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Q9UJM8 (HAOX1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hydroxyacid oxidase 1

Short name=HAOX1
EC=1.1.3.15
Alternative name(s):
Glycolate oxidase
Short name=GOX
Gene names
Name:HAO1
Synonyms:GOX1, HAOX1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length370 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7

Catalytic activity

(S)-2-hydroxy acid + O2 = 2-oxo acid + H2O2. Ref.7

Cofactor

FMN. Ref.7

Pathway

Organic acid metabolism; glycolate degradation; 3-phospho-D-glycerate from glycolate: step 1/4.

Subcellular location

Peroxisome.

Tissue specificity

Liver.

Sequence similarities

Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.

Contains 1 FMN hydroxy acid dehydrogenase domain.

Biophysicochemical properties

Kinetic parameters:

KM=141 µM for glycolate Ref.7

KM=40 µM for 2-hydroxy octanoate

KM=2200 µM for glyoxylate

Ontologies

Keywords
   Cellular componentPeroxisome
   LigandFlavoprotein
FMN
   Molecular functionOxidoreductase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

fatty acid alpha-oxidation

Inferred from direct assay Ref.7. Source: UniProtKB

glycolate catabolic process

Inferred from direct assay Ref.7. Source: UniProtKB

glyoxylate metabolic process

Traceable author statement. Source: Reactome

response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentperoxisomal matrix

Traceable author statement. Source: Reactome

peroxisome

Inferred from direct assay Ref.2. Source: UniProtKB

   Molecular_function(S)-2-hydroxy-acid oxidase activity

Inferred from direct assay Ref.2Ref.7. Source: UniProtKB

FMN binding

Inferred from direct assay Ref.7. Source: UniProtKB

glycolate oxidase activity

Inferred from direct assay Ref.2Ref.7. Source: UniProtKB

glyoxylate oxidase activity

Traceable author statement. Source: Reactome

long-chain-(S)-2-hydroxy-long-chain-acid oxidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

medium-chain-(S)-2-hydroxy-acid oxidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

receptor binding

Inferred from physical interaction PubMed 20178365. Source: UniProtKB

very-long-chain-(S)-2-hydroxy-acid oxidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 370370Hydroxyacid oxidase 1
PRO_0000206318

Regions

Domain1 – 365365FMN hydroxy acid dehydrogenase
Nucleotide binding291 – 31525FMN By similarity
Nucleotide binding291 – 2955FMN binding
Motif368 – 3703Microbody targeting signal Potential

Sites

Active site2601Proton acceptor
Binding site261Substrate
Binding site1081FMN
Binding site1301FMN
Binding site1321FMN
Binding site1321Substrate
Binding site1581FMN
Binding site1671Substrate
Binding site2361FMN
Binding site2581FMN
Binding site2631Substrate
Binding site3151FMN

Amino acid modifications

Modified residue1841N6-succinyllysine By similarity
Modified residue1941Phosphoserine By similarity

Secondary structure

.......................................................... 370
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9UJM8 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: C683C6F7CB5FD323

FASTA37040,924
        10         20         30         40         50         60 
MLPRLICIND YEQHAKSVLP KSIYDYYRSG ANDEETLADN IAAFSRWKLY PRMLRNVAET 

        70         80         90        100        110        120 
DLSTSVLGQR VSMPICVGAT AMQRMAHVDG ELATVRACQS LGTGMMLSSW ATSSIEEVAE 

       130        140        150        160        170        180 
AGPEALRWLQ LYIYKDREVT KKLVRQAEKM GYKAIFVTVD TPYLGNRLDD VRNRFKLPPQ 

       190        200        210        220        230        240 
LRMKNFETST LSFSPEENFG DDSGLAAYVA KAIDPSISWE DIKWLRRLTS LPIVAKGILR 

       250        260        270        280        290        300 
GDDAREAVKH GLNGILVSNH GARQLDGVPA TIDVLPEIVE AVEGKVEVFL DGGVRKGTDV 

       310        320        330        340        350        360 
LKALALGAKA VFVGRPIVWG LAFQGEKGVQ DVLEILKEEF RLAMALSGCQ NVKVIDKTLV 

       370 
RKNPLAVSKI 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_060015.1. NM_017545.2.
UniGeneHs.193640.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ9UJM8.
SMRQ9UJM8. Positions 3-362.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119941. 1 interaction.
IntActQ9UJM8. 1 interaction.
STRING9606.ENSP00000368066.

Chemistry

ChEMBLCHEMBL4229.

PTM databases

PhosphoSiteQ9UJM8.

Polymorphism databases

DMDM13124294.

Proteomic databases

PaxDbQ9UJM8.
PRIDEQ9UJM8.

Protocols and materials databases

DNASU54363.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000378789; ENSP00000368066; ENSG00000101323.
GeneID54363.
KEGGhsa:54363.
UCSCuc002wmw.1. human.

Organism-specific databases

CTD54363.
GeneCardsGC20M007863.
HGNCHGNC:4809. HAO1.
HPAHPA049552.
MIM605023. gene.
neXtProtNX_Q9UJM8.
PharmGKBPA29185.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1304.
HOGENOMHOG000217463.
HOVERGENHBG051881.
InParanoidQ9UJM8.
KOK11517.
OMAIDPSINW.
OrthoDBEOG7B5WW0.
PhylomeDBQ9UJM8.
TreeFamTF313363.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
SABIO-RKQ9UJM8.
UniPathwayUPA00864; UER00830.

Gene expression databases

ArrayExpressQ9UJM8.
BgeeQ9UJM8.
CleanExHS_HAO1.
GenevestigatorQ9UJM8.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR012133. Alpha-hydoxy_acid_DH_FMN.
IPR000262. FMN-dep_DH.
IPR008259. FMN_hydac_DH_AS.
[Graphical view]
PfamPF01070. FMN_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000138. Al-hdrx_acd_dh. 1 hit.
PROSITEPS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9UJM8.
GenomeRNAi54363.
NextBio56605.
PROQ9UJM8.
SOURCESearch...

Entry information

Entry nameHAOX1_HUMAN
AccessionPrimary (citable) accession number: Q9UJM8
Secondary accession number(s): Q14CQ0, Q9UPZ0, Q9Y3I7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM