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Q07523

- HAOX2_RAT

UniProt

Q07523 - HAOX2_RAT

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Protein

Hydroxyacid oxidase 2

Gene

Hao2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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

FMN.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei106 – 1061FMN1 PublicationPROSITE-ProRule annotation
Binding sitei128 – 1281FMN1 PublicationPROSITE-ProRule annotation
Binding sitei130 – 1301Substrate
Binding sitei156 – 1561FMN1 PublicationPROSITE-ProRule annotation
Binding sitei165 – 1651Substrate
Binding sitei224 – 2241FMN1 PublicationPROSITE-ProRule annotation
Active sitei248 – 2481Proton acceptorPROSITE-ProRule annotation
Binding sitei251 – 2511SubstratePROSITE-ProRule annotation
Binding sitei303 – 3031FMN1 PublicationPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi279 – 30325FMN1 PublicationPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. (S)-2-hydroxy-acid oxidase activity Source: RGD
  2. FMN binding Source: RGD
  3. long-chain-(S)-2-hydroxy-long-chain-acid oxidase activity Source: UniProtKB-EC
  4. medium-chain-(S)-2-hydroxy-acid oxidase activity Source: UniProtKB-EC
  5. very-long-chain-(S)-2-hydroxy-acid oxidase activity Source: UniProtKB-EC

GO - Biological processi

  1. fatty acid oxidation Source: Ensembl
  2. mandelate metabolic process Source: RGD
  3. protein homooligomerization Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Flavoprotein, FMN

Enzyme and pathway databases

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
ProteomesiUP000002494: Chromosome 2

Organism-specific databases

RGDi70972. Hao2.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. mitochondrion Source: Ensembl
  3. peroxisome Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 353352Hydroxyacid oxidase 2PRO_0000206322Add
BLAST

Proteomic databases

PaxDbiQ07523.
PRIDEiQ07523.

PTM databases

PhosphoSiteiQ07523.

Miscellaneous databases

PMAP-CutDBQ07523.

Expressioni

Gene expression databases

GenevestigatoriQ07523.

Interactioni

Subunit structurei

Homotetramer or homooctamer.1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000040223.

Structurei

Secondary structure

1
353
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 1510
Helixi19 – 268
Helixi33 – 4311
Beta strandi62 – 643
Beta strandi67 – 759
Helixi81 – 833
Helixi88 – 9912
Beta strandi102 – 1054
Helixi113 – 1197
Beta strandi124 – 1285
Helixi135 – 14713
Beta strandi153 – 1564
Helixi166 – 1749
Helixi177 – 1804
Helixi207 – 21610
Beta strandi221 – 2266
Helixi229 – 2379
Beta strandi241 – 2455
Helixi248 – 2503
Helixi259 – 27012
Beta strandi273 – 2819
Helixi285 – 2939
Beta strandi297 – 3026
Helixi303 – 33533
Helixi340 – 3423
Helixi345 – 3473
Beta strandi348 – 3503

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TB3X-ray2.30A/B/C/D/E/F/G/H2-353[»]
3SGZX-ray1.35A/B/C2-353[»]
ProteinModelPortaliQ07523.
SMRiQ07523. Positions 2-350.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ07523.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 353352FMN hydroxy acid dehydrogenasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi351 – 3533Microbody targeting signalSequence Analysis

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

eggNOGiCOG1304.
GeneTreeiENSGT00390000018717.
HOGENOMiHOG000217463.
HOVERGENiHBG051881.
InParanoidiQ07523.
KOiK11517.
OMAiTAFHSIA.
OrthoDBiEOG7B5WW0.
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:
EMBL
GenBank
DDBJ
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.
GeneIDi84029.
KEGGirno:84029.
UCSCiRGD:70972. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X67156 mRNA. Translation: CAA47629.1 .
BC078781 mRNA. Translation: AAH78781.1 .
PIRi S33322.
RefSeqi NP_114471.1. NM_032082.2.
UniGenei Rn.198611.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali Q07523.
SMRi Q07523. Positions 2-350.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000040223.

Chemistry

ChEMBLi CHEMBL2021745.

PTM databases

PhosphoSitei Q07523.

Proteomic databases

PaxDbi Q07523.
PRIDEi Q07523.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000046942 ; ENSRNOP00000040223 ; ENSRNOG00000019470 .
GeneIDi 84029.
KEGGi rno:84029.
UCSCi RGD:70972. rat.

Organism-specific databases

CTDi 51179.
RGDi 70972. Hao2.

Phylogenomic databases

eggNOGi COG1304.
GeneTreei ENSGT00390000018717.
HOGENOMi HOG000217463.
HOVERGENi HBG051881.
InParanoidi Q07523.
KOi K11517.
OMAi TAFHSIA.
OrthoDBi EOG7B5WW0.
PhylomeDBi Q07523.
TreeFami TF313363.

Enzyme and pathway databases

SABIO-RK Q07523.

Miscellaneous databases

EvolutionaryTracei Q07523.
NextBioi 616611.
PMAP-CutDB Q07523.
PROi Q07523.

Gene expression databases

Genevestigatori Q07523.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR013785. Aldolase_TIM.
IPR012133. Alpha-hydoxy_acid_DH_FMN.
IPR000262. FMN-dep_DH.
IPR008259. FMN_hydac_DH_AS.
[Graphical view ]
Pfami PF01070. FMN_dh. 1 hit.
[Graphical view ]
PIRSFi PIRSF000138. Al-hdrx_acd_dh. 1 hit.
PROSITEi PS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

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: October 29, 2014
This is version 114 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

External Data

Dasty 3