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Q06278 (AOXA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aldehyde oxidase

EC=1.2.3.1
Alternative name(s):
Aldehyde oxidase 1
Azaheterocycle hydroxylase
EC=1.17.3.-
Gene names
Name:AOX1
Synonyms:AO
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1338 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7 Ref.8 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18

Catalytic activity

An aldehyde + H2O + O2 = a carboxylate + H2O2. Ref.8 Ref.16

Retinal + O2 + H2O = retinoate + H2O2. Ref.8 Ref.16

Cofactor

Binds 2 2Fe-2S clusters per subunit. Ref.18

Binds 1 FAD per subunit. Ref.18

Binds 1 molybdenum-molybdopterin (Mo-MPT) cofactor per subunit. Ref.18

Enzyme regulation

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. Ref.8 Ref.13 Ref.14 Ref.16

Subunit structure

Homodimer.

Subcellular location

Cytoplasm Ref.11 Ref.12 Ref.17.

Tissue specificity

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). Ref.1 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.17

Developmental stage

Not detected in preadipocytes but strongly induced in mature adipocytes. Ref.11

Induction

In liver, is down-regulated by adiponectin and by the PPARA agonist, fenofibric acid. Ref.8 Ref.9 Ref.13 Ref.14 Ref.16

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 (Ref.15).

Sequence similarities

Belongs to the xanthine dehydrogenase family.

Contains 1 2Fe-2S ferredoxin-type domain.

Contains 1 FAD-binding PCMH-type domain.

Caution

Was originally (Ref.1) thought to be a xanthine dehydrogenase.

Biophysicochemical properties

Kinetic parameters:

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.

KM=7.1 µM for benzaldehyde (at 25 degrees Celsius and pH 7.5) Ref.8 Ref.16 Ref.18

KM=1.3 µM for phthalazine (at 25 degrees Celsius and pH 7.5)

KM=3.9 µM for phenanthridine (at 25 degrees Celsius and pH 7.5)

KM=5.2 µM for chloroquinazolinone (at 25 degrees Celsius and pH 7.5)

KM=0.42 mM for 6-deoxypenciclovir (at 37 degrees Celsius and pH 7)

KM=0.15 mM for famciclovir (at 37 degrees Celsius and pH 7)

KM=6.3 µM for N-[(2-dimethylamino)ethyl]acridine-4-carboxamide (at 37 degrees Celsius and pH 7.4)

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

Vmax=61 nmol/min/mg enzyme with famciclovir as substrate

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

Sequence caution

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.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   Ligand2Fe-2S
FAD
Flavoprotein
Iron
Iron-sulfur
Metal-binding
Molybdenum
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processinflammatory response

Traceable author statement Ref.1. Source: ProtInc

reactive oxygen species metabolic process

Traceable author statement PubMed 7570184. Source: ProtInc

small molecule metabolic process

Traceable author statement. Source: Reactome

vitamin B6 metabolic process

Traceable author statement. Source: Reactome

vitamin metabolic process

Traceable author statement. Source: Reactome

water-soluble vitamin metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

   Molecular_function2 iron, 2 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

NAD binding

Inferred from electronic annotation. Source: InterPro

UDP-N-acetylmuramate dehydrogenase activity

Inferred from electronic annotation. Source: InterPro

aldehyde oxidase activity

Traceable author statement. Source: Reactome

electron carrier activity

Inferred from electronic annotation. Source: InterPro

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

iron ion binding

Inferred from electronic annotation. Source: InterPro

molybdopterin cofactor binding

Inferred from electronic annotation. Source: InterPro

xanthine dehydrogenase activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13381338Aldehyde oxidase
PRO_0000166104

Regions

Domain5 – 92882Fe-2S ferredoxin-type
Domain236 – 421186FAD-binding PCMH-type
Nucleotide binding264 – 2718FAD By similarity

Sites

Active site12701Proton acceptor; for azaheterocycle hydroxylase activity By similarity
Metal binding441Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding491Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding521Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding741Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding1141Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1171Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1491Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1511Iron-sulfur 2 (2Fe-2S) By similarity
Binding site1131Molybdopterin By similarity
Binding site3541FAD By similarity
Binding site3581FAD By similarity
Binding site3671FAD By similarity
Binding site4111FAD; via amide nitrogen By similarity
Binding site8061Molybdopterin; via amide nitrogen By similarity
Binding site10471Molybdopterin; via amide nitrogen By similarity
Binding site12031Molybdopterin By similarity

