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Protein

Aldehyde oxidase

Gene

AOX1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 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 + H2O2.2 Publications
Retinal + O2 + H2O = retinoate + H2O2.By similarity

Cofactori

Protein has several cofactor binding sites:

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
  1. Vmax=16 nmol/min/mg enzyme with 6-deoxypenciclovir as substrate3 Publications
  2. Vmax=61 nmol/min/mg enzyme with famciclovir as substrate3 Publications
  3. 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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000138356-MONOMER.
BRENDAi1.2.3.1. 2681.
ReactomeiR-HSA-964975. Vitamins B6 activation to pyridoxal phosphate.
SABIO-RKQ06278.

Names & Taxonomyi

Protein namesi
Recommended name:
Aldehyde oxidase (EC:1.2.3.12 Publications)
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
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:553. AOX1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: GO_Central
  • extracellular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24842.

Chemistry

ChEMBLiCHEMBL3257.
DrugBankiDB00437. Allopurinol.
DB00513. Aminocaproic Acid.
DB00484. Brimonidine.
DB00426. Famciclovir.
DB09054. Idelalisib.
DB09078. Lenvatinib.
DB00170. Menadione.
DB01033. Mercaptopurine.
DB00563. Methotrexate.
DB00339. Pyrazinamide.
DB00481. Raloxifene.
DB00962. Zaleplon.
DB00909. Zonisamide.

Polymorphism and mutation databases

BioMutaiAOX1.
DMDMi215273968.

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1068 – 10681PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ06278.
PaxDbiQ06278.
PRIDEiQ06278.

PTM databases

iPTMnetiQ06278.
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

BgeeiQ06278.
CleanExiHS_AOX1.
ExpressionAtlasiQ06278. baseline and differential.
GenevisibleiQ06278. HS.

Organism-specific databases

HPAiHPA040199.
HPA040215.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi106813. 5 interactions.
DIPiDIP-61698N.
IntActiQ06278. 4 interactions.
STRINGi9606.ENSP00000363832.

Chemistry

BindingDBiQ06278.

