We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
ProRule PRU00683
View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU00683
General rule information
[?]
| Accession | PRU00683 |
| Dates | 17-JAN-2008 (Created)
19-NOV-2022 (Last updated, Version 11) |
| Data class | Domain; |
| Predictors |
PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2 |
Name | FMN-dependent alpha-hydroxy acid dehydrogenase domain |
| Function | These enzymes are oxidoreductases that act on alpha-hydroxy acids and which are FMN-containing flavoproteins with a TIM barrel structure. |
| Scope(s) |
Eukaryota Bacteria |
| Example(s) | Q6FFS1; |
Propagated annotation
[?]
Identifier, protein and gene names
[?]
| case <Feature:PS51349:278=H> | |
| Protein name | + RecName: EC=1.-.-.-; |
| end case | |
Comments
[?]
| COFACTOR | Name=FMN; Xref=ChEBI:CHEBI:58210; |
| SIMILARITY | Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family. |
Keywords
[?]
| Flavoprotein | |
| FMN | |
| case <Feature:PS51349:278=H> | |
| Oxidoreductase | |
| end case | |
Gene Ontology
[?]
| GO:0016491; Molecular function:oxidoreductase activity | |
| end case | |
Cross-references
[?]
| PROSITE | PS00557; FMN_HYDROXY_ACID_DH_1; 1; |
Features
[?]
| From: PS51349 | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| DOMAIN | from | to | /note="FMN hydroxy acid dehydrogenase #" | |||||||||
| BINDING | 309 | 313 | /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210" |
|||||||||
| BINDING | 332 | 333 | /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210" |
|||||||||
| ACT_SITE | 278 | 278 | /note="Proton acceptor" | H | ||||||||
| BINDING | 27 | 27 | /ligand="a 2-oxocarboxylate" /ligand_id="ChEBI:CHEBI:35179" |
Y | ||||||||
| BINDING | 109 | 109 | /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210" |
S | ||||||||
| BINDING | 131 | 131 | /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210" |
Q | ||||||||
| BINDING | 133 | 133 | /ligand="a 2-oxocarboxylate" /ligand_id="ChEBI:CHEBI:35179" |
Y | ||||||||
| BINDING | 159 | 159 | /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210" |
T | ||||||||
| BINDING | 168 | 168 | /ligand="a 2-oxocarboxylate" /ligand_id="ChEBI:CHEBI:35179" |
R | ||||||||
| BINDING | 254 | 254 | /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210" |
K | ||||||||
| BINDING | 281 | 281 | /ligand="a 2-oxocarboxylate" /ligand_id="ChEBI:CHEBI:35179" |
R | ||||||||
Additional information
[?]
| Size range | 340-390 amino acids |
| Related rules |
None |
| Fusion | None |
| Repeats | 1 |
| Topology | Undefined |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.
UniProtKB rule member sequences
[?]
- UniProtKB/Swiss-Prot sets
Bacteria [128] Eukaryota [35] All [ 163 ]
- Retrieve set of proteins with 3D structure for this domain