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Q07523

- HAOX2_RAT

UniProt

Q07523 - HAOX2_RAT

Protein

Hydroxyacid oxidase 2

Gene

Hao2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the oxidation of L-alpha-hydroxy acids as well as, more slowly, that of L-alpha-amino acids.

    Catalytic activityi

    (S)-2-hydroxy acid + O2 = 2-oxo acid + H2O2.

    Cofactori

    FMN.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei106 – 1061FMN1 PublicationPROSITE-ProRule annotation
    Binding sitei128 – 1281FMN1 PublicationPROSITE-ProRule annotation
    Binding sitei130 – 1301Substrate
    Binding sitei156 – 1561FMN1 PublicationPROSITE-ProRule annotation
    Binding sitei165 – 1651Substrate
    Binding sitei224 – 2241FMN1 PublicationPROSITE-ProRule annotation
    Active sitei248 – 2481Proton acceptorPROSITE-ProRule annotation
    Binding sitei251 – 2511SubstratePROSITE-ProRule annotation
    Binding sitei303 – 3031FMN1 PublicationPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi279 – 30325FMN1 PublicationPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. (S)-2-hydroxy-acid oxidase activity Source: RGD
    2. FMN binding Source: RGD
    3. long-chain-(S)-2-hydroxy-long-chain-acid oxidase activity Source: UniProtKB-EC
    4. medium-chain-(S)-2-hydroxy-acid oxidase activity Source: UniProtKB-EC
    5. very-long-chain-(S)-2-hydroxy-acid oxidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. fatty acid oxidation Source: Ensembl
    2. mandelate metabolic process Source: RGD
    3. protein homooligomerization Source: RGD

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Flavoprotein, FMN

    Enzyme and pathway databases

    SABIO-RKQ07523.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hydroxyacid oxidase 2 (EC:1.1.3.15)
    Short name:
    HAOX2
    Alternative name(s):
    (S)-2-hydroxy-acid oxidase, peroxisomal
    Long chain alpha-hydroxy acid oxidase
    Long-chain L-2-hydroxy acid oxidase
    Gene namesi
    Name:Hao2
    Synonyms:Hao3, Haox2
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 2

    Organism-specific databases

    RGDi70972. Hao2.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrion Source: Ensembl
    2. peroxisome Source: HGNC

    Keywords - Cellular componenti

    Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 353352Hydroxyacid oxidase 2PRO_0000206322Add
    BLAST

    Proteomic databases

    PaxDbiQ07523.
    PRIDEiQ07523.

    PTM databases

    PhosphoSiteiQ07523.

    Miscellaneous databases

    PMAP-CutDBQ07523.

    Expressioni

    Gene expression databases

    GenevestigatoriQ07523.

    Interactioni

    Subunit structurei

    Homotetramer or homooctamer.1 Publication

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000040223.

    Structurei

    Secondary structure

    1
    353
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 1510
    Helixi19 – 268
    Helixi33 – 4311
    Beta strandi62 – 643
    Beta strandi67 – 759
    Helixi81 – 833
    Helixi88 – 9912
    Beta strandi102 – 1054
    Helixi113 – 1197
    Beta strandi124 – 1285
    Helixi135 – 14713
    Beta strandi153 – 1564
    Helixi166 – 1749
    Helixi177 – 1804
    Helixi207 – 21610
    Beta strandi221 – 2266
    Helixi229 – 2379
    Beta strandi241 – 2455
    Helixi248 – 2503
    Helixi259 – 27012
    Beta strandi273 – 2819
    Helixi285 – 2939
    Beta strandi297 – 3026
    Helixi303 – 33533
    Helixi340 – 3423
    Helixi345 – 3473
    Beta strandi348 – 3503

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TB3X-ray2.30A/B/C/D/E/F/G/H2-353[»]
    3SGZX-ray1.35A/B/C2-353[»]
    ProteinModelPortaliQ07523.
    SMRiQ07523. Positions 2-350.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ07523.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 353352FMN hydroxy acid dehydrogenasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi351 – 3533Microbody targeting signalSequence Analysis

