Evidence={ECO:0000255|HAMAP-Rule:MF_00852, ECO:0000269|PubMed:32042199}; |
| Catalytic activity: | |
Reaction=CO2 + H2O + N(6)-[(2S,3R)-2-amino-8-carboxyoctan-3-yl]-L- lysyl-[protein] + NADP(+) = (7R,8S)-8-amino-7-(carboxyamino)nonanoate + (S)-2-amino-6-oxohexanoyl-[protein] + 3 H(+) + NADPH; Xref=Rhea:RHEA:63668, Rhea:RHEA-COMP:12448, Rhea:RHEA-COMP:16405, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:131803, ChEBI:CHEBI:149470, ChEBI:CHEBI:149472; Evidence={ECO:0000255|HAMAP- Rule:MF_00852, ECO:0000305|PubMed:32042199}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63669; Evidence={ECO:0000255|HAMAP-Rule:MF_00852, ECO:0000269|PubMed:32042199}; |
| Catalytic activity: | |
Reaction=(S)-8-amino-7-oxononanoate + H(+) + L-lysyl-[protein] + NADH = H2O + N(6)-[(2S,3R)-2-amino-8-carboxyoctan-3-yl]-L-lysyl-[protein] + NAD(+); Xref=Rhea:RHEA:63672, Rhea:RHEA-COMP:9752, Rhea:RHEA- COMP:16405, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:149468, ChEBI:CHEBI:149472; Evidence={ECO:0000255|HAMAP-Rule:MF_00852, ECO:0000269|PubMed:32042199}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63673; Evidence={ECO:0000255|HAMAP-Rule:MF_00852, ECO:0000269|PubMed:32042199}; |
| Catalytic activity: | |
Reaction=CO2 + H2O + N(6)-[(2S,3R)-2-amino-8-carboxyoctan-3-yl]-L- lysyl-[protein] + NAD(+) = (7R,8S)-8-amino-7-(carboxyamino)nonanoate + (S)-2-amino-6-oxohexanoyl-[protein] + 3 H(+) + NADH; Xref=Rhea:RHEA:63676, Rhea:RHEA-COMP:12448, Rhea:RHEA-COMP:16405, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:131803, ChEBI:CHEBI:149470, ChEBI:CHEBI:149472; Evidence={ECO:0000255|HAMAP- Rule:MF_00852, ECO:0000269|PubMed:32042199}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63677; Evidence={ECO:0000255|HAMAP-Rule:MF_00852, ECO:0000269|PubMed:32042199}; |
| Pathway: | |
Cofactor biosynthesis; biotin biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00852, ECO:0000269|PubMed:32042199}. |
| Subunit: | |
Monomer. {ECO:0000255|HAMAP-Rule:MF_00852, ECO:0000269|PubMed:32042199}. |
| Domain: | |
Has 2 domains; discontinuous domain I (residues 1-149 and 291- 331) forms a nucleotide-binding domain while domain II (residues 150- 290) binds substrate. {ECO:0000269|PubMed:32042199}. |
| Mass spectrometry: | |
Mass=37805; Method=Electrospray; Note=For native protein.; Evidence={ECO:0000269|PubMed:32042199}; |
| Mass spectrometry: | |
Mass=37976; Method=Electrospray; Note=For 7,8- diaminononanoate acid-protein (DAN) conjugate, a reaction intermediate.; Evidence={ECO:0000269|PubMed:32042199}; |
| Disruption phenotype: | |
Loss of biotin biosynthesis. {ECO:0000269|PubMed:32042199}. |
| Miscellaneous: | |
In canonical biotin synthesis a pimeloyl-conjugate is transformed into biotin by the subsequent action of BioF, BioA, BioD and BioB. This enzyme replaces BioA and performs the first half- reaction of BioD. In Synechocystis BioD acts on the product of this enzyme. {ECO:0000255|HAMAP-Rule:MF_00852, ECO:0000269|PubMed:32042199}. |
| Similarity: | |
Belongs to the BioU family. {ECO:0000255|HAMAP- Rule:MF_00852}. |
Annotations taken from UniProtKB at the EBI.