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O54754

- AOXA_MOUSE

UniProt

O54754 - AOXA_MOUSE

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Protein

Aldehyde oxidase 1

Gene

Aox1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide and N-methylphthalazinium, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. Plays a role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Participates in the bioactivation of prodrugs such as famciclovir, catalyzing the oxidation step from 6-deoxypenciclovir to penciclovir, which is a potent antiviral agent. Also plays a role in the reductive metabolism of the xenobiotic imidacloprid (IMI) via its nitroreduction to nitrosoguanidine (IMI-NNO) and aminoguanidine (IMI-NNH2). Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. Also may catalyze nitric oxide (NO) production via the reduction of nitrite to NO with NADH or aldehyde as electron donor. May play a role in adipogenesis. Cannot use xanthine and hypoxanthine as substrate.4 Publications

Catalytic activityi

An aldehyde + H2O + O2 = a carboxylate + H2O2.
Retinal + O2 + H2O = retinoate + H2O2.

Cofactori

Protein has several cofactor binding sites:

Kineticsi

kcat is 317.6 min(-1) for benzaldehyde oxidation, 128.1 min(-1) for phthalazine oxidation, 49.5 min(-1) for retinal oxidation, and 519.9 min(-1) for acetaldehyde oxidation (at 30 degrees Celsius and pH 7.5) (PubMed:19401776). In PubMed:19401776, the measures are done with the recombinant protein, which is only 20% active, due to an incomplete saturation of the molybdenum cofactor with the sulfido ligand.1 Publication

  1. KM=3.8 µM for retinal (at 37 degrees Celsius and pH 7.8)2 Publications
  2. KM=97.7 µM for benzaldehyde (at 30 degrees Celsius and pH 7.5)2 Publications
  3. KM=11.4 µM for phthalazine (at 30 degrees Celsius and pH 7.5)2 Publications
  4. KM=55.8 µM for retinal (at 30 degrees Celsius and pH 7.5)2 Publications
  5. KM=17.5 mM for acetaldehyde (at 30 degrees Celsius and pH 7.5)2 Publications

Vmax=807 nmol/min/mg enzyme with retinal as substrate (at 37 degrees Celsius and pH 7.8)2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi43 – 431Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi48 – 481Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi51 – 511Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi73 – 731Iron-sulfur 1 (2Fe-2S)By similarity
Binding sitei112 – 1121MolybdopterinBy similarity
Metal bindingi113 – 1131Iron-sulfur 2 (2Fe-2S)By similarity
Metal bindingi116 – 1161Iron-sulfur 2 (2Fe-2S)By similarity
Metal bindingi148 – 1481Iron-sulfur 2 (2Fe-2S)By similarity
Metal bindingi150 – 1501Iron-sulfur 2 (2Fe-2S)By similarity
Binding sitei353 – 3531FADBy similarity
Binding sitei357 – 3571FADBy similarity
Binding sitei366 – 3661FADBy similarity
Binding sitei410 – 4101FAD; via amide nitrogenBy similarity
Binding sitei801 – 8011Molybdopterin; via amide nitrogenBy similarity
Binding sitei1042 – 10421Molybdopterin; via amide nitrogenBy similarity
Binding sitei1198 – 11981MolybdopterinBy similarity
Active sitei1265 – 12651Proton acceptor; for azaheterocycle hydroxylase activity1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi263 – 2708FADBy similarity

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
  2. aldehyde oxidase activity Source: MGI
  3. electron carrier activity Source: MGI
  4. flavin adenine dinucleotide binding Source: InterPro
  5. iron ion binding Source: InterPro
  6. molybdopterin cofactor binding Source: InterPro
  7. NAD binding Source: InterPro
  8. UDP-N-acetylmuramate dehydrogenase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Molybdenum

Names & Taxonomyi

Protein namesi
Recommended name:
Aldehyde oxidase 1 (EC:1.2.3.1)
Alternative name(s):
Azaheterocycle hydroxylase 1 (EC:1.17.3.-)
Retinal oxidase
Gene namesi
Name:Aox1
Synonyms:Ao, Ro
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:88035. Aox1.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi806 – 8061V → E: Decreases substrate affinity and activity on benzaldehyde, phthalazine and acetaldehyde, while increases affinity for more hydrophobic aldehydes like retinal. Abolishes catalytic activity; when associated with R-884. 1 Publication
Mutagenesisi884 – 8841M → R: Abolishes catalytic activity on phthalazine and acetaldehyde. Decreases catalytic efficiency on benzaldehyde and retinal. Abolishes catalytic activity; when associated with E-806. 1 Publication
Mutagenesisi1265 – 12651E → Q: Abolishes catalytic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13331333Aldehyde oxidase 1PRO_0000166106Add
BLAST

Proteomic databases

MaxQBiO54754.
PaxDbiO54754.
PRIDEiO54754.

PTM databases

PhosphoSiteiO54754.

Expressioni

Tissue specificityi

Highest expression in esophagus. Moderately low expression in lung, liver, heart, Harderian gland, olfactory mucosa, skin and testis. In brain, expression is very high in choroid plexus, high in hind brain and low in hippocampus and cerebellum. In spinal cord expression is strongest in anterior horns. Low expression detected in spleen and eye. AOX1 expression in the livers of mice is approximately seven times greater in males than females.4 Publications

Developmental stagei

Expressed in adult liver but not in neonatal or embryonic liver. Not detected in preadipocytes but strongly induced in mature adipocytes.2 Publications

Inductioni

Repressed by pioglitazone, fenofibrate and PPARA agonists. Induced by testosterone.2 Publications

Gene expression databases

CleanExiMM_AOX1.
GenevestigatoriO54754.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

IntActiO54754. 2 interactions.
MINTiMINT-1869370.

Structurei

3D structure databases

ProteinModelPortaliO54754.
SMRiO54754. Positions 5-165, 200-533, 577-1315.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 91882Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST
Domaini235 – 420186FAD-binding PCMH-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the xanthine dehydrogenase family.Curated
Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
Contains 1 FAD-binding PCMH-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG4630.
HOGENOMiHOG000191197.
HOVERGENiHBG004182.
InParanoidiO54754.
KOiK00157.
PhylomeDBiO54754.