Natural variations

Natural variant3141Q → R.
Corresponds to variant rs58185012 [ dbSNP | Ensembl ].
VAR_061136
Natural variant8021R → C Decreases homodimerization but nearly no effect on kinetic parameters. Ref.18
Corresponds to variant rs41309768 [ dbSNP | Ensembl ].
VAR_047517
Natural variant9211R → 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. Ref.18
Corresponds to variant rs56199635 [ dbSNP | Ensembl ].
VAR_070256
Natural variant11351N → S Increases homodimerization and turnover number with phenanthridine as substrate; nearly no effect on kinetic parameters with benzaldehyde, phtalazine and chloroquinazolinone as substrate. Ref.18
Corresponds to variant rs55754655 [ dbSNP | Ensembl ].
VAR_070257
Natural variant12711S → L. Ref.18
Corresponds to variant rs141786030 [ dbSNP | Ensembl ].
VAR_070258
Natural variant12971H → R Increases homodimerization and turnover number with phenanthridine as substrate; nearly no effect on kinetic parameters with benzaldehyde, phtalazine and chloroquinazolinone as substrate. Ref.18
Corresponds to variant rs3731722 [ dbSNP | Ensembl ].
VAR_047518

Experimental info

Sequence conflict411K → P in AAA96650. Ref.1
Sequence conflict411K → P in AAB83966. Ref.2
Sequence conflict1271T → P in AAA96650. Ref.1
Sequence conflict1271T → P in AAB83966. Ref.2
Sequence conflict1521T → H in AAA96650. Ref.1
Sequence conflict1521T → H in AAB83966. Ref.2
Sequence conflict2271E → D in AAA96650. Ref.1
Sequence conflict2271E → D in AAB83966. Ref.2
Sequence conflict2511E → D in AAA96650. Ref.1
Sequence conflict4181Y → I in AAA96650. Ref.1
Sequence conflict4181Y → I in AAB83966. Ref.2
Sequence conflict5011V → L in AAB83966. Ref.2
Sequence conflict6271I → N in AAB83966. Ref.2
Sequence conflict9291A → V in AAA96650. Ref.1
Sequence conflict9291A → V in AAB83966. Ref.2
Sequence conflict10191G → A in AAA96650. Ref.1
Sequence conflict10191G → A in AAB83966. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q06278 [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: 2AB5E543F18C9261

FASTA1,338147,918
        10         20         30         40         50         60 
MDRASELLFY VNGRKVIEKN VDPETMLLPY LRKKLRLTGT KYGCGGGGCG ACTVMISRYN 

        70         80         90        100        110        120 
PITKRIRHHP ANACLIPICS LYGAAVTTVE GIGSTHTRIH PVQERIAKCH GTQCGFCTPG 

       130        140        150        160        170        180 
MVMSIYTLLR NHPEPTLDQL TDALGGNLCR CTGYRPIIDA CKTFCKTSGC CQSKENGVCC 

       190        200        210        220        230        240 
LDQGINGLPE FEEGSKTSPK LFAEEEFLPL DPTQELIFPP ELMIMAEKQS QRTRVFGSER 

       250        260        270        280        290        300 
MMWFSPVTLK ELLEFKFKYP QAPVIMGNTS VGPEVKFKGV FHPVIISPDR IEELSVVNHA 

       310        320        330        340        350        360 
YNGLTLGAGL SLAQVKDILA DVVQKLPEEK TQMYHALLKH LGTLAGSQIR NMASLGGHII 

       370        380        390        400        410        420 
SRHPDSDLNP ILAVGNCTLN LLSKEGKRQI PLNEQFLSKC PNADLKPQEI LVSVNIPYSR 

       430        440        450        460        470        480 
KWEFVSAFRQ AQRQENALAI VNSGMRVFFG EGDGIIRELC ISYGGVGPAT ICAKNSCQKL 

       490        500        510        520        530        540 
IGRHWNEQML DIACRLILNE VSLLGSAPGG KVEFKRTLII SFLFKFYLEV SQILKKMDPV 

       550        560        570        580        590        600 
HYPSLADKYE SALEDLHSKH HCSTLKYQNI GPKQHPEDPI GHPIMHLSGV KHATGEAIYC 

       610        620        630        640        650        660 
DDMPLVDQEL FLTFVTSSRA HAKIVSIDLS EALSMPGVVD IMTAEHLSDV NSFCFFTEAE 

       670        680        690        700        710        720 
KFLATDKVFC VGQLVCAVLA DSEVQAKRAA KRVKIVYQDL EPLILTIEES IQHNSSFKPE 

       730        740        750        760        770        780 
RKLEYGNVDE AFKVVDQILE GEIHMGGQEH FYMETQSMLV VPKGEDQEMD VYVSTQFPKY 

       790        800        810        820        830        840 
IQDIVASTLK LPANKVMCHV RRVGGAFGGK VLKTGIIAAV TAFAANKHGR AVRCVLERGE 

       850        860        870        880        890        900 
DMLITGGRHP YLGKYKAGFM NDGRILALDM EHYSNAGASL DESLFVIEMG LLKMDNAYKF 

