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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

    Pathway:iglycolate 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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei26 – 261Substrate
    Binding sitei108 – 1081FMNPROSITE-ProRule annotation3 Publications
    Binding sitei130 – 1301FMNPROSITE-ProRule annotation3 Publications
    Binding sitei132 – 1321FMNPROSITE-ProRule annotation3 Publications
    Binding sitei132 – 1321Substrate
    Binding sitei158 – 1581FMNPROSITE-ProRule annotation3 Publications
    Binding sitei167 – 1671Substrate
    Binding sitei236 – 2361FMNPROSITE-ProRule annotation3 Publications
    Binding sitei258 – 2581FMNPROSITE-ProRule annotation3 Publications
    Active sitei260 – 2601Proton acceptor
    Binding sitei263 – 2631Substrate
    Binding sitei315 – 3151FMNPROSITE-ProRule annotation3 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi291 – 31525FMNPROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi291 – 2955FMN bindingPROSITE-ProRule annotation3 Publications

    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

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Flavoprotein, FMN

    Enzyme and pathway databases

    BRENDAi1.1.3.15. 2681.
    ReactomeiREACT_16925. Glyoxylate metabolism.
    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
    ProteomesiUP000005640 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

    PharmGKBiPA29185.

    Polymorphism and mutation databases

    BioMutaiHAO1.
    DMDMi13124294.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 370370Hydroxyacid oxidase 1PRO_0000206318Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei184 – 1841N6-succinyllysineBy similarity
    Modified residuei194 – 1941PhosphoserineBy similarity
    Modified residuei230 – 2301Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9UJM8.
    PRIDEiQ9UJM8.

    PTM databases

    PhosphoSiteiQ9UJM8.

    Expressioni

    Tissue specificityi

    Liver.

    Gene expression databases

    BgeeiQ9UJM8.
    CleanExiHS_HAO1.
    ExpressionAtlasiQ9UJM8. baseline and differential.
    GenevisibleiQ9UJM8. HS.

    Organism-specific databases

    HPAiHPA049552.

    Interactioni

    Protein-protein interaction databases

    BioGridi119941. 4 interactions.
    IntActiQ9UJM8. 1 interaction.
    STRINGi9606.ENSP00000368066.

    Structurei

    Secondary structure

    1
    370
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 1811Combined sources
    Helixi21 – 288Combined sources
    Helixi35 – 4612Combined sources
    Beta strandi47 – 493Combined sources
    Beta strandi64 – 663Combined sources
    Beta strandi69 – 779Combined sources
    Helixi83 – 853Combined sources
    Helixi90 – 10112Combined sources
    Beta strandi104 – 1074Combined sources
    Helixi115 – 1217Combined sources
    Beta strandi125 – 1317Combined sources
    Beta strandi134 – 1363Combined sources
    Helixi137 – 14913Combined sources
    Beta strandi155 – 1584Combined sources
    Helixi168 – 1736Combined sources
    Turni189 – 1935Combined sources
    Helixi205 – 2128Combined sources
    Helixi219 – 2257Combined sources
    Beta strandi233 – 2386Combined sources
    Helixi241 – 2499Combined sources
    Beta strandi254 – 2574Combined sources
    Helixi260 – 2623Combined sources
    Helixi271 – 28212Combined sources
    Beta strandi285 – 2906Combined sources
    Helixi297 – 3059Combined sources
    Beta strandi309 – 3135Combined sources
    Helixi315 – 34632Combined sources
    Helixi352 – 3543Combined sources
    Helixi357 – 3593Combined sources
    Beta strandi360 – 3623Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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. Positions 3-362.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UJM8.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 365365FMN hydroxy acid dehydrogenasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi368 – 3703Microbody 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.
    InParanoidiQ9UJM8.
    KOiK11517.
    OMAiQKSVYDY.
    OrthoDBiEOG7B5WW0.
    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.1. 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
    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. Positions 3-362.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi119941. 4 interactions.
    IntActiQ9UJM8. 1 interaction.
    STRINGi9606.ENSP00000368066.

    Chemistry

    BindingDBiQ9UJM8.
    ChEMBLiCHEMBL4229.

    PTM databases

    PhosphoSiteiQ9UJM8.

    Polymorphism and mutation databases

    BioMutaiHAO1.
    DMDMi13124294.

    Proteomic databases

    PaxDbiQ9UJM8.
    PRIDEiQ9UJM8.

    Protocols and materials databases

    DNASUi54363.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000378789; ENSP00000368066; ENSG00000101323.
    GeneIDi54363.
    KEGGihsa:54363.
    UCSCiuc002wmw.1. human.

    Organism-specific databases

    CTDi54363.
    GeneCardsiGC20M007863.
    HGNCiHGNC:4809. HAO1.
    HPAiHPA049552.
    MIMi605023. gene.
    neXtProtiNX_Q9UJM8.
    PharmGKBiPA29185.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG1304.
    GeneTreeiENSGT00390000018717.
    HOGENOMiHOG000217463.
    HOVERGENiHBG051881.
    InParanoidiQ9UJM8.
    KOiK11517.
    OMAiQKSVYDY.
    OrthoDBiEOG7B5WW0.
    PhylomeDBiQ9UJM8.
    TreeFamiTF313363.

    Enzyme and pathway databases

    UniPathwayiUPA00864; UER00830.
    BRENDAi1.1.3.15. 2681.
    ReactomeiREACT_16925. Glyoxylate metabolism.
    SABIO-RKQ9UJM8.

    Miscellaneous databases

    EvolutionaryTraceiQ9UJM8.
    GenomeRNAii54363.
    NextBioi56605.
    PROiQ9UJM8.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9UJM8.
    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...

    Publicationsi

    « Hide 'large scale' publications
    1. "Identification and expression of a cDNA for human glycolate oxidase."
      Williams E.L., Cregeen D.P., Rumsby G.
      Biochim. Biophys. Acta 1493:246-248(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "Identification and characterization of HAOX1, HAOX2, and HAOX3, three human peroxisomal 2-hydroxy acid oxidases."
      Jones J.M., Morrell J.C., Gould S.J.
      J. Biol. Chem. 275:12590-12597(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. Stavrides G.S., Huckle E.J., Deloukas P.
      Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Isolation and characterization of a novel human liver-specific gene homologous to the plant glycolate oxidase by the differential display method."
      Watanabe T.
      Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Liver.
    7. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    8. "Active site and loop 4 movements within human glycolate oxidase: implications for substrate specificity and drug design."
      Murray M.S., Holmes R.P., Lowther W.T.
      Biochemistry 47:2439-2449(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH FMN; GLYOXYLATE AND 4-CARBOXY-5-DODECYLSULFANYL-1,2,3-TRIAZOLE, FUNCTION, COFACTOR, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    9. "Structure of human glycolate oxidase in complex with the inhibitor 4-carboxy-5-[(4-chlorophenyl)sulfanyl]-1,2,3-thiadiazole."
      Bourhis J.M., Vignaud C., Pietrancosta N., Gueritte F., Guenard D., Lederer F., Lindqvist Y.
      Acta Crystallogr. F 65:1246-1253(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.84 ANGSTROMS) IN COMPLEX WITH FMN AND THE SYNTHETIC INHIBITOR CCPST.
    10. "Crystal structure of human hydroxyacid oxidase 1."
      Structural genomics consortium (SGC)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN COMPLEX WITH FMN.

    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: July 22, 2015
    This is version 136 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

    External Data

    Dasty 3

    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 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.