Family and domain databases

Gene3Di1.10.150.120. 1 hit.
3.10.20.30. 1 hit.
3.30.365.10. 6 hits.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.90.1170.50. 1 hit.
InterProiIPR002888. 2Fe-2S-bd.
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR000674. Ald_Oxase/Xan_DH_a/b.
IPR016208. Ald_Oxase/xanthine_DH.
IPR014313. Aldehyde_oxidase.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
IPR012675. Beta-grasp_dom.
IPR005107. CO_DH_flav_C.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR002346. Mopterin_DH_FAD-bd.
IPR022407. OxRdtase_Mopterin_BS.
[Graphical view]
PfamiPF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
PF03450. CO_deh_flav_C. 1 hit.
PF00941. FAD_binding_5. 1 hit.
PF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000127. Xanthine_DH. 1 hit.
SMARTiSM01008. Ald_Xan_dh_C. 1 hit.
SM01092. CO_deh_flav_C. 1 hit.
[Graphical view]
SUPFAMiSSF47741. SSF47741. 1 hit.
SSF54292. SSF54292. 1 hit.
SSF54665. SSF54665. 1 hit.
SSF55447. SSF55447. 1 hit.
SSF56003. SSF56003. 1 hit.
SSF56176. SSF56176. 1 hit.
TIGRFAMsiTIGR02969. mam_aldehyde_ox. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O54754-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDPIQLLFYV NGQKVVEKNV DPEMMLLPYL RKNLRLTGTK YGCGGGGCGA
60 70 80 90 100
CTVMISRYNP STKAIRHHPV NACLTPICSL HGTAVTTVEG LGNTRTRLHP
110 120 130 140 150
IQERIAKCHG TQCGFCTPGM VMSMYALLRN HPEPTLDQLT DALGGNLCRC
160 170 180 190 200
TGYRPIIDAC KTFCKASACC QSKENGVCCL DQEINGLAES QEEDKTSPEL
210 220 230 240 250
FSEEEFLPLD PTQELIFPPE LMRIAEKQPP KTRVFYGERV TWISPVTLKE
260 270 280 290 300
LVEAKFKYPQ APIVMGYTSV GPEVKFKGVF HPIIISPDRI EELGVISQAR
310 320 330 340 350
DGLTLGAGLS LDQVKDILAD IVQKLPEEKT QTYRALLKHL RTLAGSQIRN
360 370 380 390 400
MASLGGHIVS RHLDSDLNPL LAVGNCTLNL LSKDGERRIP LSEEFLRKCP
410 420 430 440 450
EADLKPQEVL VSVNIPWSRK WEFVSAFRQA QRQQNALAIV NSGMRVLFRE
460 470 480 490 500
GGGVIEELSI LYGGVGSTII SAKNSCQRLI GRPWNEGMLD TRCRLVLDEV
510 520 530 540 550
TLAASAPGGK VEFKRTLIIS FLFKFYLEVS QGLKREDPGH SPSLAGNHES
560 570 580 590 600
ALDDLHSKHP WRTLTHQNVD PAQLPQDPIG RPIMHLSGIK HATGEAIYCD
610 620 630 640 650
DMPAVDRELF LTFVTSSRAH AKIVSIDLSE ALSLPGVVDI ITADHLQEAN
660 670 680 690 700
TFGTETFLAT DEVHCVGHLV CAVIADSETR AKQAAKQVKV VYQDLAPLIL
710 720 730 740 750
TIEEAIQHKS FFKSERKLEC GNVDEAFKIV DQILEGEIHI GGQEHFYMET
760 770 780 790 800
QSMLVVPKGE DGEIDIYVST QFPKYIQDIV AATLKLSANK VMCHVRRVGG
810 820 830 840 850
AFGGKVGKTS ILAAITAFAA SKHGRAVRCI LERGEDMLIT GGRHPYLGKY
860 870 880 890 900
KAGFMNEGRI LALDVEHYCN GGCSLDESLW VIEMGLLKLD NAYKFPNLRC
910 920 930 940 950
RGWACRTNLP SNTALRGFGF PQAGLVTEAC ITEVAIKCGL SPEQVRTINM
960 970 980 990 1000
YKHVDTTHYK QEFSAKALSE CWRECMAKCS YFERKAAIGK FNAENSWKKR
1010 1020 1030 1040 1050
GMAVIPLKFP VGIGSVAMGQ AAALVHIYLD GSALVSHGGI EMGQGVHTKM
1060 1070 1080 1090 1100
IQVVSRELRM PMSSVHLRGT STETVPNTNA SGGSVVADLN GLAVKDACQT
1110 1120 1130 1140 1150
LLKRLEPIIS KNPQGTWKDW AQTAFDQSIS LSAVGYFRGY ESNIDWEKGE
1160 1170 1180 1190 1200
GHPFEYFVFG AACSEVEINC LTGDHKNIRT NIVMDVGHSI NPALDIGQVE
1210 1220 1230 1240 1250
GAFIQGMGLY TIEELSYSPQ GTLYSRGPNQ YKIPAICDIP TEMHISFLPP
1260 1270 1280 1290 1300
SEHSNTLYSS KGLGESGVFL GCSVFFAIHD AVKAARQERG ISGPWKLNSP
1310 1320 1330
LTPEKIRMAC EDKFTKMIPR DEPGSYVPCN IPV
Length:1,333
Mass (Da):146,678
Last modified:May 1, 1999 - v2
Checksum:i320CF0A3742F6AC5
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti109 – 1091H → Q in strain: 129/Sv.
Natural varianti168 – 1681A → G in strain: C57BL/6 X CBA and 129/Sv.
Natural varianti449 – 4491R → T in strain: C57BL/6 X CBA.
Natural varianti492 – 4921R → A in strain: C57BL/6 X CBA, requires 2 nucleotide substitutions.
Natural varianti686 – 6872KQ → NE in strain: 129/Sv.
Natural varianti857 – 8571E → D in strain: 129/Sv.
Natural varianti983 – 9831E → D in strain: C57BL/6 X CBA.
Natural varianti1169 – 11691N → D in strain: C57BL/6 X CBA and 129/Sv.
Natural varianti1329 – 13291C → W in strain: C57BL/6 X CBA and 129/Sv.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF076216 mRNA. Translation: AAC99382.1.
AB017482 mRNA. Translation: BAA36834.1.
AF121945
, AF121911, AF121912, AF121913, AF121914, AF121915, AF121916, AF121917, AF121918, AF121919, AF121920, AF121921, AF121922, AF121923, AF121924, AF121925, AF121926, AF121927, AF121928, AF121929, AF121930, AF121931, AF121932, AF121933, AF121934, AF121935, AF121936, AF121937, AF121938, AF121939, AF121940, AF121941, AF121942, AF121943, AF121944 Genomic DNA. Translation: AAD31763.1.
CCDSiCCDS35575.1.
RefSeqiNP_033806.2. NM_009676.2.
UniGeneiMm.26787.

