[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Wistar; TISSUE=Kidney; PubMed=8508789 [NCBI, ExPASy, EBI, Israel, Japan] Belmouden A., Le K.H.D., Lederer F., Garchon H.J.; "Molecular cloning and nucleotide sequence of cDNA encoding rat kidney long-chain L-2-hydroxy acid oxidase. Expression of the catalytically active recombinant protein as a chimaera."; Eur. J. Biochem. 214:17-25(1993).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Testis; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[3]	PROTEIN SEQUENCE OF 2-353. TISSUE=Kidney; PubMed=1939137 [NCBI, ExPASy, EBI, Israel, Japan] Le K.H.D., Lederer F.; "Amino acid sequence of long chain alpha-hydroxy acid oxidase from rat kidney, a member of the family of FMN-dependent alpha-hydroxy acid-oxidizing enzymes."; J. Biol. Chem. 266:20877-20881(1991).
[4]	PROTEIN SEQUENCE OF 2-41, AND CHARACTERIZATION. DOI=10.1021/bi00419a029; PubMed=3061453 [NCBI, ExPASy, EBI, Israel, Japan] Urban P., Chirat I., Lederer F.; "Rat kidney L-2-hydroxyacid oxidase. Structural and mechanistic comparison with flavocytochrome b2 from baker's yeast."; Biochemistry 27:7365-7371(1988).
[5]	X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH FMN AND SUBSTRATE ANALOG, AND SUBUNIT. DOI=10.1021/bi048616e; PubMed=15683236 [NCBI, ExPASy, EBI, Israel, Japan] Cunane L.M., Barton J.D., Chen Z.-W., Le K.H.D., Amar D., Lederer F., Mathews F.S.; "Crystal structure analysis of recombinant rat kidney long chain hydroxy acid oxidase."; Biochemistry 44:1521-1531(2005).

Comments

FUNCTION: Catalyzes the oxidation of L-alpha-hydroxy acids as well as, more slowly, that of L-alpha-amino acids.
CATALYTIC ACTIVITY: (S)-2-hydroxy acid + O₂ = 2-oxo acid + H₂O₂.
COFACTOR: FMN.
SUBUNIT: Homotetramer or homooctamer.
SUBCELLULAR LOCATION: Peroxisome.
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

X67156; CAA47629.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC078781; AAH78781.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S33322; S33322.

NP_114471.1; -.

3D structure databases

PDB

1TB3; X-ray; 2.30 A; A/B/C/D/E/F/G/H=1-353.

[ExPASy / RCSB / EBI]

PDBsum

1TB3; -.

ModBase

Q07523.

Organism-specific databases

RGD

70972; Hao2.

Gene expression databases

ArrayExpress

Q07523; -.

GermOnline

ENSRNOG00000019470; Rattus norvegicus.

Ontologies

GO:0005777;	Cellular component: peroxisome (inferred from direct assay from HGNC).
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).

BLOCKS

Q07523.

Genome annotation databases

Ensembl

ENSRNOG00000019470; Rattus norvegicus. [Contig view]

GeneID

84029; -.

KEGG

rno:84029; -.

Phylogenomic databases

HOVERGEN

Q07523; -.

Other

ProtoNet

Q07523.

UniRef

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

Keywords

3D-structure; Direct protein sequencing; Flavoprotein; FMN; Oxidoreductase; Peroxisome.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 353`	`352`	`Hydroxyacid oxidase 2.`	`PRO_0000206322`
`DOMAIN`	`2 353`	`352`	`FMN hydroxy acid dehydrogenase.`
`NP_BIND`	`279 303`	`25`	`FMN.`
`MOTIF`	`351 353`	`3`	`Microbody targeting signal (Potential).`
`ACT_SITE`	`248 248`		`Proton acceptor (By similarity).`
`BINDING`	`106 106`		`FMN.`
`BINDING`	`128 128`		`FMN.`
`BINDING`	`130 130`		`Substrate.`
`BINDING`	`156 156`		`FMN.`
`BINDING`	`165 165`		`Substrate.`
`BINDING`	`224 224`		`FMN.`
`BINDING`	`251 251`		`Substrate (Potential).`
`HELIX`	`6 15`	`10`
`HELIX`	`19 26`	`8`
`HELIX`	`33 44`	`12`
`STRAND`	`62 64`	`3`
`STRAND`	`67 75`	`9`
`HELIX`	`81 83`	`3`
`TURN`	`86 88`	`3`
`HELIX`	`89 99`	`11`
`STRAND`	`103 105`	`3`
`HELIX`	`113 119`	`7`
`STRAND`	`125 128`	`4`
`HELIX`	`137 148`	`12`
`STRAND`	`153 156`	`4`
`HELIX`	`166 170`	`5`
`HELIX`	`207 214`	`8`
`STRAND`	`221 226`	`6`
`HELIX`	`229 237`	`9`
`STRAND`	`241 245`	`5`
`HELIX`	`248 250`	`3`
`HELIX`	`259 270`	`12`
`STRAND`	`273 281`	`9`
`HELIX`	`285 293`	`9`
`STRAND`	`299 302`	`4`
`HELIX`	`303 335`	`33`
`HELIX`	`340 342`	`3`
`HELIX`	`345 347`	`3`

Sequence information

Length: 353 AA [This is the length of the unprocessed precursor]

Molecular weight: 39201 Da [This is the MW of the unprocessed precursor]

CRC64: A2FDD4BF34E269E5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPLVCLADFK AHAQKQLSKT SWDFIEGEAD DGITYSENIA AFKRIRLRPR YLRDMSKVDT 

        70         80         90        100        110        120 
RTTIQGQEIS APICISPTAF HSIAWPDGEK STARAAQEAN ICYVISSYAS YSLEDIVAAA 

       130        140        150        160        170        180 
PEGFRWFQLY MKSDWDFNKQ MVQRAEALGF KALVITIDTP VLGNRRRDKR NQLNLEANIL 

       190        200        210        220        230        240 
LKDLRALKEE KPTQSVPVSF PKASFCWNDL SLLQSITRLP IILKGILTKE DAELAMKHNV 

       250        260        270        280        290        300 
QGIVVSNHGG RQLDEVSASI DALREVVAAV KGKIEVYMDG GVRTGTDVLK ALALGARCIF 

       310        320        330        340        350 
LGRPILWGLA CKGEDGVKEV LDILTAELHR CMTLSGCQSV AEISPDLIQF SRL

Q07523 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