       910        920        930        940        950        960 
PNLRCRGWAC RTNLPSNTAF RGFGFPQAAL ITESCITEVA AKCGLSPEKV RIINMYKEID 

       970        980        990       1000       1010       1020 
QTPYKQEINA KNLIQCWREC MAMSSYSLRK VAVEKFNAEN YWKKKGLAMV PLKFPVGLGS 

      1030       1040       1050       1060       1070       1080 
RAAGQAAALV HIYLDGSVLV THGGIEMGQG VHTKMIQVVS RELRMPMSNV HLRGTSTETV 

      1090       1100       1110       1120       1130       1140 
PNANISGGSV VADLNGLAVK DACQTLLKRL EPIISKNPKG TWKDWAQTAF DESINLSAVG 

      1150       1160       1170       1180       1190       1200 
YFRGYESDMN WEKGEGQPFE YFVYGAACSE VEIDCLTGDH KNIRTDIVMD VGCSINPAID 

      1210       1220       1230       1240       1250       1260 
IGQIEGAFIQ GMGLYTIEEL NYSPQGILHT RGPDQYKIPA ICDMPTELHI ALLPPSQNSN 

      1270       1280       1290       1300       1310       1320 
TLYSSKGLGE SGVFLGCSVF FAIHDAVSAA RQERGLHGPL TLNSPLTPEK IRMACEDKFT 

      1330 
KMIPRDEPGS YVPWNVPI 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"The role of aldehyde oxidase in drug metabolism."
Garattini E., Terao M.
Expert Opin. Drug Metab. Toxicol. 8:487-503(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L11005 mRNA. Translation: AAA96650.1. Frameshift.
AF017060 expand/collapse EMBL AC list , 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.
CCDSCCDS33360.1.
PIRA49634.
RefSeqNP_001150.3. NM_001159.3.
UniGeneHs.406238.

3D structure databases

ProteinModelPortalQ06278.
SMRQ06278. Positions 4-166.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106813. 5 interactions.
IntActQ06278. 4 interactions.
STRING9606.ENSP00000363832.

Chemistry

BindingDBQ06278.
ChEMBLCHEMBL3257.
DrugBankDB00484. Brimonidine.
DB00477. Chlorpromazine.
DB00426. Famciclovir.
DB00170. Menadione.
DB00563. Methotrexate.
DB00157. NADH.
DB00377. Palonosetron.
DB00299. Penciclovir.
DB00481. Raloxifene.
DB00962. Zaleplon.
DB00909. Zonisamide.

PTM databases

PhosphoSiteQ06278.

Polymorphism databases

DMDM215273968.

Proteomic databases

MaxQBQ06278.
PaxDbQ06278.
PRIDEQ06278.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374700; ENSP00000363832; ENSG00000138356.
GeneID316.
KEGGhsa:316.
UCSCuc002uvx.3. human.

Organism-specific databases

CTD316.
GeneCardsGC02P201450.
H-InvDBHIX0029780.
HGNCHGNC:553. AOX1.
HPAHPA040199.
HPA040215.
MIM602841. gene.
neXtProtNX_Q06278.
PharmGKBPA24842.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4630.
HOGENOMHOG000191197.
HOVERGENHBG004182.
KOK00157.
OMAWACRTNL.
OrthoDBEOG7QRQSZ.
PhylomeDBQ06278.
TreeFamTF353036.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000138356-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
SABIO-RKQ06278.

Gene expression databases

ArrayExpressQ06278.
BgeeQ06278.
CleanExHS_AOX1.
GenevestigatorQ06278.

Family and domain databases

Gene3D1.10.150.120. 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.
InterProIPR002888. 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]
PfamPF01315. 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]
PIRSFPIRSF000127. Xanthine_DH. 1 hit.
SMARTSM01008. Ald_Xan_dh_C. 1 hit.
SM01092. CO_deh_flav_C. 1 hit.
[Graphical view]
SUPFAMSSF47741. SSF47741. 1 hit.
SSF54292. SSF54292. 1 hit.
SSF54665. SSF54665. 1 hit.
SSF55447. SSF55447. 1 hit.
SSF56003. SSF56003. 1 hit.
SSF56176. SSF56176. 1 hit.
TIGRFAMsTIGR02969. mam_aldehyde_ox. 1 hit.
PROSITEPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAOX1. human.
GeneWikiAldehyde_oxidase_1.
GenomeRNAi316.
NextBio1283.
PROQ06278.
SOURCESearch...

Entry information

Entry nameAOXA_HUMAN
AccessionPrimary (citable) accession number: Q06278
Secondary accession number(s): O14765 expand/collapse secondary AC list , Q53RR8, Q53TV3, Q9BYF0, Q9UPG6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 25, 2008
Last modified: July 9, 2014
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM