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Reviewed, UniProtKB/Swiss-Prot Q07523 (HAOX2_RAT)

Last modified November 25, 2008. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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)
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 + O(2) = 2-oxo acid + H(2)O(2).

Cofactor

FMN.

Subunit structure

Homotetramer or homooctamer.

Subcellular location

Peroxisome.

Sequence similarities

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

Contains 1 FMN hydroxy acid dehydrogenase domain.

Ontologies

Keywords

   Cellular componentPeroxisome
   LigandFMN
Flavoprotein
   Molecular functionOxidoreductase
   Technical term3D-structure
Direct protein sequencing

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperoxisome

Inferred from direct assay. Source: HGNC

   Molecular function(S)-2-hydroxy-acid oxidase activity

Inferred from electronic annotation. Source: EC

FMN binding

Inferred from electronic annotation. Source: InterPro

electron carrier activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
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 Potential

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Q07523-1 [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: 8508789] [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: 15489334] [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: 1939137] [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: 3061453] [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: 15683236] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH FMN AND SUBSTRATE ANALOG, SUBUNIT.

Cross-references

Sequence databases

X67156 mRNA. Translation: CAA47629.1.
BC078781 mRNA. Translation: AAH78781.1.
PIRS33322.
RefSeqNP_114471.1.
UniGeneRn.198611

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1TB3X-ray2.30A/B/C/D/E/F/G/H1-353[»]
ModBaseSearch...

Genome annotation databases

EnsemblENSRNOG00000019470. Rattus norvegicus. [Contig view]
GeneID84029.
KEGGrno:84029.

Organism-specific databases

RGD70972. Hao2.

Phylogenomic databases

HOVERGENQ07523.

Gene expression databases

ArrayExpressQ07523.
GermOnlineENSRNOG00000019470. Rattus norvegicus.

Family and domain databases

InterProIPR013785. Aldolase_TIM.
IPR012133. Alpha_OHA_DHase_FMN.
IPR008259. FMN_hydac_DHase_AS.
IPR000262. FMN_OHA_DHase.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
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 Resources

NextBio616611.

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: November 25, 2008
This is version 70 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents