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Q06278

- AOXA_HUMAN

UniProt

Q06278 - AOXA_HUMAN

Protein

Aldehyde oxidase

Gene

AOX1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 2 (25 Nov 2008)
      Previous versions | rss
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    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 key 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. 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.8 Publications

    Catalytic activityi

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

    Cofactori

    Binds 2 2Fe-2S clusters per subunit.1 Publication
    Binds 1 FAD per subunit.1 Publication
    Binds 1 molybdenum-molybdopterin (Mo-MPT) cofactor per subunit.1 Publication

    Enzyme regulationi

    Is very potently inhibited by raloxifene. Also inhibited by estradiol, ethinyl estradiol, hydralazine, menadione, and isovanillin. Not inhibited by allopurinol, a xanthine dehydrogenase potent inhibitor.4 Publications

    Kineticsi

    kcat is 6.4 min(-1) for benzaldehyde oxidation, 5.6 min(-1) for phthalazine oxidation, 12.2 min(-1) for phenanthridine oxidation and 5.6 min(-1) for chloroquinazolinone oxidation.

    1. KM=7.1 µM for benzaldehyde (at 25 degrees Celsius and pH 7.5)3 Publications
    2. KM=1.3 µM for phthalazine (at 25 degrees Celsius and pH 7.5)3 Publications
    3. KM=3.9 µM for phenanthridine (at 25 degrees Celsius and pH 7.5)3 Publications
    4. KM=5.2 µM for chloroquinazolinone (at 25 degrees Celsius and pH 7.5)3 Publications
    5. KM=0.42 mM for 6-deoxypenciclovir (at 37 degrees Celsius and pH 7)3 Publications
    6. KM=0.15 mM for famciclovir (at 37 degrees Celsius and pH 7)3 Publications
    7. KM=6.3 µM for N-[(2-dimethylamino)ethyl]acridine-4-carboxamide (at 37 degrees Celsius and pH 7.4)3 Publications

    Vmax=16 nmol/min/mg enzyme with 6-deoxypenciclovir as substrate3 Publications

    Vmax=61 nmol/min/mg enzyme with famciclovir as substrate3 Publications

    Vmax=2.3 nmol/min/mg enzyme with N-[(2-dimethylamino)ethyl]acridine-4-carboxamide as substrate3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi44 – 441Iron-sulfur 1 (2Fe-2S)By similarity
    Metal bindingi49 – 491Iron-sulfur 1 (2Fe-2S)By similarity
    Metal bindingi52 – 521Iron-sulfur 1 (2Fe-2S)By similarity
    Metal bindingi74 – 741Iron-sulfur 1 (2Fe-2S)By similarity
    Binding sitei113 – 1131MolybdopterinBy similarity
    Metal bindingi114 – 1141Iron-sulfur 2 (2Fe-2S)By similarity
    Metal bindingi117 – 1171Iron-sulfur 2 (2Fe-2S)By similarity
    Metal bindingi149 – 1491Iron-sulfur 2 (2Fe-2S)By similarity
    Metal bindingi151 – 1511Iron-sulfur 2 (2Fe-2S)By similarity
    Binding sitei354 – 3541FADBy similarity
    Binding sitei358 – 3581FADBy similarity
    Binding sitei367 – 3671FADBy similarity
    Binding sitei411 – 4111FAD; via amide nitrogenBy similarity
    Binding sitei806 – 8061Molybdopterin; via amide nitrogenBy similarity
    Binding sitei1047 – 10471Molybdopterin; via amide nitrogenBy similarity
    Binding sitei1203 – 12031MolybdopterinBy similarity
    Active sitei1270 – 12701Proton acceptor; for azaheterocycle hydroxylase activityBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi264 – 2718FADBy similarity

    GO - Molecular functioni

    1. 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
    2. aldehyde oxidase activity Source: Reactome
    3. electron carrier activity Source: InterPro
    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
    9. xanthine dehydrogenase activity Source: ProtInc

