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Protein

Hydroxyacid oxidase 2

Gene

Hao2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the oxidation of L-alpha-hydroxy acids as well as, more slowly, that of L-alpha-amino acids.

Catalytic activityi

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

Cofactori

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei106FMNPROSITE-ProRule annotation1 Publication1
Binding sitei128FMNPROSITE-ProRule annotation1 Publication1
Binding sitei130Substrate1
Binding sitei156FMNPROSITE-ProRule annotation1 Publication1
Binding sitei165Substrate1
Binding sitei224FMNPROSITE-ProRule annotation1 Publication1
Active sitei248Proton acceptorPROSITE-ProRule annotation1
Binding sitei251SubstratePROSITE-ProRule annotation1
Binding sitei303FMNPROSITE-ProRule annotation1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi279 – 303FMNPROSITE-ProRule annotation1 PublicationAdd BLAST25

GO - Molecular functioni

GO - Biological processi

  • mandelate metabolic process Source: RGD
  • protein homooligomerization Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Flavoprotein, FMN

Enzyme and pathway databases

BRENDAi1.1.3.15. 5301.
ReactomeiR-RNO-390918. Peroxisomal lipid metabolism.
SABIO-RKQ07523.

Names & Taxonomyi

Protein namesi
Recommended name:
Hydroxyacid oxidase 2 (EC:1.1.3.15)
Short name:
HAOX2
Alternative name(s):
(S)-2-hydroxy-acid oxidase, peroxisomal
Long chain alpha-hydroxy acid oxidase
Long-chain L-2-hydroxy acid oxidase
Gene namesi
Name:Hao2
Synonyms:Hao3, Haox2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi70972. Hao2.

Subcellular locationi

GO - Cellular componenti

  • peroxisome Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2021745.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00002063222 – 353Hydroxyacid oxidase 2Add BLAST352

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei133PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ07523.
PRIDEiQ07523.

PTM databases

iPTMnetiQ07523.
PhosphoSitePlusiQ07523.

Miscellaneous databases

PMAP-CutDBQ07523.

Expressioni

Gene expression databases

BgeeiENSRNOG00000019470.
ExpressionAtlasiQ07523. baseline and differential.
GenevisibleiQ07523. RN.

Interactioni

Subunit structurei

Homotetramer or homooctamer.1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000040223.

Chemistry databases

BindingDBiQ07523.

Structurei

Secondary structure

1353
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 15Combined sources10
Helixi19 – 26Combined sources8
Helixi33 – 43Combined sources11
Beta strandi62 – 64Combined sources3
Beta strandi67 – 75Combined sources9
Helixi81 – 83Combined sources3
Helixi88 – 99Combined sources12
Beta strandi102 – 105Combined sources4
Helixi113 – 119Combined sources7
Beta strandi124 – 128Combined sources5
Helixi135 – 147Combined sources13
Beta strandi153 – 156Combined sources4
Helixi166 – 174Combined sources9
Helixi177 – 180Combined sources4
Helixi207 – 216Combined sources10
Beta strandi221 – 226Combined sources6
Helixi229 – 237Combined sources9
Beta strandi241 – 245Combined sources5
Helixi248 – 250Combined sources3
Helixi259 – 270Combined sources12
Beta strandi273 – 281Combined sources9
Helixi285 – 293Combined sources9
Beta strandi297 – 302Combined sources6
Helixi303 – 335Combined sources33
Helixi340 – 342Combined sources3
Helixi345 – 347Combined sources3
Beta strandi348 – 350Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TB3X-ray2.30A/B/C/D/E/F/G/H2-353[»]
3SGZX-ray1.35A/B/C2-353[»]
ProteinModelPortaliQ07523.
SMRiQ07523.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ07523.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 353FMN hydroxy acid dehydrogenasePROSITE-ProRule annotationAdd BLAST352

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi351 – 353Microbody targeting signalSequence analysis3

