AC   MF_00852;
DC   Protein; auto
TR   HAMAP; MF_00852; -; 1; level=0
XX
Names: BioU
XX
ID   BIOU
DE   RecName: Full=(S)-8-amino-7-oxononanoate synthase BioU;
DE            EC=2.6.1.121;
DE   AltName: Full=8-amino-7-oxononanoate carboxylating dehydrogenase;
GN   Name=bioU;
XX
CC   -!- FUNCTION: A 'suicide' enzyme that participates in biotin synthesis.
CC       Catalyzes the formation of (S)-8-amino-7-oxononanoate (DAN-carbamic
CC       acid) from (7R,8S)-8-amino-7-(carboxyamino)nonanoate (DAN), a function
CC       equivalent to the cannonical BioA reaction and the first half-reaction
CC       of BioD. The cellular requirement for biotin is thought be low enough
CC       that this single turnover enzyme supplies a sufficient amount of the
CC       cofactor. Overall it catalyzes three reactions: formation of a covalent
CC       linkage with 8-amino-7-oxononanoate to yield a BioU-DAN conjugate at
CC       the epsilon-amino group of Lys124 of BioU using NAD(P)H, carboxylation
CC       of the conjugate to form BioU-DAN-carbamic acid, and release of DAN-
CC       carbamic acid using NAD(P)+.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(8S)-8-amino-7-oxononanoate + CO2 + L-lysyl-[protein] =
CC         (7R,8S)-8-amino-7-(carboxyamino)nonanoate + (S)-2-amino-6-
CC         oxohexanoyl-[protein] + 2 H(+); Xref=Rhea:RHEA:63660, Rhea:RHEA-
CC         COMP:9752, Rhea:RHEA-COMP:12448, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:29969, ChEBI:CHEBI:131803,
CC         ChEBI:CHEBI:149468, ChEBI:CHEBI:149470; EC=2.6.1.121;
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:63662;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(8S)-8-amino-7-oxononanoate + H(+) + L-lysyl-[protein] + NADPH
CC         = H2O + N(6)-[(2S,3R)-2-amino-8-carboxyoctan-3-yl]-L-lysyl-[protein]
CC         + NADP(+); Xref=Rhea:RHEA:63664, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC         COMP:16405, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:149468,
CC         ChEBI:CHEBI:149472;
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:63666;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CO2 + H2O + N(6)-[(2S,3R)-2-amino-8-carboxyoctan-3-yl]-L-
CC         lysyl-[protein] + NADP(+) = (7R,8S)-8-amino-7-(carboxyamino)nonanoate
CC         + (S)-2-amino-6-oxohexanoyl-[protein] + 3 H(+) + NADPH;
CC         Xref=Rhea:RHEA:63668, Rhea:RHEA-COMP:12448, Rhea:RHEA-COMP:16405,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:131803,
CC         ChEBI:CHEBI:149470, ChEBI:CHEBI:149472;
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:63670;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(8S)-8-amino-7-oxononanoate + H(+) + L-lysyl-[protein] + NADH
CC         = H2O + N(6)-[(2S,3R)-2-amino-8-carboxyoctan-3-yl]-L-lysyl-[protein]
CC         + NAD(+); Xref=Rhea:RHEA:63672, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC         COMP:16405, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:149468,
CC         ChEBI:CHEBI:149472;
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:63674;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CO2 + H2O + N(6)-[(2S,3R)-2-amino-8-carboxyoctan-3-yl]-L-
CC         lysyl-[protein] + NAD(+) = (7R,8S)-8-amino-7-(carboxyamino)nonanoate
CC         + (S)-2-amino-6-oxohexanoyl-[protein] + 3 H(+) + NADH;
CC         Xref=Rhea:RHEA:63676, Rhea:RHEA-COMP:12448, Rhea:RHEA-COMP:16405,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:131803,
CC         ChEBI:CHEBI:149470, ChEBI:CHEBI:149472;
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:63678;
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC   -!- SUBUNIT: Monomer.
CC   -!- MISCELLANEOUS: In cannonical biotin synthesis a pimeloyl-conjugate is
CC       transformed into biotin by the subsequent action of BioF, BioA, BioD
CC       and BioB. This enzyme replaces BioA and performs the first half-
CC       reaction of BioD.
CC   -!- SIMILARITY: Belongs to the BioU family.
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KW   Aminotransferase
KW   Biotin biosynthesis
KW   NAD
KW   NADP
KW   Nucleotide-binding
KW   Transferase
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GO   GO:0009102; P:biotin biosynthetic process
GO   GO:0050661; F:NADP binding
GO   GO:0051287; F:NAD binding
XX
FT   From: BIOU_SYNY3 (Q55650)
FT   BINDING         15..19
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: G-[FYT]-G-G-[LI]
FT   BINDING         190..191
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: [ASG]-T
FT   ACT_SITE        124
FT                   /note="Nucleophile"
FT   Condition: K
FT   ACT_SITE        194
FT                   /note="Proton acceptor"
FT   Condition: E
FT   ACT_SITE        198
FT                   /note="Proton donor and proton acceptor"
FT   Condition: H
FT   BINDING         60
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Optional; Condition: Y
FT   MOD_RES         124
FT                   /note="Allysine"
FT   Condition: K
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Size: 315-385;
Related: None;
Template: Q55650;
Scope:
 Bacteria; Cyanobacteriota
 Archaea; Halobacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: in HALMT, HALBP
Comments: None
XX
# Revision 1.7 2023/02/17
//