AC   MF_01693;
DC   Protein; auto
TR   HAMAP; MF_01693; -; 1; level=0
XX
Names: BioF_aminotrans_2
XX
ID   BIOF
DE   RecName: Full=8-amino-7-oxononanoate synthase;
DE            Short=AONS;
DE            EC=2.3.1.47;
DE   AltName: Full=7-keto-8-amino-pelargonic acid synthase;
DE            Short=7-KAP synthase;
DE            Short=KAPA synthase;
DE   AltName: Full=8-amino-7-ketopelargonate synthase;
GN   Name=bioF;
XX
CC   -!- FUNCTION: Catalyzes the decarboxylative condensation of pimeloyl-[acyl-
CC       carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON),
CC       [acyl-carrier protein], and carbon dioxide.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-carboxyhexanoyl-[ACP] + H(+) + L-alanine = (8S)-8-amino-7-
CC         oxononanoate + CO2 + holo-[ACP]; Xref=Rhea:RHEA:42288, Rhea:RHEA-
CC         COMP:9685, Rhea:RHEA-COMP:9955, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57972, ChEBI:CHEBI:64479, ChEBI:CHEBI:78846,
CC         ChEBI:CHEBI:149468; EC=2.3.1.47;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. BioF subfamily.
XX
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1; trigger=no
DR   Pfam; PF00155; Aminotran_1_2; 1; trigger=no
DR   NCBIfam; TIGR00858; BioF; 1; trigger=no
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KW   Biotin biosynthesis
KW   Pyridoxal phosphate
KW   Transferase
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GO   GO:0008710; F:8-amino-7-oxononanoate synthase activity
GO   GO:0030170; F:pyridoxal phosphate binding
GO   GO:0009102; P:biotin biosynthetic process
XX
FT   From: BIOF_ECOLI (P12998)
FT   BINDING         108..109
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: G-[FY]
FT   BINDING         21
FT                   /ligand="substrate"
FT   Condition: R
FT   BINDING         133
FT                   /ligand="substrate"
FT   Condition: H
FT   BINDING         179
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: S
FT   BINDING         207
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: H
FT   BINDING         233
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: T
FT   BINDING         352
FT                   /ligand="substrate"
FT   Condition: T
FT   MOD_RES         236
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT   Condition: K
XX
Size: 377-471;
Related: None;
Template: P12998;
Scope:
 Bacteria; Pseudomonadota
Fusion:
 Nter: MF_00668 (bioW)
 Cter: None
Duplicate: in POLSJ
Plasmid: None
Comments: In most cases, AON synthase activity has been tested with
 pimeloyl-CoA as substrate, however it is believed that pimeloyl-ACP rather
 than pimeloyl-CoA is the physiological substrate of BioF (PubMed:20693992).
 BioF (8-amino-7-oxononanoate synthase)(TIGR00858) and Kbl
 (2-amino-3-ketobutyrate coenzyme A ligase)(TIGR01822) catalyze very
 close reactions, and alignment of the amino acid sequences of both
 enzymes reveals a very close homology, which does not allow to
 separate them.
 The only way to create a specific family for the BioF enzymes is to
 limit the rule to Pseudomonadota. A few Bacillota (LYSSH and
 some close orthologs), are annotated as a 8-amino-7-oxononanoate
 synthase (BioF) due to their characterisation but are not members
 of the family.
 The rest of proteins which cannot be differentiated, is annotated
 as a putative 8-amino-7-oxononanoate synthase in DE line
 and are not members of the family.
 Proteins with both activites (TIGR00858/TIGR01825) are annotated
 as putative 8-amino-7-oxononanoate synthase/2-amino-3-ketobutyrate
 coenzyme A ligase in DE lines and BIKB in ID lines.
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# Revision 1.29 2023/06/01
//