Structurei

Secondary structure

1
1338
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 116Combined sources
Beta strandi14 – 207Combined sources
Helixi27 – 337Combined sources
Beta strandi45 – 495Combined sources
Beta strandi53 – 608Combined sources
Turni61 – 644Combined sources
Beta strandi65 – 728Combined sources
Helixi73 – 753Combined sources
Helixi78 – 814Combined sources
Beta strandi85 – 873Combined sources
Helixi89 – 924Combined sources
Beta strandi95 – 973Combined sources
Helixi101 – 1088Combined sources
Helixi118 – 13114Combined sources
Helixi137 – 1437Combined sources
Helixi144 – 1463Combined sources
Beta strandi150 – 1523Combined sources
Helixi155 – 1628Combined sources
Helixi204 – 2063Combined sources
Helixi212 – 2143Combined sources
Helixi220 – 2267Combined sources
Beta strandi234 – 2374Combined sources
Beta strandi242 – 2454Combined sources
Helixi249 – 25810Combined sources
Helixi271 – 2777Combined sources
Beta strandi283 – 2864Combined sources
Helixi292 – 2954Combined sources
Beta strandi297 – 2993Combined sources
Beta strandi301 – 3077Combined sources
Helixi312 – 32514Combined sources
Turni328 – 3303Combined sources
Helixi332 – 34312Combined sources
Helixi347 – 3526Combined sources
Helixi355 – 3617Combined sources
Helixi369 – 3746Combined sources
Beta strandi378 – 3825Combined sources
Beta strandi387 – 3915Combined sources
Helixi394 – 3974Combined sources
Turni401 – 4033Combined sources
Beta strandi410 – 4178Combined sources
Beta strandi423 – 4308Combined sources
Beta strandi432 – 4376Combined sources
Beta strandi440 – 4489Combined sources
Beta strandi451 – 4533Combined sources
Beta strandi458 – 46912Combined sources
Helixi474 – 4807Combined sources
Helixi487 – 49812Combined sources
Helixi512 – 53726Combined sources
Turni539 – 5413Combined sources
Turni547 – 5493Combined sources
Helixi550 – 5523Combined sources
Beta strandi562 – 5665Combined sources
Beta strandi572 – 5743Combined sources
Helixi589 – 5935Combined sources
Helixi600 – 6023Combined sources
Beta strandi610 – 6167Combined sources
Beta strandi620 – 6289Combined sources
Helixi630 – 6334Combined sources
Beta strandi638 – 6425Combined sources
Helixi644 – 6463Combined sources
Helixi648 – 6503Combined sources
Beta strandi666 – 6683Combined sources
Beta strandi674 – 6829Combined sources
Helixi683 – 6908Combined sources
Beta strandi694 – 6996Combined sources
Helixi709 – 7113Combined sources
Beta strandi721 – 7266Combined sources
Helixi728 – 7314Combined sources
Helixi732 – 7343Combined sources
Beta strandi736 – 74510Combined sources
Beta strandi756 – 7627Combined sources
Beta strandi769 – 7735Combined sources
Helixi778 – 78912Combined sources
Helixi793 – 7953Combined sources
Beta strandi796 – 8016Combined sources
Helixi812 – 82817Combined sources
Beta strandi832 – 8354Combined sources
Helixi838 – 8447Combined sources
Beta strandi851 – 8599Combined sources
Beta strandi865 – 87814Combined sources
Helixi884 – 89310Combined sources
Turni894 – 8974Combined sources
Beta strandi901 – 91111Combined sources
Turni921 – 9244Combined sources
Helixi925 – 94319Combined sources
Helixi947 – 9548Combined sources
Beta strandi958 – 9614Combined sources
Beta strandi967 – 9693Combined sources
Helixi971 – 98414Combined sources
Helixi986 – 99914Combined sources
Beta strandi1001 – 101616Combined sources
Helixi1022 – 10243Combined sources
Beta strandi1026 – 10327Combined sources
Beta strandi1038 – 10436Combined sources
Beta strandi1047 – 10493Combined sources
Helixi1051 – 106212Combined sources
Helixi1067 – 10693Combined sources
Turni1077 – 10793Combined sources
Helixi1091 – 111525Combined sources
Helixi1122 – 113110Combined sources
Beta strandi1137 – 11426Combined sources
Beta strandi1148 – 11503Combined sources
Turni1151 – 11544Combined sources
Beta strandi1155 – 11573Combined sources
Beta strandi1160 – 117415Combined sources
Turni1175 – 11773Combined sources
Beta strandi1180 – 119011Combined sources
Helixi1197 – 121519Combined sources
Helixi1232 – 12343Combined sources
Helixi1241 – 12433Combined sources
Beta strandi1246 – 12527Combined sources
Helixi1262 – 12643Combined sources
Helixi1271 – 12766Combined sources
Helixi1277 – 129317Combined sources
Helixi1308 – 13147Combined sources
Helixi1318 – 13225Combined sources
Helixi1328 – 13303Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4UHWX-ray2.60A1-1338[»]
4UHXX-ray2.70A1-1338[»]
5EPGX-ray3.39A1-1338[»]
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

eggNOGiKOG0430. Eukaryota.
COG4630. LUCA.
COG4631. LUCA.
GeneTreeiENSGT00390000003772.
HOGENOMiHOG000191197.
HOVERGENiHBG004182.
InParanoidiQ06278.
KOiK00157.
OMAiMDPVHYP.
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

