Reviewed, UniProtKB/Swiss-Prot Q07523 (HAOX2_RAT)

Names and origin

Protein names

Recommended name:
    Hydroxyacid oxidase 2
      Short name=HAOX2
    EC=1.1.3.15
Alternative name(s):
    (S)-2-hydroxy-acid oxidase, peroxisomal
    Long chain alpha-hydroxy acid oxidase
    Long-chain L-2-hydroxy acid oxidase

Gene names

Name:	Hao2
Synonyms:	Hao3, Haox2

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	353 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the oxidation of L-alpha-hydroxy acids as well as, more slowly, that of L-alpha-amino acids.
Catalytic activity	(S)-2-hydroxy acid + O2 = 2-oxo acid + H2O2.
Cofactor	FMN.
Subunit structure	Homotetramer or homooctamer. Ref.5
Subcellular location	Peroxisome.
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 Direct protein sequencing
Gene Ontology (GO)
Biological process	mandelate metabolic process Ref.1 Inferred from direct assay. Source: RGD oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW protein homooligomerization Ref.5 Inferred from direct assay. Source: RGD
Cellular component	peroxisome Inferred from direct assay. Source: HGNC
Molecular function	(S)-2-hydroxy-acid oxidase activity Ref.1 Inferred from direct assay. Source: RGD FMN binding Ref.5 Inferred from direct assay. Source: RGD electron carrier activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.3 Ref.4

Chain

2 – 353

352

Hydroxyacid oxidase 2

PRO_0000206322

Regions

Domain

2 – 353

352

FMN hydroxy acid dehydrogenase

Nucleotide binding

279 – 303

25

FMN

Motif

351 – 353

3

Microbody targeting signal Potential

Sites

Active site

248

1

Proton acceptor By similarity

Binding site

106

1

FMN

Binding site

128

1

FMN

Binding site

130

1

Substrate

Binding site

156

1

FMN

Binding site

165

1

Substrate

Binding site

224

1

FMN

Binding site

251

1

Substrate Potential

Secondary structure

1

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353

Helix Strand Turn

Details...

Helix

6 – 15

10

Helix

19 – 26

8

Helix

33 – 44

12

Beta strand

62 – 64

3

Beta strand

67 – 75

9

Helix

81 – 83

3

Turn

86 – 88

3

Helix

89 – 99

11

Beta strand

103 – 105

3

Helix

113 – 119

7

Beta strand

125 – 128

4

Helix

137 – 148

12

Beta strand

153 – 156

4

Helix

166 – 170

5

Helix

207 – 214

8

Beta strand

221 – 226

6

Helix

229 – 237

9

Beta strand

241 – 245

5

Helix

248 – 250

3

Helix

259 – 270

12

Beta strand

273 – 281

9

Helix

285 – 293

9

Beta strand

299 – 302

4

Helix

303 – 335

33

Helix

340 – 342

3

Helix

345 – 347

3

Sequences

	Sequence		Length	Mass (Da)
	Q07523-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: A2FDD4BF34E269E5	FASTA	353	39,201
	10 20 30 40 50 60 MPLVCLADFK AHAQKQLSKT SWDFIEGEAD DGITYSENIA AFKRIRLRPR YLRDMSKVDT 70 80 90 100 110 120 RTTIQGQEIS APICISPTAF HSIAWPDGEK STARAAQEAN ICYVISSYAS YSLEDIVAAA 130 140 150 160 170 180 PEGFRWFQLY MKSDWDFNKQ MVQRAEALGF KALVITIDTP VLGNRRRDKR NQLNLEANIL 190 200 210 220 230 240 LKDLRALKEE KPTQSVPVSF PKASFCWNDL SLLQSITRLP IILKGILTKE DAELAMKHNV 250 260 270 280 290 300 QGIVVSNHGG RQLDEVSASI DALREVVAAV KGKIEVYMDG GVRTGTDVLK ALALGARCIF 310 320 330 340 350 LGRPILWGLA CKGEDGVKEV LDILTAELHR CMTLSGCQSV AEISPDLIQF SRL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and nucleotide sequence of cDNA encoding rat kidney long-chain L-2-hydroxy acid oxidase. Expression of the catalytically active recombinant protein as a chimaera." Belmouden A., Le K.H.D., Lederer F., Garchon H.J. Eur. J. Biochem. 214:17-25(1993) [PubMed: 8508789] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Wistar. Tissue: Kidney.
[2]	"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: Testis.
[3]	"Amino acid sequence of long chain alpha-hydroxy acid oxidase from rat kidney, a member of the family of FMN-dependent alpha-hydroxy acid-oxidizing enzymes." Le K.H.D., Lederer F. J. Biol. Chem. 266:20877-20881(1991) [PubMed: 1939137] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-353. Tissue: Kidney.
[4]	"Rat kidney L-2-hydroxyacid oxidase. Structural and mechanistic comparison with flavocytochrome b2 from baker's yeast." Urban P., Chirat I., Lederer F. Biochemistry 27:7365-7371(1988) [PubMed: 3061453] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-41, CHARACTERIZATION.
[5]	"Crystal structure analysis of recombinant rat kidney long chain hydroxy acid oxidase." Cunane L.M., Barton J.D., Chen Z.-W., Le K.H.D., Amar D., Lederer F., Mathews F.S. Biochemistry 44:1521-1531(2005) [PubMed: 15683236] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH FMN AND SUBSTRATE ANALOG, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X67156 mRNA. Translation: CAA47629.1.
BC078781 mRNA. Translation: AAH78781.1.

IPI

IPI00231245.

PIR

S33322.

RefSeq

NP_114471.1.

UniGene

Rn.198611

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TB3	X-ray	2.30	A/B/C/D/E/F/G/H	2-353	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q07523.

PTM databases

PhosphoSite

Q07523.

Proteomic databases

PRIDE

Q07523.

Genome annotation databases

Ensembl

ENSRNOT00000026357; ENSRNOP00000026357; ENSRNOG00000019470; Rattus norvegicus. [Genome view]
ENSRNOT00000046942; ENSRNOP00000040223; ENSRNOG00000019470; Rattus norvegicus. [Genome view]

GeneID

84029.

KEGG

rno:84029.

UCSC

NM_032082. rat.

Organism-specific databases

CTD

84029.

RGD

70972. Hao2.

Phylogenomic databases

HOVERGEN

Q07523.

OMA

RPRMLRD.

Enzyme and pathway databases

BRENDA

1.1.3.15. 248.

Gene expression databases

ArrayExpress

Q07523.

Genevestigator

Q07523.

GermOnline

ENSRNOG00000019470. Rattus norvegicus.

Family and domain databases

InterPro

IPR012133. a-Hydoxy_acid_DH_FMN.
IPR013785. Aldolase_TIM.
IPR000262. FMN-dep_DH.
IPR017934. FMN-dep_OHA_DH.
IPR008259. FMN_hydac_DH_AS.
[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]

ProtoNet

Search...

Other Resources

NextBio

616611.

PMAP-CutDB

Q07523.

Entry information

Entry name

HAOX2_RAT

Accession

Primary (citable) accession number: Q07523

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)