Genome annotation databases

GeneIDi11761.
KEGGimmu:11761.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF076216 mRNA. Translation: AAC99382.1 .
AB017482 mRNA. Translation: BAA36834.1 .
AF121945
, AF121911 , AF121912 , AF121913 , AF121914 , AF121915 , AF121916 , AF121917 , AF121918 , AF121919 , AF121920 , AF121921 , AF121922 , AF121923 , AF121924 , AF121925 , AF121926 , AF121927 , AF121928 , AF121929 , AF121930 , AF121931 , AF121932 , AF121933 , AF121934 , AF121935 , AF121936 , AF121937 , AF121938 , AF121939 , AF121940 , AF121941 , AF121942 , AF121943 , AF121944 Genomic DNA. Translation: AAD31763.1 .
CCDSi CCDS35575.1.
RefSeqi NP_033806.2. NM_009676.2.
UniGenei Mm.26787.

3D structure databases

ProteinModelPortali O54754.
SMRi O54754. Positions 5-165, 200-533, 577-1315.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi O54754. 2 interactions.
MINTi MINT-1869370.

Chemistry

BindingDBi O54754.
ChEMBLi CHEMBL1641354.

PTM databases

PhosphoSitei O54754.

Proteomic databases

MaxQBi O54754.
PaxDbi O54754.
PRIDEi O54754.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 11761.
KEGGi mmu:11761.

Organism-specific databases

CTDi 316.
MGIi MGI:88035. Aox1.

Phylogenomic databases

eggNOGi COG4630.
HOGENOMi HOG000191197.
HOVERGENi HBG004182.
InParanoidi O54754.
KOi K00157.
PhylomeDBi O54754.

Miscellaneous databases

ChiTaRSi Aox1. mouse.
NextBioi 279515.
PROi O54754.
SOURCEi Search...

Gene expression databases

CleanExi MM_AOX1.
Genevestigatori O54754.

