HAMAP rule MF_00852
General rule information
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| Accession | MF_00852 |
| Dates | 30-APR-2020 (Created)
17-FEB-2023 (Last updated, Version 7) |
| Name | BioU |
| Scope(s) |
Bacteria Cyanobacteriota Archaea Halobacteria |
| Template(s) | Q55650 (BIOU_SYNY3); [ Recover all ] |
| Triggered by |
HAMAP; MF_00852 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | BIOU |
| Protein name | RecName: Full=(S)-8-amino-7-oxononanoate synthase BioU; EC=2.6.1.121; AltName: Full=8-amino-7-oxononanoate carboxylating dehydrogenase; |
| Gene name | Name=bioU; |
Comments
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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)+. |
| CATALYTIC ACTIVITY | Reaction=(8S)-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; EC=2.6.1.121; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:63662; |
| CATALYTIC ACTIVITY | Reaction=(8S)-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; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:63666; |
| 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; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:63670; |
| CATALYTIC ACTIVITY | Reaction=(8S)-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; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:63674; |
| 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; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:63678; |
| PATHWAY | Cofactor biosynthesis; biotin biosynthesis. |
| SUBUNIT | Monomer. |
| MISCELLANEOUS | In cannonical 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. |
| SIMILARITY | Belongs to the BioU family. |
Keywords
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Gene Ontology
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| GO:0009102; Biological process:biotin biosynthetic process |
| GO:0050661; Molecular function:NADP binding |
| GO:0051287; Molecular function:NAD binding |
Cross-references
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Features
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| From: BIOU_SYNY3 (Q55650) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 15 | 19 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
G-[FYT]-G-G-[LI] | ||||||||
| BINDING | 190 | 191 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
[ASG]-T | ||||||||
| ACT_SITE | 124 | 124 | /note="Nucleophile" | K | ||||||||
| ACT_SITE | 194 | 194 | /note="Proton acceptor" | E | ||||||||
| ACT_SITE | 198 | 198 | /note="Proton donor and proton acceptor" | H | ||||||||
| BINDING | 60 | 60 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
Y | ||||||||
| MOD_RES | 124 | 124 | /note="Allysine" | K | ||||||||
Additional information
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| Size range | 315-385 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |