Hydroxyacid oxidase 2 - Rattus norvegicus (Rat)

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Q07523 (HAOX2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 104. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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) [Reference proteome]

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 Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid oxidation Inferred from electronic annotation. Source: Compara mandelate metabolic process Inferred from direct assay Ref.1. Source: RGD protein homooligomerization Inferred from direct assay Ref.5. Source: RGD
Cellular_component	mitochondrion Inferred from electronic annotation. Source: Compara peroxisome Inferred from direct assay PubMed 14561759. Source: HGNC
Molecular_function	(S)-2-hydroxy-acid oxidase activity Inferred from direct assay Ref.1. Source: RGD FMN binding Inferred from direct assay Ref.5. Source: RGD 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

Initiator methionine

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

FMN

Motif

351 – 353

Microbody targeting signal Potential

Sites

Active site

248

Proton acceptor By similarity

Binding site

106

FMN

Binding site

128

FMN

Binding site

130

Substrate

Binding site

156

FMN

Binding site

165

Substrate

Binding site

224

FMN

Binding site

251

Substrate By similarity

Binding site

303

FMN

Secondary structure

353

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q07523 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: A2FDD4BF34E269E5
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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

« Hide

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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

EMBL
GenBank
DDBJ

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

IPI

IPI00231245.

PIR

S33322.

RefSeq

NP_114471.1. NM_032082.2.

UniGene

Rn.198611.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TB3	X-ray	2.30	A/B/C/D/E/F/G/H	2-353	[»]
3SGZ	X-ray	1.35	A/B/C	2-353	[»]

ProteinModelPortal

Q07523.

SMR

Q07523. Positions 2-350.

ModBase

Search...

Protein-protein interaction databases

STRING

10116.ENSRNOP00000040223.

PTM databases

PhosphoSite

Q07523.

Proteomic databases

PaxDb

Q07523.

PRIDE

Q07523.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000046942; ENSRNOP00000040223; ENSRNOG00000019470.

GeneID

84029.

KEGG

rno:84029.

UCSC

RGD:70972. rat.

Organism-specific databases

CTD

51179.

RGD

70972. Hao2.

Phylogenomic databases

eggNOG

COG1304.

GeneTree

ENSGT00390000018717.

HOGENOM

HOG000217463.

HOVERGEN

HBG051881.

InParanoid

Q07523.

K11517.

OMA

SKTSWDF.

OrthoDB

EOG4QRH46.

Enzyme and pathway databases

SABIO-RK

Q07523.

Gene expression databases

Genevestigator

Q07523.

GermOnline

ENSRNOG00000019470. Rattus norvegicus.

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

EvolutionaryTrace

Q07523.

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:	April 3, 2013
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents