P32953 · CYBL_RHOGR
- Protein(S)-mandelate dehydrogenase, mitochondrial
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids565 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the oxidation of (S)-mandelate to benzoylformate and enables utilization of mandelate as substrate for growth.
Catalytic activity
- (S)-mandelate + A = AH2 + phenylglyoxylate
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 FMN per subunit.
Note: Binds 1 heme b group per subunit.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.47 mM | D,L-mandelate (with ferricyanide as electron acceptor) | |||||
0.53 mM | 2-deuterated D,L-mandelate (with ferricyanide as electron acceptor) | |||||
0.78 mM | D,L-mandelate (with cytochrome c as electron acceptor) | |||||
1.33 mM | 2-deuterated D,L-mandelate (with cytochrome c as electron acceptor) |
Pathway
Aromatic compound metabolism; (R)-mandelate degradation; benzoate from (R)-mandelate: step 2/4.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 121 | Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 144 | Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 215 | heme b (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 215 | phenylglyoxylate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 267-270 | FMN (UniProtKB | ChEBI) | ||||
Sequence: APAG | ||||||
Binding site | 322 | phenylglyoxylate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 364 | heme b (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 451 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 451 | phenylglyoxylate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 454 | phenylglyoxylate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 485-489 | FMN (UniProtKB | ChEBI) | ||||
Sequence: DGQAR | ||||||
Binding site | 508-509 | FMN (UniProtKB | ChEBI) | ||||
Sequence: GR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial intermembrane space | |
Cellular Component | respirasome | |
Molecular Function | (S)-mandelate dehydrogenase activity | |
Molecular Function | heme binding | |
Molecular Function | L-lactate dehydrogenase (cytochrome) activity | |
Molecular Function | metal ion binding | |
Biological Process | lactate metabolic process | |
Biological Process | mandelate catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name(S)-mandelate dehydrogenase, mitochondrial
- EC number
- Alternative names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Pucciniomycotina > Microbotryomycetes > Sporidiobolales > Sporidiobolaceae > Rhodotorula
Accessions
- Primary accessionP32953
- Secondary accessions
Subcellular Location
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-54 | Mitochondrion | ||||
Sequence: MSFARVRTALRCQRAAASPAPPKVQARRFANKAAPHASASSAGSRAFHLGLAAG | ||||||
Chain | PRO_0000206328 | 55-565 | (S)-mandelate dehydrogenase, mitochondrial | |||
Sequence: AALAVGGAGLYLFSRSPVLLDAQLPVKQRGRARSISAAEVAKHNSRDSMWVCIDDEVWDITNFVELHPGGAKVLEQNAGKDVTKVFKSIHPPKTLEKFLTDDNFVGRIDVDEVTKIGGGKNAEDLRIEQARKELRNVETVVCLDEFEEISQKILSEMAMAYYGTGAETEQTLRDEREAWQRVRFRPRVLRKMRHIDTNTTFLGIPTPLPIFVAPAGLARLGHPDGEQNIVRGVAKHDILQVVSSGASCSIDEIFEVKEPDQNLAWQFYVHSDKKIAEEKLKRALALGAKAIFVTVDVPVLGKRERDLKLKARSQNYEHPIAAQWKAAGSKVEETIAKRGVSDIPDTAHIDANLNWDDIAWIKERAPGVPIVIKGVGCVEDVELAKQYGADGVVLSTHGARQLDGARAPLDVLIEVRRKNPALLKEIEVYVDGQARRGTDVLKALCLGARGVGFGRGFLYAQSAYGADGVDKAIRILENEIQNAMRLLGANTLADLKPEMVECSFPERWVPE |
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 86-163 | Cytochrome b5 heme-binding | ||||
Sequence: ARSISAAEVAKHNSRDSMWVCIDDEVWDITNFVELHPGGAKVLEQNAGKDVTKVFKSIHPPKTLEKFLTDDNFVGRID | ||||||
Domain | 189-559 | FMN hydroxy acid dehydrogenase | ||||
Sequence: RNVETVVCLDEFEEISQKILSEMAMAYYGTGAETEQTLRDEREAWQRVRFRPRVLRKMRHIDTNTTFLGIPTPLPIFVAPAGLARLGHPDGEQNIVRGVAKHDILQVVSSGASCSIDEIFEVKEPDQNLAWQFYVHSDKKIAEEKLKRALALGAKAIFVTVDVPVLGKRERDLKLKARSQNYEHPIAAQWKAAGSKVEETIAKRGVSDIPDTAHIDANLNWDDIAWIKERAPGVPIVIKGVGCVEDVELAKQYGADGVVLSTHGARQLDGARAPLDVLIEVRRKNPALLKEIEVYVDGQARRGTDVLKALCLGARGVGFGRGFLYAQSAYGADGVDKAIRILENEIQNAMRLLGANTLADLKPEMVECSFP |
Sequence similarities
In the N-terminal section; belongs to the cytochrome b5 family.
In the C-terminal section; belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length565
- Mass (Da)61,974
- Last updated2013-07-24 v2
- ChecksumA16F5BB4CFE418F1
Keywords
- Technical term