    GO - Biological processi

    1. inflammatory response Source: ProtInc
    2. reactive oxygen species metabolic process Source: ProtInc
    3. small molecule metabolic process Source: Reactome
    4. vitamin B6 metabolic process Source: Reactome
    5. vitamin metabolic process Source: Reactome
    6. water-soluble vitamin metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000138356-MONOMER.
    ReactomeiREACT_25012. Vitamins B6 activation to pyridoxal phosphate.
    SABIO-RKQ06278.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aldehyde oxidase (EC:1.2.3.1)
    Alternative name(s):
    Aldehyde oxidase 1
    Azaheterocycle hydroxylase (EC:1.17.3.-)
    Gene namesi
    Name:AOX1
    Synonyms:AO
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:553. AOX1.

    Subcellular locationi

    Cytoplasm 3 Publications

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24842.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13381338Aldehyde oxidasePRO_0000166104Add
    BLAST

    Proteomic databases

    MaxQBiQ06278.
    PaxDbiQ06278.
    PRIDEiQ06278.

    PTM databases

    PhosphoSiteiQ06278.

    Expressioni

    Tissue specificityi

    Abundant in liver, expressed in adipose tissue and at lower levels in lung, skeletal muscle, pancreas. In contrast to mice, no significant gender difference in AOX1 expression level (at protein level).7 Publications

    Developmental stagei

    Not detected in preadipocytes but strongly induced in mature adipocytes.1 Publication

    Inductioni

    In liver, is down-regulated by adiponectin and by the PPARA agonist, fenofibric acid.1 Publication

    Gene expression databases

    ArrayExpressiQ06278.
    BgeeiQ06278.
    CleanExiHS_AOX1.
    GenevestigatoriQ06278.

    Organism-specific databases

    HPAiHPA040199.
    HPA040215.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi106813. 5 interactions.
    IntActiQ06278. 4 interactions.
    STRINGi9606.ENSP00000363832.

    Structurei

    3D structure databases

    ProteinModelPortaliQ06278.
    SMRiQ06278. Positions 4-166.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 92882Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
    BLAST
    Domaini236 – 421186FAD-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.
    KOiK00157.
    OMAiWACRTNL.
    OrthoDBiEOG7QRQSZ.
    PhylomeDBiQ06278.
    TreeFamiTF353036.

    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.

