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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

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

  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
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

  1. peroxisomal matrix Source: Reactome
  2. 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.
GenevestigatoriQ9UJM8.

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.
OMAiAEQMGYK.
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.

Polymorphism and mutation databases

BioMutaiHAO1.

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.
OMAiAEQMGYK.
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.
GenevestigatoriQ9UJM8.

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: April 29, 2015
This is version 134 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.