        10         20         30         40         50
MDRASELLFY VNGRKVIEKN VDPETMLLPY LRKKLRLTGT KYGCGGGGCG
60 70 80 90 100
ACTVMISRYN PITKRIRHHP ANACLIPICS LYGAAVTTVE GIGSTHTRIH
110 120 130 140 150
PVQERIAKCH GTQCGFCTPG MVMSIYTLLR NHPEPTLDQL TDALGGNLCR
160 170 180 190 200
CTGYRPIIDA CKTFCKTSGC CQSKENGVCC LDQGINGLPE FEEGSKTSPK
210 220 230 240 250
LFAEEEFLPL DPTQELIFPP ELMIMAEKQS QRTRVFGSER MMWFSPVTLK
260 270 280 290 300
ELLEFKFKYP QAPVIMGNTS VGPEVKFKGV FHPVIISPDR IEELSVVNHA
310 320 330 340 350
YNGLTLGAGL SLAQVKDILA DVVQKLPEEK TQMYHALLKH LGTLAGSQIR
360 370 380 390 400
NMASLGGHII SRHPDSDLNP ILAVGNCTLN LLSKEGKRQI PLNEQFLSKC
410 420 430 440 450
PNADLKPQEI LVSVNIPYSR KWEFVSAFRQ AQRQENALAI VNSGMRVFFG
460 470 480 490 500
EGDGIIRELC ISYGGVGPAT ICAKNSCQKL IGRHWNEQML DIACRLILNE
510 520 530 540 550
VSLLGSAPGG KVEFKRTLII SFLFKFYLEV SQILKKMDPV HYPSLADKYE
560 570 580 590 600
SALEDLHSKH HCSTLKYQNI GPKQHPEDPI GHPIMHLSGV KHATGEAIYC
610 620 630 640 650
DDMPLVDQEL FLTFVTSSRA HAKIVSIDLS EALSMPGVVD IMTAEHLSDV
660 670 680 690 700
NSFCFFTEAE KFLATDKVFC VGQLVCAVLA DSEVQAKRAA KRVKIVYQDL
710 720 730 740 750
EPLILTIEES IQHNSSFKPE RKLEYGNVDE AFKVVDQILE GEIHMGGQEH
760 770 780 790 800
FYMETQSMLV VPKGEDQEMD VYVSTQFPKY IQDIVASTLK LPANKVMCHV
810 820 830 840 850
RRVGGAFGGK VLKTGIIAAV TAFAANKHGR AVRCVLERGE DMLITGGRHP
860 870 880 890 900
YLGKYKAGFM NDGRILALDM EHYSNAGASL DESLFVIEMG LLKMDNAYKF
910 920 930 940 950
PNLRCRGWAC RTNLPSNTAF RGFGFPQAAL ITESCITEVA AKCGLSPEKV
960 970 980 990 1000
RIINMYKEID QTPYKQEINA KNLIQCWREC MAMSSYSLRK VAVEKFNAEN
1010 1020 1030 1040 1050
YWKKKGLAMV PLKFPVGLGS RAAGQAAALV HIYLDGSVLV THGGIEMGQG
1060 1070 1080 1090 1100
VHTKMIQVVS RELRMPMSNV HLRGTSTETV PNANISGGSV VADLNGLAVK
1110 1120 1130 1140 1150
DACQTLLKRL EPIISKNPKG TWKDWAQTAF DESINLSAVG YFRGYESDMN
1160 1170 1180 1190 1200
WEKGEGQPFE YFVYGAACSE VEIDCLTGDH KNIRTDIVMD VGCSINPAID
1210 1220 1230 1240 1250
IGQIEGAFIQ GMGLYTIEEL NYSPQGILHT RGPDQYKIPA ICDMPTELHI
1260 1270 1280 1290 1300
ALLPPSQNSN TLYSSKGLGE SGVFLGCSVF FAIHDAVSAA RQERGLHGPL
1310 1320 1330
TLNSPLTPEK IRMACEDKFT KMIPRDEPGS YVPWNVPI
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. Curated
The sequence AAB83966.1 differs from that shown. Reason: Frameshift at positions 284, 286, 294 and 302. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti41 – 411K → P in AAA96650 (PubMed:8248161).Curated
Sequence conflicti41 – 411K → P in AAB83966 (Ref. 2) Curated
Sequence conflicti127 – 1271T → P in AAA96650 (PubMed:8248161).Curated
Sequence conflicti127 – 1271T → P in AAB83966 (Ref. 2) Curated
Sequence conflicti152 – 1521T → H in AAA96650 (PubMed:8248161).Curated
Sequence conflicti152 – 1521T → H in AAB83966 (Ref. 2) Curated
Sequence conflicti227 – 2271E → D in AAA96650 (PubMed:8248161).Curated
Sequence conflicti227 – 2271E → D in AAB83966 (Ref. 2) Curated
Sequence conflicti251 – 2511E → D in AAA96650 (PubMed:8248161).Curated
Sequence conflicti418 – 4181Y → I in AAA96650 (PubMed:8248161).Curated
Sequence conflicti418 – 4181Y → I in AAB83966 (Ref. 2) Curated
Sequence conflicti501 – 5011V → L in AAB83966 (Ref. 2) Curated
Sequence conflicti627 – 6271I → N in AAB83966 (Ref. 2) Curated
Sequence conflicti929 – 9291A → V in AAA96650 (PubMed:8248161).Curated
Sequence conflicti929 – 9291A → V in AAB83966 (Ref. 2) Curated
Sequence conflicti1019 – 10191G → A in AAA96650 (PubMed:8248161).Curated
Sequence conflicti1019 – 10191G → A in AAB83966 (Ref. 2) Curated

