HAMAP rule MF_01693
General rule information
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Accession | MF_01693 |
Dates | 1-JUL-2009 (Created)
1-JUN-2023 (Last updated, Version 29) |
Name | BioF_aminotrans_2 |
Scope(s) |
Bacteria Pseudomonadota |
Template(s) | P12998 (BIOF_ECOLI); [ Recover all ] |
Triggered by |
HAMAP; MF_01693 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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Identifier | BIOF |
Protein name | RecName: Full=8-amino-7-oxononanoate synthase; Short=AONS; EC=2.3.1.47; AltName: Full=7-keto-8-amino-pelargonic acid synthase; Short=7-KAP synthase; Short=KAPA synthase; AltName: Full=8-amino-7-ketopelargonate synthase; |
Gene name | Name=bioF; |
Comments
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FUNCTION | Catalyzes the decarboxylative condensation of pimeloyl-[acyl- carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide. |
CATALYTIC ACTIVITY | Reaction=6-carboxyhexanoyl-[ACP] + H(+) + L-alanine = (8S)-8-amino-7- oxononanoate + CO2 + holo-[ACP]; Xref=Rhea:RHEA:42288, Rhea:RHEA- COMP:9685, Rhea:RHEA-COMP:9955, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57972, ChEBI:CHEBI:64479, ChEBI:CHEBI:78846, ChEBI:CHEBI:149468; EC=2.3.1.47; |
COFACTOR | Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; |
PATHWAY | Cofactor biosynthesis; biotin biosynthesis. |
SUBUNIT | Homodimer. |
SIMILARITY | Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. BioF subfamily. |
Keywords
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Gene Ontology
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GO:0008710; Molecular function:8-amino-7-oxononanoate synthase activity |
GO:0030170; Molecular function:pyridoxal phosphate binding |
GO:0009102; Biological process:biotin biosynthetic process |
Cross-references
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PROSITE | PS00599; AA_TRANSFER_CLASS_2; 1; |
Pfam | PF00155; Aminotran_1_2; 1; |
NCBIfam | TIGR00858; BioF; 1; |
Features
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From: BIOF_ECOLI (P12998) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 108 | 109 | /ligand="pyridoxal 5'-phosphate" /ligand_id="ChEBI:CHEBI:597326" |
G-[FY] | ||||||||
BINDING | 21 | 21 | /ligand="substrate" | R | ||||||||
BINDING | 133 | 133 | /ligand="substrate" | H | ||||||||
BINDING | 179 | 179 | /ligand="pyridoxal 5'-phosphate" /ligand_id="ChEBI:CHEBI:597326" |
S | ||||||||
BINDING | 207 | 207 | /ligand="pyridoxal 5'-phosphate" /ligand_id="ChEBI:CHEBI:597326" |
H | ||||||||
BINDING | 233 | 233 | /ligand="pyridoxal 5'-phosphate" /ligand_id="ChEBI:CHEBI:597326" |
T | ||||||||
BINDING | 352 | 352 | /ligand="substrate" | T | ||||||||
MOD_RES | 236 | 236 | /note="N6-(pyridoxal phosphate)lysine" | K |
Additional information
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Size range | 377-471 amino acids |
Related rules |
None |
Fusion | Nter: MF_00668 (bioW) Cter: 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. |