    Q06278-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDRASELLFY VNGRKVIEKN VDPETMLLPY LRKKLRLTGT KYGCGGGGCG     50
    ACTVMISRYN PITKRIRHHP ANACLIPICS LYGAAVTTVE GIGSTHTRIH 100
    PVQERIAKCH GTQCGFCTPG MVMSIYTLLR NHPEPTLDQL TDALGGNLCR 150
    CTGYRPIIDA CKTFCKTSGC CQSKENGVCC LDQGINGLPE FEEGSKTSPK 200
    LFAEEEFLPL DPTQELIFPP ELMIMAEKQS QRTRVFGSER MMWFSPVTLK 250
    ELLEFKFKYP QAPVIMGNTS VGPEVKFKGV FHPVIISPDR IEELSVVNHA 300
    YNGLTLGAGL SLAQVKDILA DVVQKLPEEK TQMYHALLKH LGTLAGSQIR 350
    NMASLGGHII SRHPDSDLNP ILAVGNCTLN LLSKEGKRQI PLNEQFLSKC 400
    PNADLKPQEI LVSVNIPYSR KWEFVSAFRQ AQRQENALAI VNSGMRVFFG 450
    EGDGIIRELC ISYGGVGPAT ICAKNSCQKL IGRHWNEQML DIACRLILNE 500
    VSLLGSAPGG KVEFKRTLII SFLFKFYLEV SQILKKMDPV HYPSLADKYE 550
    SALEDLHSKH HCSTLKYQNI GPKQHPEDPI GHPIMHLSGV KHATGEAIYC 600
    DDMPLVDQEL FLTFVTSSRA HAKIVSIDLS EALSMPGVVD IMTAEHLSDV 650
    NSFCFFTEAE KFLATDKVFC VGQLVCAVLA DSEVQAKRAA KRVKIVYQDL 700
    EPLILTIEES IQHNSSFKPE RKLEYGNVDE AFKVVDQILE GEIHMGGQEH 750
    FYMETQSMLV VPKGEDQEMD VYVSTQFPKY IQDIVASTLK LPANKVMCHV 800
    RRVGGAFGGK VLKTGIIAAV TAFAANKHGR AVRCVLERGE DMLITGGRHP 850
    YLGKYKAGFM NDGRILALDM EHYSNAGASL DESLFVIEMG LLKMDNAYKF 900
    PNLRCRGWAC RTNLPSNTAF RGFGFPQAAL ITESCITEVA AKCGLSPEKV 950
    RIINMYKEID QTPYKQEINA KNLIQCWREC MAMSSYSLRK VAVEKFNAEN 1000
    YWKKKGLAMV PLKFPVGLGS RAAGQAAALV HIYLDGSVLV THGGIEMGQG 1050
    VHTKMIQVVS RELRMPMSNV HLRGTSTETV PNANISGGSV VADLNGLAVK 1100
    DACQTLLKRL EPIISKNPKG TWKDWAQTAF DESINLSAVG YFRGYESDMN 1150
    WEKGEGQPFE YFVYGAACSE VEIDCLTGDH KNIRTDIVMD VGCSINPAID 1200
    IGQIEGAFIQ GMGLYTIEEL NYSPQGILHT RGPDQYKIPA ICDMPTELHI 1250
    ALLPPSQNSN TLYSSKGLGE SGVFLGCSVF FAIHDAVSAA RQERGLHGPL 1300
    TLNSPLTPEK IRMACEDKFT KMIPRDEPGS YVPWNVPI 1338
    Length:1,338
    Mass (Da):147,918
    Last modified:November 25, 2008 - v2
    Checksum:i2AB5E543F18C9261
    GO

    Sequence cautioni

    The sequence AAA96650.1 differs from that shown. Reason: Frameshift at positions 284, 286, 294 and 302.
    The sequence AAB83966.1 differs from that shown. Reason: Frameshift at positions 284, 286, 294 and 302.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti41 – 411K → P in AAA96650. (PubMed:8248161)Curated
    Sequence conflicti41 – 411K → P in AAB83966. 1 PublicationCurated
    Sequence conflicti127 – 1271T → P in AAA96650. (PubMed:8248161)Curated
    Sequence conflicti127 – 1271T → P in AAB83966. 1 PublicationCurated
    Sequence conflicti152 – 1521T → H in AAA96650. (PubMed:8248161)Curated
    Sequence conflicti152 – 1521T → H in AAB83966. 1 PublicationCurated
    Sequence conflicti227 – 2271E → D in AAA96650. (PubMed:8248161)Curated
    Sequence conflicti227 – 2271E → D in AAB83966. 1 PublicationCurated
    Sequence conflicti251 – 2511E → D in AAA96650. (PubMed:8248161)Curated
    Sequence conflicti418 – 4181Y → I in AAA96650. (PubMed:8248161)Curated
    Sequence conflicti418 – 4181Y → I in AAB83966. 1 PublicationCurated
    Sequence conflicti501 – 5011V → L in AAB83966. 1 PublicationCurated
    Sequence conflicti627 – 6271I → N in AAB83966. 1 PublicationCurated
    Sequence conflicti929 – 9291A → V in AAA96650. (PubMed:8248161)Curated
    Sequence conflicti929 – 9291A → V in AAB83966. 1 PublicationCurated
    Sequence conflicti1019 – 10191G → A in AAA96650. (PubMed:8248161)Curated
    Sequence conflicti1019 – 10191G → A in AAB83966. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti314 – 3141Q → R.
    Corresponds to variant rs58185012 [ dbSNP | Ensembl ].
    VAR_061136
    Natural varianti802 – 8021R → C Decreases homodimerization but nearly no effect on kinetic parameters. 1 Publication
    Corresponds to variant rs41309768 [ dbSNP | Ensembl ].
    VAR_047517
    Natural varianti921 – 9211R → H Increases homodimerization; abolishes enzymatic activity on phenanthridine; decreases turnover number with benzaldehyde, phtalazine and chloroquinazolinone as substrate, while nearly no effect on the KM. 1 Publication
    Corresponds to variant rs56199635 [ dbSNP | Ensembl ].
    VAR_070256
    Natural varianti1135 – 11351N → S Increases homodimerization and turnover number with phenanthridine as substrate; nearly no effect on kinetic parameters with benzaldehyde, phtalazine and chloroquinazolinone as substrate. 1 Publication
    Corresponds to variant rs55754655 [ dbSNP | Ensembl ].
    VAR_070257
    Natural varianti1271 – 12711S → L.1 Publication
    Corresponds to variant rs141786030 [ dbSNP | Ensembl ].
    VAR_070258
    Natural varianti1297 – 12971H → R Increases homodimerization and turnover number with phenanthridine as substrate; nearly no effect on kinetic parameters with benzaldehyde, phtalazine and chloroquinazolinone as substrate. 1 Publication
    Corresponds to variant rs3731722 [ dbSNP | Ensembl ].
    VAR_047518

