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Q9UJM8

- HAOX1_HUMAN

UniProt

Q9UJM8 - HAOX1_HUMAN

Protein

Hydroxyacid oxidase 1

Gene

HAO1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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

    FMN.1 PublicationPROSITE-ProRule annotation

    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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei26 – 261Substrate
    Binding sitei108 – 1081FMN3 PublicationsPROSITE-ProRule annotation
    Binding sitei130 – 1301FMN3 PublicationsPROSITE-ProRule annotation
    Binding sitei132 – 1321FMN3 PublicationsPROSITE-ProRule annotation
    Binding sitei132 – 1321Substrate
    Binding sitei158 – 1581FMN3 PublicationsPROSITE-ProRule annotation
    Binding sitei167 – 1671Substrate
    Binding sitei236 – 2361FMN3 PublicationsPROSITE-ProRule annotation
    Binding sitei258 – 2581FMN3 PublicationsPROSITE-ProRule annotation
    Active sitei260 – 2601Proton acceptor
    Binding sitei263 – 2631Substrate
    Binding sitei315 – 3151FMN3 PublicationsPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi291 – 31525FMNPROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi291 – 2955FMN binding3 PublicationsPROSITE-ProRule annotation

    GO - Molecular functioni

    1. (S)-2-hydroxy-acid oxidase activity Source: UniProtKB
    2. FMN binding Source: UniProtKB
    3. glycolate oxidase activity Source: UniProtKB
    4. glyoxylate oxidase activity Source: Reactome
    5. long-chain-(S)-2-hydroxy-long-chain-acid oxidase activity Source: UniProtKB-EC
    6. medium-chain-(S)-2-hydroxy-acid oxidase activity Source: UniProtKB-EC
    7. receptor binding Source: UniProtKB
    8. very-long-chain-(S)-2-hydroxy-acid oxidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cellular nitrogen compound metabolic process Source: Reactome
    2. fatty acid alpha-oxidation Source: UniProtKB
    3. glycolate catabolic process Source: UniProtKB
    4. glyoxylate metabolic process Source: Reactome
    5. response to oxidative stress Source: Ensembl
    6. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Flavoprotein, FMN

    Enzyme and pathway databases

    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: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:4809. HAO1.

    Subcellular locationi

    GO - Cellular componenti

    1. peroxisomal matrix Source: Reactome
    2. peroxisome Source: UniProtKB

    Keywords - Cellular componenti

    Peroxisome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29185.

    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

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9UJM8.
    PRIDEiQ9UJM8.

    PTM databases

    PhosphoSiteiQ9UJM8.

    Expressioni

    Tissue specificityi

    Liver.

    Gene expression databases

    ArrayExpressiQ9UJM8.
    BgeeiQ9UJM8.
    CleanExiHS_HAO1.
    GenevestigatoriQ9UJM8.

    Organism-specific databases

    HPAiHPA049552.

    Interactioni

    Protein-protein interaction databases

    BioGridi119941. 1 interaction.
    IntActiQ9UJM8. 1 interaction.
    STRINGi9606.ENSP00000368066.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000217463.
    HOVERGENiHBG051881.
    InParanoidiQ9UJM8.
    KOiK11517.
    OMAiSPTENFG.
    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

    MLPRLICIND YEQHAKSVLP KSIYDYYRSG ANDEETLADN IAAFSRWKLY    50
    PRMLRNVAET DLSTSVLGQR VSMPICVGAT AMQRMAHVDG ELATVRACQS 100
    LGTGMMLSSW ATSSIEEVAE AGPEALRWLQ LYIYKDREVT KKLVRQAEKM 150
    GYKAIFVTVD TPYLGNRLDD VRNRFKLPPQ LRMKNFETST LSFSPEENFG 200
    DDSGLAAYVA KAIDPSISWE DIKWLRRLTS LPIVAKGILR GDDAREAVKH 250
    GLNGILVSNH GARQLDGVPA TIDVLPEIVE AVEGKVEVFL DGGVRKGTDV 300
    LKALALGAKA VFVGRPIVWG LAFQGEKGVQ DVLEILKEEF RLAMALSGCQ 350
    NVKVIDKTLV RKNPLAVSKI 370
    Length:370
    Mass (Da):40,924
    Last modified:May 1, 2000 - v1
    Checksum:iC683C6F7CB5FD323
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi13124294.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS13100.1.
    RefSeqi NP_060015.1. NM_017545.2.
    UniGenei Hs.193640.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2NZL X-ray 1.35 A 1-370 [» ]
    2RDT X-ray 1.95 A 1-370 [» ]
    2RDU X-ray 1.65 A 1-370 [» ]
    2RDW X-ray 1.95 A 1-370 [» ]
    2W0U X-ray 2.84 A/B/C/D 1-370 [» ]
    ProteinModelPortali Q9UJM8.
    SMRi Q9UJM8. Positions 3-362.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119941. 1 interaction.
    IntActi Q9UJM8. 1 interaction.
    STRINGi 9606.ENSP00000368066.

    Chemistry

    ChEMBLi CHEMBL4229.

    PTM databases

    PhosphoSitei Q9UJM8.

    Polymorphism databases

    DMDMi 13124294.

    Proteomic databases

    PaxDbi Q9UJM8.
    PRIDEi Q9UJM8.

    Protocols and materials databases

    DNASUi 54363.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000378789 ; ENSP00000368066 ; ENSG00000101323 .
    GeneIDi 54363.
    KEGGi hsa:54363.
    UCSCi uc002wmw.1. human.

    Organism-specific databases

    CTDi 54363.
    GeneCardsi GC20M007863.
    HGNCi HGNC:4809. HAO1.
    HPAi HPA049552.
    MIMi 605023. gene.
    neXtProti NX_Q9UJM8.
    PharmGKBi PA29185.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1304.
    HOGENOMi HOG000217463.
    HOVERGENi HBG051881.
    InParanoidi Q9UJM8.
    KOi K11517.
    OMAi SPTENFG.
    OrthoDBi EOG7B5WW0.
    PhylomeDBi Q9UJM8.
    TreeFami TF313363.

    Enzyme and pathway databases

    UniPathwayi UPA00864 ; UER00830 .
    Reactomei REACT_16925. Glyoxylate metabolism.
    SABIO-RK Q9UJM8.

    Miscellaneous databases

    EvolutionaryTracei Q9UJM8.
    GenomeRNAii 54363.
    NextBioi 56605.
    PROi Q9UJM8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UJM8.
    Bgeei Q9UJM8.
    CleanExi HS_HAO1.
    Genevestigatori Q9UJM8.

    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. "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. "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.
    8. "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.
    9. "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: October 1, 2014
    This is version 128 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