Reviewed, UniProtKB/Swiss-Prot Q9UJM8 (HAOX1_HUMAN)

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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	370 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	(S)-2-hydroxy acid + O(2) = 2-oxo acid + H(2)O(2).
Cofactor	FMN.
Pathway	Organic acid metabolism; glycolic acid degradation; 3-phospho-D-glyceric acid from glycolic acid: 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.

Ontologies

Keywords
Cellular component	Peroxisome
Ligand	FMN Flavoprotein
Molecular function	Oxidoreductase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	fatty acid alpha-oxidation Ref.2 Traceable author statement. Source: UniProtKB
Cellular component	peroxisome Ref.2 Traceable author statement. Source: UniProtKB
Molecular function	(S)-2-hydroxy-acid oxidase activity Ref.2 Traceable author statement. Source: UniProtKB
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

Motif

368 – 370

3

Microbody targeting signal Potential

Sites

Active site

260

1

Proton acceptor By similarity

Binding site

26

1

Substrate Potential

Binding site

108

1

FMN By similarity

Binding site

130

1

FMN By similarity

Binding site

132

1

Substrate By similarity

Binding site

158

1

FMN By similarity

Binding site

167

1

Substrate By similarity

Binding site

236

1

FMN By similarity

Binding site

263

1

Substrate Potential

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

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

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

Sequences

	Sequence		Length	Mass (Da)
	Q9UJM8-1 [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: 10978532] [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: 10777549] [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: 11780052] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

RefSeq

NP_060015.1.

UniGene

Hs.193640

3D structure databases

PDBMSD

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	[»]

ModBase

Search...

PTM databases

PhosphoSite

Q9UJM8.

Genome annotation databases

Ensembl

ENSG00000101323. Homo sapiens. [Contig view]

GeneID

54363.

KEGG

hsa:54363.

Organism-specific databases

H-InvDB

HIX0040489.

HGNC

HGNC:4809. HAO1.

MIM

605023. gene.

PharmGKB

PA29185.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

Q9UJM8.

HOVERGEN

Q9UJM8.

Gene expression databases

ArrayExpress

Q9UJM8.

CleanEx

HS_HAO1.

GermOnline

ENSG00000101323. Homo sapiens.

Family and domain databases

InterPro

IPR013785. Aldolase_TIM.
IPR012133. Alpha_OHA_DHase_FMN.
IPR008259. FMN_hydac_DHase_AS.
IPR000262. FMN_OHA_DHase.
[Graphical view]

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.

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]

BLOCKS

Search...

ProtoNet

Search...

Other Resources

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:	November 4, 2008
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)