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L11005 mRNA. Translation: AAA96650.1. Frameshift.
    AF017060
    , AF009441, AF009442, AF009443, AF009444, AF009445, AF009446, AF009447, AF009448, AF009449, AF009450, AF009451, AF009452, AF009453, AF009454, AF009455, AF009456, AF009457, AF009458, AF009459, AF009460, AF009461, AF009462, AF009463, AF009464, AF009465, AF009466, AF009467, AF009468, AF009469, AF009470, AF009471, AF009472, AF009473, AF009474 Genomic DNA. Translation: AAB83966.1. Frameshift.
    AF010260 Genomic DNA. Translation: AAB83968.1.
    AB046692 mRNA. Translation: BAB40305.1.
    AC007163 Genomic DNA. Translation: AAX93285.1.
    AC080164 Genomic DNA. Translation: AAY24265.1.
    CH471063 Genomic DNA. Translation: EAW70209.1.
    BC117179 mRNA. Translation: AAI17180.1.
    BC117181 mRNA. Translation: AAI17182.1.
    CCDSiCCDS33360.1.
    PIRiA49634.
    RefSeqiNP_001150.3. NM_001159.3.
    UniGeneiHs.406238.

    Genome annotation databases

    EnsembliENST00000374700; ENSP00000363832; ENSG00000138356.
    GeneIDi316.
    KEGGihsa:316.
    UCSCiuc002uvx.3. human.

    Polymorphism databases

    DMDMi215273968.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L11005 mRNA. Translation: AAA96650.1 . Frameshift.
    AF017060
    , AF009441 , AF009442 , AF009443 , AF009444 , AF009445 , AF009446 , AF009447 , AF009448 , AF009449 , AF009450 , AF009451 , AF009452 , AF009453 , AF009454 , AF009455 , AF009456 , AF009457 , AF009458 , AF009459 , AF009460 , AF009461 , AF009462 , AF009463 , AF009464 , AF009465 , AF009466 , AF009467 , AF009468 , AF009469 , AF009470 , AF009471 , AF009472 , AF009473 , AF009474 Genomic DNA. Translation: AAB83966.1 . Frameshift.
    AF010260 Genomic DNA. Translation: AAB83968.1 .
    AB046692 mRNA. Translation: BAB40305.1 .
    AC007163 Genomic DNA. Translation: AAX93285.1 .
    AC080164 Genomic DNA. Translation: AAY24265.1 .
    CH471063 Genomic DNA. Translation: EAW70209.1 .
    BC117179 mRNA. Translation: AAI17180.1 .
    BC117181 mRNA. Translation: AAI17182.1 .
    CCDSi CCDS33360.1.
    PIRi A49634.
    RefSeqi NP_001150.3. NM_001159.3.
    UniGenei Hs.406238.

