[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-30. STRAIN=ATCC 12633 / DSM 291 / NCIB 9494 / NCTC 10936 / Stanier 90; DOI=10.1021/bi00494a015; PubMed=2271624 [NCBI, ExPASy, EBI, Israel, Japan] Tsou A.Y., Ransom S.C., Gerlt J.A., Buechter D.D., Babbitt P.C., Kenyon G.L.; "Mandelate pathway of Pseudomonas putida: sequence relationships involving mandelate racemase, (S)-mandelate dehydrogenase, and benzoylformate decarboxylase and expression of benzoylformate decarboxylase in Escherichia coli."; Biochemistry 29:9856-9862(1990).
[2]	X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH FMN, AND SUBUNIT. DOI=10.1021/bi010938k; PubMed=11502180 [NCBI, ExPASy, EBI, Israel, Japan] Sukumar N., Xu Y., Gatti D.L., Mitra B., Mathews F.S.; "Structure of an active soluble mutant of the membrane-associated (S)-mandelate dehydrogenase."; Biochemistry 40:9870-9878(2001).
[3]	X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN COMPLEX WITH FMN, AND SUBUNIT. DOI=10.1074/jbc.M310049200; PubMed=14604988 [NCBI, ExPASy, EBI, Israel, Japan] Sukumar N., Dewanti A.R., Mitra B., Mathews F.S.; "High resolution structures of an oxidized and reduced flavoprotein. The water switch in a soluble form of (S)-mandelate dehydrogenase."; J. Biol. Chem. 279:3749-3757(2004).

Comments

FUNCTION: Reduction of (S)-mandelate to benzoylformate.
CATALYTIC ACTIVITY: (S)-2-hydroxy-2-phenylacetate + acceptor = 2-oxo-2-phenylacetate + reduced acceptor.
COFACTOR: FMN.
PATHWAY: Aromatic compound metabolism; mandelic acid degradation; benzoic acid from (R)-mandelic acid: step 2/4 .
SUBUNIT: Homotetramer.
SUBCELLULAR LOCATION: Membrane.
SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.
SIMILARITY: Contains 1 FMN hydroxy acid dehydrogenase domain.

Copyright

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

Cross-references

Sequence databases

EMBL

AY143338; AAC15503.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B44767; B44767.

3D structure databases

PDB

1HUV; X-ray; 2.15 A; A=1-393.	[ExPASy / RCSB / EBI]
1P4C; X-ray; 1.35 A; A=1-393.	[ExPASy / RCSB / EBI]
1P5B; X-ray; 1.35 A; A=1-393.	[ExPASy / RCSB / EBI]
2A7N; X-ray; 1.80 A; A=1-393.	[ExPASy / RCSB / EBI]
2A7P; X-ray; 2.20 A; A=1-393.	[ExPASy / RCSB / EBI]
2A85; X-ray; 2.50 A; A=1-393.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1HUV; -.
1P4C; -.
1P5B; -.
2A7N; -.
2A7P; -.
2A85; -.

ModBase

P20932.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-2422; -.

Ontologies

GO:0033720;	Molecular function: (S)-mandelate dehydrogenase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR013785; Aldolase_TIM.
IPR012133; Alpha_OHA_DHase_FMN.
IPR008259; FMN_hydac_DHase_AS.
IPR000262; FMN_OHA_DHase.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.70; Aldolase_TIM; 1.

Pfam

PF01070; FMN_dh; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000138; Al-hdrx_acd_dh; 1.

PROSITE

PS00557; FMN_HYDROXY_ACID_DH_1; 1.
PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PROSITE graphical view of domain structure (profiles).

Other

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

Keywords

3D-structure; Aromatic hydrocarbons catabolism; Direct protein sequencing; Flavoprotein; FMN; Mandelate pathway; Membrane; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 393`	`393`	`(S)-mandelate dehydrogenase.`	`PRO_0000206327`
`DOMAIN`	`1 377`	`377`	`FMN hydroxy acid dehydrogenase.`
`NP_BIND`	`303 327`	`25`	`FMN.`
`ACT_SITE`	`274 274`		`Proton acceptor (By similarity).`
`BINDING`	`26 26`		`Substrate (Potential).`
`BINDING`	`108 108`		`FMN.`
`BINDING`	`129 129`		`FMN.`
`BINDING`	`131 131`		`Substrate (By similarity).`
`BINDING`	`156 156`		`FMN.`
`BINDING`	`165 165`		`Substrate (By similarity).`
`BINDING`	`250 250`		`FMN.`
`BINDING`	`277 277`		`Substrate (Potential).`
`HELIX`	`8 18`	`11`
`HELIX`	`21 28`	`8`
`HELIX`	`35 42`	`8`
`HELIX`	`43 46`	`4`
`STRAND`	`47 49`	`3`
`STRAND`	`64 66`	`3`
`STRAND`	`69 77`	`9`
`HELIX`	`83 85`	`3`
`HELIX`	`90 101`	`12`
`STRAND`	`105 107`	`3`
`HELIX`	`115 121`	`7`
`STRAND`	`126 130`	`5`
`HELIX`	`135 147`	`13`
`STRAND`	`152 156`	`5`
`HELIX`	`166 171`	`6`
`HELIX`	`182 184`	`3`
`TURN`	`214 218`	`5`
`HELIX`	`219 222`	`4`
`HELIX`	`233 242`	`10`
`STRAND`	`245 252`	`8`
`HELIX`	`255 263`	`9`
`STRAND`	`267 271`	`5`
`HELIX`	`274 276`	`3`
`HELIX`	`285 287`	`3`
`HELIX`	`289 296`	`8`
`STRAND`	`300 302`	`3`
`HELIX`	`309 317`	`9`
`STRAND`	`323 326`	`4`
`HELIX`	`327 359`	`33`
`HELIX`	`364 366`	`3`
`HELIX`	`369 371`	`3`
`STRAND`	`372 374`	`3`

Sequence information

Length: 393 AA [This is the length of the unprocessed precursor]

Molecular weight: 43437 Da [This is the MW of the unprocessed precursor]

CRC64: 18BE23E459BB3987 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSQNLFNVED YRKLRQKRLP KMVYDYLEGG AEDEYGVKHN RDVFQQWRFK PKRLVDVSRR 

        70         80         90        100        110        120 
SLQAEVLGKR QSMPLLIGPT GLNGALWPKG DLALARAATK AGIPFVLSTA SNMSIEDLAR 

       130        140        150        160        170        180 
QCDGDLWFQL YVIHREIAQG MVLKALHTGY TTLVLTTDVA VNGYRERDLH NRFKIPMSYS 

       190        200        210        220        230        240 
AKVVLDGCLH PRWSLDFVRH GMPQLANFVS SQTSSLEMQA ALMSRQMDAS FNWEALRWLR 

       250        260        270        280        290        300 
DLWPHKLLVK GLLSAEDADR CIAEGADGVI LSNHGGRQLD CAISPMEVLA QSVAKTGKPV 

       310        320        330        340        350        360 
LIDSGFRRGS DIVKALALGA EAVLLGRATL YGLAARGETG VDEVLTLLKA DIDRTLAQIG 

       370        380        390 
CPDITSLSPD YLQNEGVTNT APVDHLIGKG THA

P20932 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