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Protein

Hydroxyacid oxidase 1

Gene

HAO1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has 2-hydroxyacid oxidase activity. Most active on the 2-carbon substrate glycolate, but is also active on 2-hydroxy fatty acids, with high activity towards 2-hydroxy palmitate and 2-hydroxy octanoate.1 Publication

Catalytic activityi

(S)-2-hydroxy acid + O2 = 2-oxo acid + H2O2.1 Publication

Cofactori

FMNPROSITE-ProRule annotation1 Publication

Kineticsi

  1. KM=141 µM for glycolate1 Publication
  2. KM=40 µM for 2-hydroxy octanoate1 Publication
  3. KM=2200 µM for glyoxylate1 Publication

    Pathwayi: glycolate degradation

    This protein is involved in step 1 of the subpathway that synthesizes 3-phospho-D-glycerate from glycolate.
    Proteins known to be involved in the 4 steps of the subpathway in this organism are:
    1. Hydroxyacid oxidase 1 (HAO1)
    2. no protein annotated in this organism
    3. no protein annotated in this organism
    4. no protein annotated in this organism
    This subpathway is part of the pathway glycolate degradation, which is itself part of Organic acid metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes 3-phospho-D-glycerate from glycolate, the pathway glycolate degradation and in Organic acid metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei26Substrate1
    Binding sitei108FMNPROSITE-ProRule annotation3 Publications1
    Binding sitei130FMNPROSITE-ProRule annotation3 Publications1
    Binding sitei132FMNPROSITE-ProRule annotation3 Publications1
    Binding sitei132Substrate1
    Binding sitei158FMNPROSITE-ProRule annotation3 Publications1
    Binding sitei167Substrate1
    Binding sitei236FMNPROSITE-ProRule annotation3 Publications1
    Binding sitei258FMNPROSITE-ProRule annotation3 Publications1
    Active sitei260Proton acceptor1
    Binding sitei263Substrate1
    Binding sitei315FMNPROSITE-ProRule annotation3 Publications1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi291 – 315FMNPROSITE-ProRule annotationAdd BLAST25
    Nucleotide bindingi291 – 295FMN bindingPROSITE-ProRule annotation3 Publications5

    GO - Molecular functioni

    • (S)-2-hydroxy-acid oxidase activity Source: UniProtKB
    • FMN binding Source: UniProtKB
    • glycolate oxidase activity Source: UniProtKB
    • glyoxylate oxidase activity Source: Reactome
    • long-chain-(S)-2-hydroxy-long-chain-acid oxidase activity Source: UniProtKB-EC
    • medium-chain-(S)-2-hydroxy-acid oxidase activity Source: UniProtKB-EC
    • receptor binding Source: UniProtKB
    • very-long-chain-(S)-2-hydroxy-acid oxidase activity Source: UniProtKB-EC

    GO - Biological processi

    • fatty acid alpha-oxidation Source: UniProtKB
    • glycolate catabolic process Source: UniProtKB
    • glyoxylate metabolic process Source: Reactome
    • response to oxidative stress Source: Ensembl
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Flavoprotein, FMN

    Enzyme and pathway databases

    BioCyciZFISH:HS02241-MONOMER.
    BRENDAi1.1.3.15. 2681.
    ReactomeiR-HSA-389661. Glyoxylate metabolism and glycine degradation.
    SABIO-RKQ9UJM8.
    UniPathwayiUPA00864; UER00830.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hydroxyacid oxidase 1 (EC:1.1.3.15)
    Short name:
    HAOX1
    Alternative name(s):
    Glycolate oxidase
    Short name:
    GOX
    Gene namesi
    Name:HAO1
    Synonyms:GOX1, HAOX1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:4809. HAO1.

    Subcellular locationi

    GO - Cellular componenti

    • peroxisomal matrix Source: Reactome
    • peroxisome Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Peroxisome

    Pathology & Biotechi

    Organism-specific databases

    DisGeNETi54363.
    OpenTargetsiENSG00000101323.
    PharmGKBiPA29185.

    Chemistry databases

    ChEMBLiCHEMBL4229.

    Polymorphism and mutation databases

    BioMutaiHAO1.
    DMDMi13124294.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002063181 – 370Hydroxyacid oxidase 1Add BLAST370

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei184N6-succinyllysineBy similarity1
    Modified residuei194PhosphoserineBy similarity1
    Modified residuei230PhosphoserineCombined sources1

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9UJM8.
    PeptideAtlasiQ9UJM8.
    PRIDEiQ9UJM8.