    3D structure databases

    ProteinModelPortali Q06278.
    SMRi Q06278. Positions 4-166.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106813. 5 interactions.
    IntActi Q06278. 4 interactions.
    STRINGi 9606.ENSP00000363832.

    Chemistry

    BindingDBi Q06278.
    ChEMBLi CHEMBL3257.
    DrugBanki DB00484. Brimonidine.
    DB00477. Chlorpromazine.
    DB00426. Famciclovir.
    DB00170. Menadione.
    DB00563. Methotrexate.
    DB00157. NADH.
    DB00377. Palonosetron.
    DB00299. Penciclovir.
    DB00481. Raloxifene.
    DB00962. Zaleplon.
    DB00909. Zonisamide.

    PTM databases

    PhosphoSitei Q06278.

    Polymorphism databases

    DMDMi 215273968.

    Proteomic databases

    MaxQBi Q06278.
    PaxDbi Q06278.
    PRIDEi Q06278.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000374700 ; ENSP00000363832 ; ENSG00000138356 .
    GeneIDi 316.
    KEGGi hsa:316.
    UCSCi uc002uvx.3. human.

    Organism-specific databases

    CTDi 316.
    GeneCardsi GC02P201450.
    H-InvDB HIX0029780.
    HGNCi HGNC:553. AOX1.
    HPAi HPA040199.
    HPA040215.
    MIMi 602841. gene.
    neXtProti NX_Q06278.
    PharmGKBi PA24842.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4630.
    HOGENOMi HOG000191197.
    HOVERGENi HBG004182.
    KOi K00157.
    OMAi WACRTNL.
    OrthoDBi EOG7QRQSZ.
    PhylomeDBi Q06278.
    TreeFami TF353036.

    Enzyme and pathway databases

    BioCyci MetaCyc:ENSG00000138356-MONOMER.
    Reactomei REACT_25012. Vitamins B6 activation to pyridoxal phosphate.
    SABIO-RK Q06278.

    Miscellaneous databases

    ChiTaRSi AOX1. human.
    GeneWikii Aldehyde_oxidase_1.
    GenomeRNAii 316.
    NextBioi 1283.
    PROi Q06278.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q06278.
    Bgeei Q06278.
    CleanExi HS_AOX1.
    Genevestigatori Q06278.