    Sequence similaritiesi

    Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.PROSITE-ProRule annotation
    Contains 1 FMN hydroxy acid dehydrogenase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG1304.
    GeneTreeiENSGT00390000018717.
    HOGENOMiHOG000217463.
    HOVERGENiHBG051881.
    InParanoidiQ07523.
    KOiK11517.
    OMAiTAFHSIA.
    OrthoDBiEOG7B5WW0.
    PhylomeDBiQ07523.
    TreeFamiTF313363.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR012133. Alpha-hydoxy_acid_DH_FMN.
    IPR000262. FMN-dep_DH.
    IPR008259. FMN_hydac_DH_AS.
    [Graphical view]
    PfamiPF01070. FMN_dh. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000138. Al-hdrx_acd_dh. 1 hit.
    PROSITEiPS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
    PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q07523-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPLVCLADFK AHAQKQLSKT SWDFIEGEAD DGITYSENIA AFKRIRLRPR    50
    YLRDMSKVDT RTTIQGQEIS APICISPTAF HSIAWPDGEK STARAAQEAN 100
    ICYVISSYAS YSLEDIVAAA PEGFRWFQLY MKSDWDFNKQ MVQRAEALGF 150
    KALVITIDTP VLGNRRRDKR NQLNLEANIL LKDLRALKEE KPTQSVPVSF 200
    PKASFCWNDL SLLQSITRLP IILKGILTKE DAELAMKHNV QGIVVSNHGG 250
    RQLDEVSASI DALREVVAAV KGKIEVYMDG GVRTGTDVLK ALALGARCIF 300
    LGRPILWGLA CKGEDGVKEV LDILTAELHR CMTLSGCQSV AEISPDLIQF 350
    SRL 353
    Length:353
    Mass (Da):39,201
    Last modified:January 23, 2007 - v2
    Checksum:iA2FDD4BF34E269E5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X67156 mRNA. Translation: CAA47629.1.
    BC078781 mRNA. Translation: AAH78781.1.
    PIRiS33322.
    RefSeqiNP_114471.1. NM_032082.2.
    UniGeneiRn.198611.

    Genome annotation databases

    EnsembliENSRNOT00000046942; ENSRNOP00000040223; ENSRNOG00000019470.
    GeneIDi84029.
    KEGGirno:84029.
    UCSCiRGD:70972. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X67156 mRNA. Translation: CAA47629.1 .
    BC078781 mRNA. Translation: AAH78781.1 .
    PIRi S33322.
    RefSeqi NP_114471.1. NM_032082.2.
    UniGenei Rn.198611.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1TB3 X-ray 2.30 A/B/C/D/E/F/G/H 2-353 [» ]
    3SGZ X-ray 1.35 A/B/C 2-353 [» ]
    ProteinModelPortali Q07523.
    SMRi Q07523. Positions 2-350.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000040223.

    Chemistry

    ChEMBLi CHEMBL2021745.

    PTM databases

    PhosphoSitei Q07523.

    Proteomic databases

    PaxDbi Q07523.
    PRIDEi Q07523.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000046942 ; ENSRNOP00000040223 ; ENSRNOG00000019470 .
    GeneIDi 84029.
    KEGGi rno:84029.
    UCSCi RGD:70972. rat.

    Organism-specific databases

    CTDi 51179.
    RGDi 70972. Hao2.

    Phylogenomic databases

    eggNOGi COG1304.
    GeneTreei ENSGT00390000018717.
    HOGENOMi HOG000217463.
    HOVERGENi HBG051881.
    InParanoidi Q07523.
    KOi K11517.
    OMAi TAFHSIA.
    OrthoDBi EOG7B5WW0.
    PhylomeDBi Q07523.
    TreeFami TF313363.

    Enzyme and pathway databases

    SABIO-RK Q07523.

    Miscellaneous databases

    EvolutionaryTracei Q07523.
    NextBioi 616611.
    PMAP-CutDB Q07523.
    PROi Q07523.

    Gene expression databases

    Genevestigatori Q07523.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    InterProi IPR013785. Aldolase_TIM.
    IPR012133. Alpha-hydoxy_acid_DH_FMN.
    IPR000262. FMN-dep_DH.
    IPR008259. FMN_hydac_DH_AS.
    [Graphical view ]
    Pfami PF01070. FMN_dh. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000138. Al-hdrx_acd_dh. 1 hit.
    PROSITEi PS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
    PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiHAOX2_RAT
    AccessioniPrimary (citable) accession number: Q07523
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 113 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3