Family and domain databases

Gene3Di 1.10.150.120. 1 hit.
3.10.20.30. 1 hit.
3.30.365.10. 6 hits.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.90.1170.50. 1 hit.
InterProi IPR002888. 2Fe-2S-bd.
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR000674. Ald_Oxase/Xan_DH_a/b.
IPR016208. Ald_Oxase/xanthine_DH.
IPR014313. Aldehyde_oxidase.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
IPR012675. Beta-grasp_dom.
IPR005107. CO_DH_flav_C.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR002346. Mopterin_DH_FAD-bd.
IPR022407. OxRdtase_Mopterin_BS.
[Graphical view ]
Pfami PF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
PF03450. CO_deh_flav_C. 1 hit.
PF00941. FAD_binding_5. 1 hit.
PF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view ]
PIRSFi PIRSF000127. Xanthine_DH. 1 hit.
SMARTi SM01008. Ald_Xan_dh_C. 1 hit.
SM01092. CO_deh_flav_C. 1 hit.
[Graphical view ]
SUPFAMi SSF47741. SSF47741. 1 hit.
SSF54292. SSF54292. 1 hit.
SSF54665. SSF54665. 1 hit.
SSF55447. SSF55447. 1 hit.
SSF56003. SSF56003. 1 hit.
SSF56176. SSF56176. 1 hit.
TIGRFAMsi TIGR02969. mam_aldehyde_ox. 1 hit.
PROSITEi PS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning of the cDNA coding for mouse aldehyde oxidase: tissue distribution and regulation in vivo by testosterone."
    Kurosaki M., Demontis S., Barzago M.M., Garattini E., Terao M.
    Biochem. J. 341:71-80(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INDUCTION, TISSUE SPECIFICITY.
    Strain: CD-1.
    Tissue: Liver.
  2. "Molecular cloning of retinal oxidase/aldehyde oxidase cDNAs from rabbit and mouse livers and functional expression of recombinant mouse retinal oxidase cDNA in Escherichia coli."
    Huang D.-Y., Furukawa A., Ichikawa Y.
    Arch. Biochem. Biophys. 364:264-272(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION AS RETINAL OXIDASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, HOMODIMER.
    Strain: C57BL/6 X CBA.
    Tissue: Liver.
  3. "The mouse aldehyde oxidase gene: molecular cloning, chromosomal mapping and functional characterization of the 5'-flanking region."
    Demontis S., Kurosaki M., Saccone S., Salvatore M., Garattini E., Terao M.
    Biochim. Biophys. Acta 1489:207-222(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE.
    Strain: 129/Sv.
    Tissue: Thymus.
  4. "Selective localization of mouse aldehyde oxidase mRNA in the choroid plexus and motor neurons."
    Bendotti C., Prosperini E., Kurosaki M., Garattini E., Terao M.
    NeuroReport 8:2343-2349(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 561-746, TISSUE SPECIFICITY.
    Strain: C57BL/6J.
    Tissue: Liver.
  5. "Small-interference RNA-mediated knock-down of aldehyde oxidase 1 in 3T3-L1 cells impairs adipogenesis and adiponectin release."
    Weigert J., Neumeier M., Bauer S., Mages W., Schnitzbauer A.A., Obed A., Groeschl B., Hartmann A., Schaeffler A., Aslanidis C., Schoelmerich J., Buechler C.
    FEBS Lett. 582:2965-2972(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ADIPOGENESIS, DEVELOPMENTAL STAGE, INDUCTION.
  6. "Site directed mutagenesis of amino acid residues at the active site of mouse aldehyde oxidase AOX1."
    Schumann S., Terao M., Garattini E., Saggu M., Lendzian F., Hildebrandt P., Leimkuhler S.
    PLoS ONE 4:E5348-E5348(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS OXIDASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, HOMODIMER, KINETIC PARAMETERS, REACTION MECHANISM, ACTIVE SITE, MUTAGENESIS OF VAL-806; MET-884 AND GLU-1265.
  7. "Structure and evolution of vertebrate aldehyde oxidases: from gene duplication to gene suppression."
    Kurosaki M., Bolis M., Fratelli M., Barzago M.M., Pattini L., Perretta G., Terao M., Garattini E.
    Cell. Mol. Life Sci. 70:1807-1830(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, IDENTIFICATION OF PARALOGS.
  8. "Aldehyde oxidase importance in vivo in xenobiotic metabolism: imidacloprid nitroreduction in mice."
    Swenson T.L., Casida J.E.
    Toxicol. Sci. 133:22-28(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN XENOBIOTIC METABOLISM, TISSUE SPECIFICITY.

Entry informationi

Entry nameiAOXA_MOUSE
AccessioniPrimary (citable) accession number: O54754
Secondary accession number(s): Q9WU85, Q9Z2Z5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2002
Last sequence update: May 1, 1999
Last modified: November 26, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

AOX genes evolved from a xanthine oxidoreductase ancestral precursor via a series of gene duplication and suppression/deletion events. Different animal species contain a different complement of AOX genes encoding an equivalent number of AOX isoenzymes. In mammals, the two extremes are represented by certain rodents such as mice and rats, which are endowed with 4 AOX genes, and by humans, whose genome is characterized by a single active gene (PubMed:23263164).1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3