    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. "cDNA cloning, characterization, and tissue-specific expression of human xanthine dehydrogenase/xanthine oxidase."
      Wright R.M., Vaitaitis G.M., Wilson C.M., Repine T.B., Terada L.S., Repine J.E.
      Proc. Natl. Acad. Sci. U.S.A. 90:10690-10694(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Tissue: Liver.
    2. "Molecular cloning, refined chromosomal mapping, and structural analysis of the human gene encoding aldehyde oxidase (AOX1), a candidate for the ALS2 gene."
      Wright R.M., Weigel L.K., Varella-Garcia M., Vaitaitis G., Repine J.E.
      Redox Rep. 3:135-144(1997)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Mutation of human molybdenum cofactor sulfurase gene is responsible to classical xanthinuria type II."
      Ichida K., Matsumura T., Sakuma R., Hosoya T., Nishino T.
      Biochem. Biophys. Res. Commun. 282:1194-1200(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Colon.
    7. "Substrate specificity of human liver aldehyde oxidase toward substituted quinazolines and phthalazines: a comparison with hepatic enzyme from guinea pig, rabbit, and baboon."
      Beedham C., Critchley D.J., Rance D.J.
      Arch. Biochem. Biophys. 319:481-490(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS AZAHETEROCYCLE OXIDASE, SUBSTRATE SPECIFICITY.
    8. "In vitro oxidation of famciclovir and 6-deoxypenciclovir by aldehyde oxidase from human, guinea pig, rabbit, and rat liver."
      Rashidi M.R., Smith J.A., Clarke S.E., Beedham C.
      Drug Metab. Dispos. 25:805-813(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS AZAHETEROCYCLE OXIDASE, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    9. "Aldehyde oxidase 1 is highly abundant in hepatic steatosis and is down-regulated by adiponectin and fenofibric acid in hepatocytes in vitro."
      Neumeier M., Weigert J., Schaeffler A., Weiss T.S., Schmidl C., Buettner R., Bollheimer C., Aslanidis C., Schoelmerich J., Buechler C.
      Biochem. Biophys. Res. Commun. 350:731-735(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    10. "Mammalian aldehyde oxidases: genetics, evolution and biochemistry."
      Garattini E., Fratelli M., Terao M.
      Cell. Mol. Life Sci. 65:1019-1048(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW, NOMENCLATURE, TISSUE SPECIFICITY.
    11. "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: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION.
    12. "In vitro-in vivo correlation for intrinsic clearance for drugs metabolized by human aldehyde oxidase."
      Zientek M., Jiang Y., Youdim K., Obach R.S.
      Drug Metab. Dispos. 38:1322-1327(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS DRUG-METABOLIZING ENZYME, SUBSTRATE SPECIFICITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    13. "Characterization of aldehyde oxidase enzyme activity in cryopreserved human hepatocytes."
      Hutzler J.M., Yang Y.S., Albaugh D., Fullenwider C.L., Schmenk J., Fisher M.B.
      Drug Metab. Dispos. 40:267-275(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS DRUG-METABOLIZING ENZYME, ENZYME REGULATION, SUBSTRATE SPECIFICITY, TISSUE SPECIFICITY.
    14. "Hydralazine as a selective probe inactivator of aldehyde oxidase in human hepatocytes: estimation of the contribution of aldehyde oxidase to metabolic clearance."
      Strelevitz T.J., Orozco C.C., Obach R.S.
      Drug Metab. Dispos. 40:1441-1448(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS DRUG-METABOLIZING ENZYME, ENZYME REGULATION, SUBSTRATE SPECIFICITY, TISSUE SPECIFICITY.
    15. Cited for: REVIEW.
    16. "Evidence for substrate-dependent inhibition profiles for human liver aldehyde oxidase."
      Barr J.T., Jones J.P.
      Drug Metab. Dispos. 41:24-29(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS AZAHETEROCYCLE OXIDASE, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    17. "Aldehyde oxidase 1 (AOX1) in human liver cytosols: quantitative characterization of AOX1 expression level and activity relationship."
      Fu C., Di L., Han X., Soderstrom C., Snyder M., Troutman M.D., Obach R.S., Zhang H.
      Drug Metab. Dispos. 41:1797-1804(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS DRUG-METABOLIZING ENZYME, SUBSTRATE SPECIFICITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    18. "The impact of single nucleotide polymorphisms on human aldehyde oxidase."
      Hartmann T., Terao M., Garattini E., Teutloff C., Alfaro J.F., Jones J.P., Leimkuehler S.
      Drug Metab. Dispos. 40:856-864(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CYS-802; HIS-921; SER-1135; LEU-1271 AND ARG-1297, CHARACTERIZATION OF VARIANTS CYS-802; HIS-921; SER-1135 AND ARG-1297, FUNCTION AS OXIDASE, HOMODIMER, COFACTOR, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiAOXA_HUMAN
    AccessioniPrimary (citable) accession number: Q06278
    Secondary accession number(s): O14765
    , Q53RR8, Q53TV3, Q9BYF0, Q9UPG6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 145 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    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:22335465).1 Publication

    Caution

    Was originally thought to be a xanthine dehydrogenase.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

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