    PTM databases

    iPTMnetiQ9UJM8.
    PhosphoSitePlusiQ9UJM8.

    Expressioni

    Tissue specificityi

    Liver.

    Gene expression databases

    BgeeiENSG00000101323.
    CleanExiHS_HAO1.
    ExpressionAtlasiQ9UJM8. baseline and differential.
    GenevisibleiQ9UJM8. HS.

    Organism-specific databases

    HPAiHPA049552.

    Interactioni

    GO - Molecular functioni

    • receptor binding Source: UniProtKB

    Protein-protein interaction databases

    BioGridi119941. 4 interactors.
    IntActiQ9UJM8. 1 interactor.
    STRINGi9606.ENSP00000368066.

    Chemistry databases

    BindingDBiQ9UJM8.

    Structurei

    Secondary structure

    1370
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi8 – 18Combined sources11
    Helixi21 – 28Combined sources8
    Helixi35 – 46Combined sources12
    Beta strandi47 – 49Combined sources3
    Beta strandi64 – 66Combined sources3
    Beta strandi69 – 77Combined sources9
    Helixi83 – 85Combined sources3
    Helixi90 – 101Combined sources12
    Beta strandi104 – 107Combined sources4
    Helixi115 – 121Combined sources7
    Beta strandi125 – 131Combined sources7
    Beta strandi134 – 136Combined sources3
    Helixi137 – 149Combined sources13
    Beta strandi155 – 158Combined sources4
    Helixi168 – 173Combined sources6
    Turni189 – 193Combined sources5
    Helixi205 – 212Combined sources8
    Helixi219 – 225Combined sources7
    Beta strandi233 – 238Combined sources6
    Helixi241 – 249Combined sources9
    Beta strandi254 – 257Combined sources4
    Helixi260 – 262Combined sources3
    Helixi271 – 282Combined sources12
    Beta strandi285 – 290Combined sources6
    Helixi297 – 305Combined sources9
    Beta strandi309 – 313Combined sources5
    Helixi315 – 346Combined sources32
    Helixi352 – 354Combined sources3
    Helixi357 – 359Combined sources3
    Beta strandi360 – 362Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2NZLX-ray1.35A1-370[»]
    2RDTX-ray1.95A1-370[»]
    2RDUX-ray1.65A1-370[»]
    2RDWX-ray1.95A1-370[»]
    2W0UX-ray2.84A/B/C/D1-370[»]
    ProteinModelPortaliQ9UJM8.
    SMRiQ9UJM8.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UJM8.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini1 – 365FMN hydroxy acid dehydrogenasePROSITE-ProRule annotationAdd BLAST365

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Motifi368 – 370Microbody targeting signalSequence analysis3

    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

    eggNOGiKOG0538. Eukaryota.
    COG1304. LUCA.
    GeneTreeiENSGT00390000018717.
    HOGENOMiHOG000217463.
    HOVERGENiHBG051881.
    InParanoidiQ9UJM8.
    KOiK11517.
    OMAiQKSVYDY.
    OrthoDBiEOG091G0ADA.
    PhylomeDBiQ9UJM8.
    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.

    Q9UJM8-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MLPRLICIND YEQHAKSVLP KSIYDYYRSG ANDEETLADN IAAFSRWKLY
    60 70 80 90 100
    PRMLRNVAET DLSTSVLGQR VSMPICVGAT AMQRMAHVDG ELATVRACQS
    110 120 130 140 150
    LGTGMMLSSW ATSSIEEVAE AGPEALRWLQ LYIYKDREVT KKLVRQAEKM
    160 170 180 190 200
    GYKAIFVTVD TPYLGNRLDD VRNRFKLPPQ LRMKNFETST LSFSPEENFG
    210 220 230 240 250
    DDSGLAAYVA KAIDPSISWE DIKWLRRLTS LPIVAKGILR GDDAREAVKH
    260 270 280 290 300
    GLNGILVSNH GARQLDGVPA TIDVLPEIVE AVEGKVEVFL DGGVRKGTDV
    310 320 330 340 350
    LKALALGAKA VFVGRPIVWG LAFQGEKGVQ DVLEILKEEF RLAMALSGCQ
    360 370
    NVKVIDKTLV RKNPLAVSKI
    Length:370
    Mass (Da):40,924
    Last modified:May 1, 2000 - v1
    Checksum:iC683C6F7CB5FD323
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF244134 mRNA. Translation: AAF63219.1.
    AF231916 mRNA. Translation: AAF40199.1.
    AL121739 mRNA. Translation: CAB57329.1.
    AB024079 mRNA. Translation: BAA82872.1.
    AL021879 Genomic DNA. Translation: CAC34364.1.
    BC113665 mRNA. Translation: AAI13666.1.
    BC113667 mRNA. Translation: AAI13668.1.
    CCDSiCCDS13100.1.
    RefSeqiNP_060015.1. NM_017545.2.
    UniGeneiHs.193640.