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:
EMBLi
GenBanki
DDBJi
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.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4UHWX-ray2.60A1-1338[»]
4UHXX-ray2.70A1-1338[»]
5EPGX-ray3.39A1-1338[»]
ProteinModelPortaliQ06278.
SMRiQ06278. Positions 4-166.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106813. 5 interactions.
DIPiDIP-61698N.
IntActiQ06278. 4 interactions.
STRINGi9606.ENSP00000363832.

Chemistry

BindingDBiQ06278.
ChEMBLiCHEMBL3257.
DrugBankiDB00437. Allopurinol.
DB00513. Aminocaproic Acid.
DB00484. Brimonidine.
DB00426. Famciclovir.
DB09054. Idelalisib.
DB09078. Lenvatinib.
DB00170. Menadione.
DB01033. Mercaptopurine.
DB00563. Methotrexate.
DB00339. Pyrazinamide.
DB00481. Raloxifene.
DB00962. Zaleplon.
DB00909. Zonisamide.

PTM databases

iPTMnetiQ06278.
PhosphoSiteiQ06278.

Polymorphism and mutation databases

BioMutaiAOX1.
DMDMi215273968.

Proteomic databases

MaxQBiQ06278.
PaxDbiQ06278.
PRIDEiQ06278.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000374700; ENSP00000363832; ENSG00000138356.
GeneIDi316.
KEGGihsa:316.
UCSCiuc002uvx.4. human.

Organism-specific databases

CTDi316.
GeneCardsiAOX1.
H-InvDBHIX0029780.
HGNCiHGNC:553. AOX1.
HPAiHPA040199.
HPA040215.
MIMi602841. gene.
neXtProtiNX_Q06278.
PharmGKBiPA24842.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0430. Eukaryota.
COG4630. LUCA.
COG4631. LUCA.
GeneTreeiENSGT00390000003772.
HOGENOMiHOG000191197.
HOVERGENiHBG004182.
InParanoidiQ06278.
KOiK00157.
OMAiMDPVHYP.
OrthoDBiEOG7QRQSZ.
PhylomeDBiQ06278.
TreeFamiTF353036.

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000138356-MONOMER.
BRENDAi1.2.3.1. 2681.
ReactomeiR-HSA-964975. Vitamins B6 activation to pyridoxal phosphate.
SABIO-RKQ06278.

Miscellaneous databases

ChiTaRSiAOX1. human.
GeneWikiiAldehyde_oxidase_1.
GenomeRNAii316.
NextBioi1283.
PROiQ06278.
SOURCEiSearch...

Gene expression databases

BgeeiQ06278.
CleanExiHS_AOX1.
ExpressionAtlasiQ06278. baseline and differential.
GenevisibleiQ06278. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1068, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. "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: April 13, 2016
This is version 162 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.