Sequence similaritiesi

Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.PROSITE-ProRule annotation
Contains 1 FMN hydroxy acid dehydrogenase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0538. Eukaryota.
COG1304. LUCA.
GeneTreeiENSGT00390000018717.
HOGENOMiHOG000217463.
HOVERGENiHBG051881.
InParanoidiQ07523.
KOiK11517.
PhylomeDBiQ07523.
TreeFamiTF313363.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR012133. Alpha-hydoxy_acid_DH_FMN.
IPR000262. FMN-dep_DH.
IPR008259. FMN_hydac_DH_AS.
[Graphical view]
PfamiPF01070. FMN_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000138. Al-hdrx_acd_dh. 1 hit.
PROSITEiPS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q07523-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPLVCLADFK AHAQKQLSKT SWDFIEGEAD DGITYSENIA AFKRIRLRPR
60 70 80 90 100
YLRDMSKVDT RTTIQGQEIS APICISPTAF HSIAWPDGEK STARAAQEAN
110 120 130 140 150
ICYVISSYAS YSLEDIVAAA PEGFRWFQLY MKSDWDFNKQ MVQRAEALGF
160 170 180 190 200
KALVITIDTP VLGNRRRDKR NQLNLEANIL LKDLRALKEE KPTQSVPVSF
210 220 230 240 250
PKASFCWNDL SLLQSITRLP IILKGILTKE DAELAMKHNV QGIVVSNHGG
260 270 280 290 300
RQLDEVSASI DALREVVAAV KGKIEVYMDG GVRTGTDVLK ALALGARCIF
310 320 330 340 350
LGRPILWGLA CKGEDGVKEV LDILTAELHR CMTLSGCQSV AEISPDLIQF

SRL
Length:353
Mass (Da):39,201
Last modified:January 23, 2007 - v2
Checksum:iA2FDD4BF34E269E5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67156 mRNA. Translation: CAA47629.1.
BC078781 mRNA. Translation: AAH78781.1.
PIRiS33322.
RefSeqiNP_114471.1. NM_032082.2.
UniGeneiRn.198611.

Genome annotation databases

EnsembliENSRNOT00000046942; ENSRNOP00000040223; ENSRNOG00000019470.
ENSRNOT00000091444; ENSRNOP00000071695; ENSRNOG00000019470.
GeneIDi84029.
KEGGirno:84029.
UCSCiRGD:70972. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67156 mRNA. Translation: CAA47629.1.
BC078781 mRNA. Translation: AAH78781.1.
PIRiS33322.
RefSeqiNP_114471.1. NM_032082.2.
UniGeneiRn.198611.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TB3X-ray2.30A/B/C/D/E/F/G/H2-353[»]
3SGZX-ray1.35A/B/C2-353[»]
ProteinModelPortaliQ07523.
SMRiQ07523.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000040223.

Chemistry databases

BindingDBiQ07523.
ChEMBLiCHEMBL2021745.

PTM databases

iPTMnetiQ07523.
PhosphoSitePlusiQ07523.

Proteomic databases

PaxDbiQ07523.
PRIDEiQ07523.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000046942; ENSRNOP00000040223; ENSRNOG00000019470.
ENSRNOT00000091444; ENSRNOP00000071695; ENSRNOG00000019470.
GeneIDi84029.
KEGGirno:84029.
UCSCiRGD:70972. rat.

Organism-specific databases

CTDi51179.
RGDi70972. Hao2.

Phylogenomic databases

eggNOGiKOG0538. Eukaryota.
COG1304. LUCA.
GeneTreeiENSGT00390000018717.
HOGENOMiHOG000217463.
HOVERGENiHBG051881.
InParanoidiQ07523.
KOiK11517.
PhylomeDBiQ07523.
TreeFamiTF313363.

Enzyme and pathway databases

BRENDAi1.1.3.15. 5301.
ReactomeiR-RNO-390918. Peroxisomal lipid metabolism.
SABIO-RKQ07523.

Miscellaneous databases

EvolutionaryTraceiQ07523.
PMAP-CutDBQ07523.
PROiQ07523.

Gene expression databases

BgeeiENSRNOG00000019470.
ExpressionAtlasiQ07523. baseline and differential.
GenevisibleiQ07523. RN.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR012133. Alpha-hydoxy_acid_DH_FMN.
IPR000262. FMN-dep_DH.
IPR008259. FMN_hydac_DH_AS.
[Graphical view]
PfamiPF01070. FMN_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000138. Al-hdrx_acd_dh. 1 hit.
PROSITEiPS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHAOX2_RAT
AccessioniPrimary (citable) accession number: Q07523
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.