Reviewed, UniProtKB/Swiss-Prot P32953 (CYBL_RHOGR)

Names and origin

Protein names	Recommended name:     (S)-mandelate dehydrogenase     EC=1.1.99.31 Alternative name(s):     L(+)-mandelate dehydrogenase     Flavocytochrome b
Organism	Rhodotorula graminis (Yeast)
Taxonomic identifier	29898 [NCBI]
Taxonomic lineage	Eukaryota › Fungi › Dikarya › Basidiomycota › Pucciniomycotina › Microbotryomycetes › Sporidiobolales › mitosporic Sporidiobolales › Rhodotorula

Protein attributes

Sequence length	32 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (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. Binds 1 heme group per subunit.
Pathway	Aromatic compound metabolism; mandelic acid degradation; benzoic acid from (R)-mandelic acid: step 2/4.
Subunit structure	Homotetramer.
Subcellular location	Membrane; Peripheral membrane protein. Mitochondrion intermembrane space.
Sequence similarities	To yeast flavocytochrome B2.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism Electron transport Mandelate pathway Respiratory chain Transport
Cellular component	Membrane Mitochondrion
Ligand	FMN Flavoprotein Heme Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW mandelate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial intermembrane space Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial respiratory chain Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	(S)-mandelate dehydrogenase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – ›32	›32	(S)-mandelate dehydrogenase		PRO_0000206328
Sites
	Active site	23	1	Proton acceptor By similarity
	Binding site	26	1	Substrate Potential
Experimental info
	Non-terminal residue	32	1

Sequences

	Sequence		Length	Mass (Da)
	P32953-1 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: 752EA0D48C7EF701	FASTA	32	3,588
	10 20 30 DAQLPVKQRG RARSISAAEV AKHNSRDXMW VV

References

[1]	"L(+)-mandelate dehydrogenase from Rhodotorula graminis: purification, partial characterization and identification as a flavocytochrome b." Yasin M., Fewson C.A. Biochem. J. 293:455-460(1993) [PubMed: 8343125] [Abstract] Cited for: PROTEIN SEQUENCE, FUNCTION, COFACTORS, SUBUNIT. Strain: KGX 39.

Cross-references

Sequence databases
PIR	S35053.
3D structure databases
ModBase	Search...
Family and domain databases
InterPro	IPR008259. FMN_hydac_DHase_AS. [Graphical view]
PROSITE	PS00557. FMN_HYDROXY_ACID_DH_1. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CYBL_RHOGR

Accession

Primary (citable) accession number: P32953

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	November 4, 2008
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)