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HAMAP rule MF_01693

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General rule information [?]

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 [?]

Identifier, protein and gene names [?]

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 [?]

FUNCTIONCatalyzes 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;
PATHWAYCofactor biosynthesis; biotin biosynthesis.
SUBUNITHomodimer.
SIMILARITYBelongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. BioF subfamily.

Keywords [?]


Gene Ontology [?]

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 [?]

PROSITE PS00599; AA_TRANSFER_CLASS_2; 1;
Pfam PF00155; Aminotran_1_2; 1;
NCBIfam TIGR00858; BioF; 1;

Features [?]

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 [?]

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.



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