A0A7J5JGW2 · A0A7J5JGW2_BACT4
- ProteinMultifunctional fusion protein
- GenebioB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids804 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only aminotransferase known to utilize SAM as an amino donor.
Catalyzes two activities which are involved in the biotine biosynthesis: the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism, and the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA).
Catalytic activity
- (4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]
CHEBI:149473 + RHEA-COMP:14737 + 2 RHEA-COMP:10001 + 2 CHEBI:59789 = 2 CHEBI:17319 + RHEA-COMP:14739 + CHEBI:57586 + 2 CHEBI:57844 + 2 RHEA-COMP:10000
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine.
Note: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Pathway
Cofactor biosynthesis; biotin biosynthesis; 7,8-diaminononanoate from 8-amino-7-oxononanoate (SAM route): step 1/1.
Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 125 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 129 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 132 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 169 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 201 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 261 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 331 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Site | 396 | Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAM | ||||
Sequence: Y | ||||||
Binding site | 431 | substrate | ||||
Sequence: W | ||||||
Binding site | 491-492 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: GS | ||||||
Binding site | 524 | substrate | ||||
Sequence: Y | ||||||
Binding site | 625 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 654 | substrate | ||||
Sequence: K | ||||||
Binding site | 687 | substrate | ||||
Sequence: G | ||||||
Binding site | 688-689 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: PT | ||||||
Binding site | 771 | substrate | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 2 iron, 2 sulfur cluster binding | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity | |
Molecular Function | biotin synthase activity | |
Molecular Function | iron ion binding | |
Molecular Function | pyridoxal phosphate binding | |
Biological Process | biotin biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMultifunctional fusion protein
Including 2 domains:
- Recommended nameAdenosylmethionine-8-amino-7-oxononanoate aminotransferase
- EC number
- Alternative names
- Recommended nameBiotin synthase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacteroidota > Bacteroidia > Bacteroidales > Bacteroidaceae > Bacteroides
Accessions
- Primary accessionA0A7J5JGW2
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 654 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 107-336 | Radical SAM core | ||||
Sequence: CASHEFDMCSIINAKSGRCPENCKWCAQSSHYKTQAEIYDLLPAEECLRQAKYNESQDVNRFSLVTSGRKPSPKQISQLCDAARLMRKHSSIQLCASLGLLNEEELRALHTAGITRYHCNLETAPSYFPTLCSTHTQEQKLATLDAARRVGMDICCGGIIGMGETMEQRIEFAFTLAELNVQSIPINLLSPIPGTPLENEKALSEEEILRTIALFRFINPTAFLRFAGGR |
Sequence similarities
Belongs to the radical SAM superfamily. Biotin synthase family.
In the C-terminal section; belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. BioA subfamily.
In the N-terminal section; belongs to the radical SAM superfamily. Biotin synthase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length804
- Mass (Da)89,584
- Last updated2021-04-07 v1
- ChecksumCC8C8F743A644444