[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; PubMed=8248161 [NCBI, ExPASy, EBI, Israel, Japan] Wright R.M., Vaitaitis G.M., Wilson C.M., Repine T.B., Terada L.S., Repine J.E.; "cDNA cloning, characterization, and tissue-specific expression of human xanthine dehydrogenase/xanthine oxidase."; Proc. Natl. Acad. Sci. U.S.A. 90:10690-10694(1993).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Wright R.M., Weigel L.K., Varella-Garcia M., Vaitaitis G., Repine J.E.; "Molecular cloning, refined chromosomal mapping, and structural analysis of the human gene encoding aldehyde oxidase (AOX1), a candidate for the ALS2 gene."; Redox Rep. 3:135-144(1997).

Comments

CATALYTIC ACTIVITY: An aldehyde + H₂O + O₂ = a carboxylic acid + H₂O₂.
COFACTOR: Binds 2 2Fe-2S clusters.
COFACTOR: FAD.
COFACTOR: Molybdopterin.
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Cytoplasm.
TISSUE SPECIFICITY: Abundant in liver, lower levels in lung, skeletal muscle, pancreas. Undetected in heart, brain and kidney.
SIMILARITY: Belongs to the xanthine dehydrogenase family.
SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain.
SIMILARITY: Contains 1 FAD-binding PCMH-type domain.
CAUTION: Was originally (PubMed:8248161) thought to be a xanthine dehydrogenase.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

L11005; AAA96650.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF017060; AAB83966.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF009441; AAB83966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF009442; AAB83966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF009443; AAB83966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF009444; AAB83966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF009445; AAB83966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF009446; AAB83966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF009447; AAB83966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF009448; AAB83966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF009449; AAB83966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF009450; AAB83966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF009451; AAB83966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF009452; AAB83966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF009453; AAB83966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF009454; AAB83966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF009455; AAB83966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF009456; AAB83966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF009457; AAB83966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF009458; AAB83966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF009459; AAB83966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF009460; AAB83966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF009461; AAB83966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF009462; AAB83966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF009463; AAB83966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF009464; AAB83966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF009465; AAB83966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF009466; AAB83966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF009467; AAB83966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF009468; AAB83966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF009469; AAB83966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF009470; AAB83966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF009471; AAB83966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF009472; AAB83966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF009473; AAB83966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF009474; AAB83966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF010260; AAB83968.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A49634; A49634.

UniGene

Hs.406238

3D structure databases

HSSP

P80457; 1FO4. [HSSP ENTRY / PDB]

ModBase

Q06278.

Enzyme and pathway databases

BioCyc

MetaCyc:ENSG00000138356-MON; -.

Organism-specific databases

HIX0029780; -.

HGNC:553; AOX1.

602841; gene. [NCBI / EBI]

PharmGKB

PA24842; -.

GeneCards

Q06278.

Gene expression databases

ArrayExpress

Q06278; -.

CleanEx

HS_AOX1; -.

GermOnline

ENSG00000138356; Homo sapiens.

Ontologies

GO:0004031;	Molecular function: aldehyde oxidase activity (traceable author statement from ProtInc).
GO:0004854;	Molecular function: xanthine dehydrogenase activity (traceable author statement from ProtInc).
GO:0006954;	Biological process: inflammatory response (traceable author statement from ProtInc).
GO:0006800;	Biological process: oxygen and reactive oxygen species metabolic process (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR002888; 2Fe-2S_bd.
IPR006058; 2Fe2S_fd_BS.
IPR000674; Ald_Oxase/Xan_DHase_a/b.
IPR016208; Ald_Oxase/xanthine_DHase.
IPR014313; Aldehyde_oxidase.
IPR008274; AldOxase/xan_DHase_Mopterin-bd.
IPR012675; b-grasp_ferredoxin-like.
IPR005107; CO_DHase_flav_C.
IPR016169; CO_DHase_flavot_FAD-bd_sub2.
IPR016167; FAD-bd_2_sub1.
IPR001041; Ferredoxin.
IPR002346; Mopterin_DHase_FAD-bd.
IPR000572; OxRdtase_Mopterin-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.365.10; Ald_xan_DH_mo_bd; 2.
G3DSA:3.90.1170.50; Aldxan_DH_hamm; 1.
G3DSA:3.30.390.50; CO_DH_flav_C; 1.
G3DSA:3.30.465.10; CO_DH_flavoprot_FAD-bd_sub2; 1.
G3DSA:3.30.43.10; FAD-binding_2_sub1; 1.
G3DSA:3.10.20.30; Ferredoxin_fold; 1.

Pfam

PF01315; Ald_Xan_dh_C; 1.
PF02738; Ald_Xan_dh_C2; 1.
PF03450; CO_deh_flav_C; 1.
PF00941; FAD_binding_5; 1.
PF00111; Fer2; 1.
PF01799; Fer2_2; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000127; Xanthine_DH; 1.

ProDom

PD186071; 2Fe-2S_bind; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR02969; mam_aldehyde_ox; 1.

PROSITE

PS00197; 2FE2S_FER_1; 1.
PS51085; 2FE2S_FER_2; 1.
PS51387; FAD_PCMH; 1.
PS00559; MOLYBDOPTERIN_EUK; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q06278.

Genome annotation databases

Ensembl

ENSG00000138356; Homo sapiens. [Contig view]

Phylogenomic databases

HOVERGEN

Q06278; -.

Other

DrugBank

DB00484; Brimonidine.
DB00477; Chlorpromazine.
DB00426; Famciclovir.
DB00170; Menadione.
DB00563; Methotrexate.
DB00157; NADH.
DB00377; Palonosetron.
DB00299; Penciclovir.
DB00481; Raloxifene.
DB00962; Zaleplon.
DB00909; Zonisamide.

Q06278; -.

AOX1; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

2Fe-2S; Cytoplasm; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding; Molybdenum; NAD; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 1338`	`1338`	`Aldehyde oxidase.`	`PRO_0000166104`
`DOMAIN`	`5 92`	`88`	`2Fe-2S ferredoxin-type.`
`DOMAIN`	`236 421`	`186`	`FAD-binding PCMH-type.`
`METAL`	`44 44`		`Iron-sulfur (2Fe-2S) (By similarity).`
`METAL`	`49 49`		`Iron-sulfur (2Fe-2S) (By similarity).`
`METAL`	`52 52`		`Iron-sulfur (2Fe-2S) (By similarity).`
`CONFLICT`	`251 251`		`D -> E (in Ref. 2; AAB83966).`
`CONFLICT`	`501 501`		`V -> L (in Ref. 2; AAB83966).`
`CONFLICT`	`627 627`		`I -> N (in Ref. 2; AAB83966).`

Sequence information

Length: 1338 AA [This is the length of the unprocessed precursor]

Molecular weight: 147931 Da [This is the MW of the unprocessed precursor]

CRC64: 14B5F9A2CE90BCF0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDRASELLFY VNGRKVIEKN VDPETMLLPY LRKKLRLTGT PYGCGGGGCG ACTVMISRYN 

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

       130        140        150        160        170        180 
MVMSIYPLLR NHPEPTLDQL TDALGGNLCR CHGYRPIIDA CKTFCKTSGC CQSKENGVCC 

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

       250        260        270        280        290        300 
MMWFSPVTLK DLLEFKFKYP QAPVIMGNTS VGPEVKFKGV FHPGYNSPDR IEEPECCKPC 

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

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

       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 RGFGFPQAVL ITESCITEVA AKCGLSPEKV RIINMYKEID 

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

      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

Q06278 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools