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Q07523 (HAOX2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hydroxyacid oxidase 2

Short name=HAOX2
EC=1.1.3.15
Alternative name(s):
(S)-2-hydroxy-acid oxidase, peroxisomal
Long chain alpha-hydroxy acid oxidase
Long-chain L-2-hydroxy acid oxidase
Gene names
Name:Hao2
Synonyms:Hao3, Haox2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length353 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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 structure

Homotetramer or homooctamer. Ref.5

Subcellular location

Peroxisome.

Sequence similarities

Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.

Contains 1 FMN hydroxy acid dehydrogenase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3 Ref.4
Chain2 – 353352Hydroxyacid oxidase 2
PRO_0000206322

Regions

Domain2 – 353352FMN hydroxy acid dehydrogenase
Nucleotide binding279 – 30325FMN
Motif351 – 3533Microbody targeting signal Potential

Sites

Active site2481Proton acceptor By similarity
Binding site1061FMN
Binding site1281FMN
Binding site1301Substrate
Binding site1561FMN
Binding site1651Substrate
Binding site2241FMN
Binding site2511Substrate By similarity
Binding site3031FMN

Secondary structure

..................................................... 353
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q07523 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: A2FDD4BF34E269E5

FASTA35339,201
        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 

« Hide

References

« Hide 'large scale' references
[1]"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."
Belmouden A., Le K.H.D., Lederer F., Garchon H.J.
Eur. J. Biochem. 214:17-25(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Kidney.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[3]"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."
Le K.H.D., Lederer F.
J. Biol. Chem. 266:20877-20881(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-353.
Tissue: Kidney.
[4]"Rat kidney L-2-hydroxyacid oxidase. Structural and mechanistic comparison with flavocytochrome b2 from baker's yeast."
Urban P., Chirat I., Lederer F.
Biochemistry 27:7365-7371(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-41, CHARACTERIZATION.
[5]"Crystal structure analysis of recombinant rat kidney long chain hydroxy acid oxidase."
Cunane L.M., Barton J.D., Chen Z.-W., Le K.H.D., Amar D., Lederer F., Mathews F.S.
Biochemistry 44:1521-1531(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH FMN AND SUBSTRATE ANALOG, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X67156 mRNA. Translation: CAA47629.1.
BC078781 mRNA. Translation: AAH78781.1.
PIRS33322.
RefSeqNP_114471.1. NM_032082.2.
UniGeneRn.198611.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TB3X-ray2.30A/B/C/D/E/F/G/H2-353[»]
3SGZX-ray1.35A/B/C2-353[»]
ProteinModelPortalQ07523.
SMRQ07523. Positions 2-350.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000040223.

Chemistry

ChEMBLCHEMBL2021745.

PTM databases

PhosphoSiteQ07523.

Proteomic databases

PaxDbQ07523.
PRIDEQ07523.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000046942; ENSRNOP00000040223; ENSRNOG00000019470.
GeneID84029.
KEGGrno:84029.
UCSCRGD:70972. rat.

Organism-specific databases

CTD51179.
RGD70972. Hao2.

Phylogenomic databases

eggNOGCOG1304.
GeneTreeENSGT00390000018717.
HOGENOMHOG000217463.
HOVERGENHBG051881.
InParanoidQ07523.
KOK11517.
OMATAFHSIA.
OrthoDBEOG7B5WW0.
PhylomeDBQ07523.
TreeFamTF313363.

Enzyme and pathway databases

SABIO-RKQ07523.

Gene expression databases

GenevestigatorQ07523.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR012133. Alpha-hydoxy_acid_DH_FMN.
IPR000262. FMN-dep_DH.
IPR008259. FMN_hydac_DH_AS.
[Graphical view]
PfamPF01070. FMN_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000138. Al-hdrx_acd_dh. 1 hit.
PROSITEPS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ07523.
NextBio616611.
PMAP-CutDBQ07523.
PROQ07523.

Entry information

Entry nameHAOX2_RAT
AccessionPrimary (citable) accession number: Q07523
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references