    Genome annotation databases

    EnsembliENST00000378789; ENSP00000368066; ENSG00000101323.
    GeneIDi54363.
    KEGGihsa:54363.
    UCSCiuc002wmw.2. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF244134 mRNA. Translation: AAF63219.1.
    AF231916 mRNA. Translation: AAF40199.1.
    AL121739 mRNA. Translation: CAB57329.1.
    AB024079 mRNA. Translation: BAA82872.1.
    AL021879 Genomic DNA. Translation: CAC34364.1.
    BC113665 mRNA. Translation: AAI13666.1.
    BC113667 mRNA. Translation: AAI13668.1.
    CCDSiCCDS13100.1.
    RefSeqiNP_060015.1. NM_017545.2.
    UniGeneiHs.193640.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2NZLX-ray1.35A1-370[»]
    2RDTX-ray1.95A1-370[»]
    2RDUX-ray1.65A1-370[»]
    2RDWX-ray1.95A1-370[»]
    2W0UX-ray2.84A/B/C/D1-370[»]
    ProteinModelPortaliQ9UJM8.
    SMRiQ9UJM8.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi119941. 4 interactors.
    IntActiQ9UJM8. 1 interactor.
    STRINGi9606.ENSP00000368066.

    Chemistry databases

    BindingDBiQ9UJM8.
    ChEMBLiCHEMBL4229.

    PTM databases

    iPTMnetiQ9UJM8.
    PhosphoSitePlusiQ9UJM8.

    Polymorphism and mutation databases

    BioMutaiHAO1.
    DMDMi13124294.

    Proteomic databases

    PaxDbiQ9UJM8.
    PeptideAtlasiQ9UJM8.
    PRIDEiQ9UJM8.

    Protocols and materials databases

    DNASUi54363.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000378789; ENSP00000368066; ENSG00000101323.
    GeneIDi54363.
    KEGGihsa:54363.
    UCSCiuc002wmw.2. human.

    Organism-specific databases

    CTDi54363.
    DisGeNETi54363.
    GeneCardsiHAO1.
    HGNCiHGNC:4809. HAO1.
    HPAiHPA049552.
    MIMi605023. gene.
    neXtProtiNX_Q9UJM8.
    OpenTargetsiENSG00000101323.
    PharmGKBiPA29185.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG0538. Eukaryota.
    COG1304. LUCA.
    GeneTreeiENSGT00390000018717.
    HOGENOMiHOG000217463.
    HOVERGENiHBG051881.
    InParanoidiQ9UJM8.
    KOiK11517.
    OMAiQKSVYDY.
    OrthoDBiEOG091G0ADA.
    PhylomeDBiQ9UJM8.
    TreeFamiTF313363.

    Enzyme and pathway databases

    UniPathwayiUPA00864; UER00830.
    BioCyciZFISH:HS02241-MONOMER.
    BRENDAi1.1.3.15. 2681.
    ReactomeiR-HSA-389661. Glyoxylate metabolism and glycine degradation.
    SABIO-RKQ9UJM8.

    Miscellaneous databases

    EvolutionaryTraceiQ9UJM8.
    GenomeRNAii54363.
    PROiQ9UJM8.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000101323.
    CleanExiHS_HAO1.
    ExpressionAtlasiQ9UJM8. baseline and differential.
    GenevisibleiQ9UJM8. HS.

    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]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiHAOX1_HUMAN
    AccessioniPrimary (citable) accession number: Q9UJM8
    Secondary accession number(s): Q14CQ0, Q9UPZ0, Q9Y3I7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: May 1, 2000
    Last modified: November 2, 2016
    This is version 147 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.