PROTEIN SEQUENCE, FUNCTION, COFACTORS, AND SUBUNIT.
STRAIN=KGX 39;
PubMed=8343125 [NCBI, ExPASy, EBI, Israel, Japan]
Yasin M., Fewson C.A.;
"L(+)-mandelate dehydrogenase from Rhodotorula graminis: purification, partial characterization and identification as a flavocytochrome b.";
Biochem. J. 293:455-460(1993).

Comments

FUNCTION: Reduction of (S)-mandelate to benzoylformate.
CATALYTIC ACTIVITY: (S)-2-hydroxy-2-phenylacetate + acceptor = 2-oxo-2-phenylacetate + reduced acceptor.
COFACTOR: Binds 1 FMN per subunit.
COFACTOR: Binds 1 heme group per subunit.
PATHWAY: Aromatic compound metabolism; mandelic acid degradation; benzoic acid from (R)-mandelic acid: step 2/4 .
SUBUNIT: Homotetramer.
SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. Mitochondrion intermembrane space.
SIMILARITY: To yeast flavocytochrome B2.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

PIR

S35053; S35053.

3D structure databases

ModBase

P32953.

Ontologies

GO:0005758;	Cellular component: mitochondrial intermembrane space (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005746;	Cellular component: mitochondrial respiratory chain (inferred from electronic annotation from UniProtKB-KW).
GO:0033720;	Molecular function: (S)-mandelate dehydrogenase activity (inferred from electronic annotation from EC).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0019439;	Biological process: aromatic compound catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0022900;	Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0018924;	Biological process: mandelate metabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0006810;	Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR008259; FMN_hydac_DHase_AS.
Graphical view of domain structure.

PROSITE

PS00557; FMN_HYDROXY_ACID_DH_1; PARTIAL.

ProtoNet

P32953.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Aromatic hydrocarbons catabolism; Direct protein sequencing; Electron transport; Flavoprotein; FMN; Heme; Iron; Mandelate pathway; Membrane; Metal-binding; Mitochondrion; Oxidoreductase; Respiratory chain; Transport.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 >32`	`>32`	`(S)-mandelate dehydrogenase.`	`PRO_0000206328`
`ACT_SITE`	`23 23`		`Proton acceptor (By similarity).`
`BINDING`	`26 26`		`Substrate (Potential).`
`NON_TER`	`32 32`

Sequence information

Length: 32 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 3588 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 752EA0D48C7EF701 [This is a checksum on the sequence]

        10         20         30 
DAQLPVKQRG RARSISAAEV AKHNSRDXMW VV

P32953 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools