Q9UJM8 (HAOX1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	370 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Peroxisome
Ligand	FMN Flavoprotein
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular 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: Compara
Cellular_component	peroxisomal matrix Traceable author statement. Source: Reactome
Molecular_function	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: EC medium-chain-(S)-2-hydroxy-acid oxidase activity Inferred from electronic annotation. Source: EC very-long-chain-(S)-2-hydroxy-acid oxidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 370

370

Hydroxyacid oxidase 1

PRO_0000206318

Regions

Domain

1 – 365

365

FMN hydroxy acid dehydrogenase

Nucleotide binding

291 – 315

25

FMN By similarity

Nucleotide binding

291 – 295

5

FMN binding

Motif

368 – 370

3

Microbody targeting signal Potential

Sites

Active site

260

1

Proton acceptor

Binding site

26

1

Substrate

Binding site

108

1

FMN

Binding site

130

1

FMN

Binding site

132

1

FMN

Binding site

132

1

Substrate

Binding site

158

1

FMN

Binding site

167

1

Substrate

Binding site

236

1

FMN

Binding site

258

1

FMN

Binding site

263

1

Substrate

Binding site

315

1

FMN

Secondary structure

1

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370

Helix Strand Turn

Details...

Helix

8 – 18

11

Helix

21 – 28

8

Helix

35 – 46

12

Beta strand

47 – 49

3

Beta strand

64 – 66

3

Beta strand

69 – 77

9

Helix

83 – 85

3

Helix

90 – 101

12

Beta strand

104 – 107

4

Helix

115 – 121

7

Beta strand

125 – 131

7

Beta strand

134 – 136

3

Helix

137 – 149

13

Beta strand

155 – 158

4

Helix

168 – 173

6

Turn

189 – 193

5

Helix

205 – 212

8

Helix

219 – 225

7

Beta strand

233 – 238

6

Helix

241 – 249

9

Beta strand

254 – 257

4

Helix

260 – 262

3

Helix

271 – 282

12

Beta strand

285 – 290

6

Helix

297 – 305

9

Beta strand

309 – 313

5

Helix

315 – 346

32

Helix

352 – 354

3

Helix

357 – 359

3

Beta strand

360 – 362

3

Sequences

	Sequence		Length	Mass (Da)
	Q9UJM8 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: C683C6F7CB5FD323	FASTA	370	40,924
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

IPI

IPI00006934.

RefSeq

NP_060015.1. NM_017545.2.

UniGene

Hs.193640.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q9UJM8.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000368066.

PTM databases

PhosphoSite

Q9UJM8.

Polymorphism databases

DMDM

13124294.

Proteomic databases

PaxDb

Q9UJM8.

PRIDE

Q9UJM8.

Protocols and materials databases

DNASU

54363.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000378789; ENSP00000368066; ENSG00000101323.

GeneID

54363.

KEGG

hsa:54363.

UCSC

uc002wmw.1. human.

Organism-specific databases

CTD

54363.

GeneCards

GC20M007863.

HGNC

HGNC:4809. HAO1.

HPA

HPA049552.

MIM

605023. gene.

neXtProt

NX_Q9UJM8.

PharmGKB

PA29185.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1304.

HOGENOM

HOG000217463.

HOVERGEN

HBG051881.

InParanoid

Q9UJM8.

KO

K11517.

OMA

ESPTMST.

OrthoDB

EOG4MGS7T.

PhylomeDB

Q9UJM8.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

SABIO-RK

Q9UJM8.

UniPathway

UPA00864; UER00830.

Gene expression databases

ArrayExpress

Q9UJM8.

Bgee

Q9UJM8.

CleanEx

HS_HAO1.

Genevestigator

Q9UJM8.

GermOnline

ENSG00000101323. Homo sapiens.

Family and domain databases

Gene3D

3.20.20.70. 1 hit.

InterPro

IPR013785. Aldolase_TIM.
IPR012133. Alpha-hydoxy_acid_DH_FMN.
IPR000262. FMN-dep_DH.
IPR008259. FMN_hydac_DH_AS.
[Graphical view]

Pfam

PF01070. FMN_dh. 1 hit.
[Graphical view]

PIRSF

PIRSF000138. Al-hdrx_acd_dh. 1 hit.

PROSITE

PS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL4229.

EvolutionaryTrace

Q9UJM8.

GenomeRNAi

54363.

NextBio

56605.

SOURCE

Search...

Entry information

Entry name

HAOX1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 116 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.