A0A0J1DD78 · A0A0J1DD78_9BURK
- ProteinLactate dehydrogenase
- GenelldD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids377 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
Cofactor
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 24 | glyoxylate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 77-79 | FMN (UniProtKB | ChEBI) | ||||
Sequence: PVG | ||||||
Binding site | 106 | FMN (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 127 | FMN (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 129 | glyoxylate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 155 | FMN (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 164 | glyoxylate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 251 | FMN (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 273 | FMN (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 275 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 275 | glyoxylate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 278 | glyoxylate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 306-310 | FMN (UniProtKB | ChEBI) | ||||
Sequence: DGGVR | ||||||
Binding site | 329-330 | FMN (UniProtKB | ChEBI) | ||||
Sequence: GR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | FMN binding | |
Molecular Function | L-lactate dehydrogenase (cytochrome) activity | |
Biological Process | lactate metabolic process |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Submitted names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Oxalobacteraceae > Telluria group > Massilia
Accessions
- Primary accessionA0A0J1DD78
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-377 | FMN hydroxy acid dehydrogenase | ||||
Sequence: MIISSATDYREGARRRIPPFLFHYLDGGAGAEQTLRANIDDLQQVKLRQRVLKGSEQLDLSTEWFGVKYDLPVALAPVGLTGMYARRGEVQAARAAAERNIPFIQSTVSVCPLKEVASASKRPIWFQLYVLKDRGFMRDVLQRARELGATTLVFTVDMPVPGARYRDAHSGMSGASGPRRRMWQAMMHPRWALDVGLRGRPHDLGNISAYRGHATGLEDYIGWLAANFDPGIGWSDLQWIRDEWQGPMVIKGILEAQDARDAKAFGADGIVVSNHGGRQLDGALSSARALPAIADAVKGDLTIFADGGVRTGTDVIRMLGLGADGVLLGRAFVYALATHGEAGVRKLFQLFEKDIRTNMVLTGVRSIREIGRDILAL |
Sequence similarities
Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length377
- Mass (Da)41,337
- Last updated2015-10-14 v1
- ChecksumA5DFBF74B3548D21
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LELH02000009 EMBL· GenBank· DDBJ | KLU37030.1 EMBL· GenBank· DDBJ | Genomic DNA |