Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Aldehyde oxidase 1

Gene

AOX1

Organism
Bos taurus (Bovine)
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. 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.1 Publication

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • [2Fe-2S] clusterBy similarityNote: Binds 2 [2Fe-2S] clusters per subunit.By similarity
  • FADBy similarityNote: Binds 1 FAD per subunit.By similarity
  • Mo-molybdopterinBy similarityNote: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi44Iron-sulfur 1 (2Fe-2S)By similarity1
Metal bindingi49Iron-sulfur 1 (2Fe-2S)By similarity1
Metal bindingi52Iron-sulfur 1 (2Fe-2S)By similarity1
Metal bindingi74Iron-sulfur 1 (2Fe-2S)By similarity1
Binding sitei113MolybdopterinBy similarity1
Metal bindingi114Iron-sulfur 2 (2Fe-2S)By similarity1
Metal bindingi117Iron-sulfur 2 (2Fe-2S)By similarity1
Metal bindingi149Iron-sulfur 2 (2Fe-2S)By similarity1
Metal bindingi151Iron-sulfur 2 (2Fe-2S)By similarity1
Binding sitei354FADBy similarity1
Binding sitei358FADBy similarity1
Binding sitei367FADBy similarity1
Binding sitei411FAD; via amide nitrogenBy similarity1
Binding sitei807Molybdopterin; via amide nitrogenBy similarity1
Binding sitei1048Molybdopterin; via amide nitrogenBy similarity1
Binding sitei1204MolybdopterinBy similarity1
Active sitei1271Proton acceptor; for azaheterocycle hydroxylase activityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi264 – 271FADBy similarity8

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

BRENDAi1.2.3.1. 908.

Names & Taxonomyi

Protein namesi
Recommended name:
Aldehyde oxidase 1 (EC:1.2.3.1By similarity)
Alternative name(s):
Azaheterocycle hydroxylase 1 (EC:1.17.3.-)
Gene namesi
Name:AOX1
Synonyms:AO
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001661031 – 1339Aldehyde oxidase 1Add BLAST1339

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1069PhosphoserineBy similarity1

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP48034.
PeptideAtlasiP48034.
PRIDEiP48034.

Expressioni

Tissue specificityi

Expressed at high levels in liver, lung and spleen. Also expressed in kindey, eye, testis, duodenum, esophagus and thymus (at protein level).1 Publication

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000012827.

Structurei

3D structure databases

ProteinModelPortaliP48034.
SMRiP48034.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 922Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST88
Domaini236 – 421FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST186

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.
HOGENOMiHOG000191197.
HOVERGENiHBG004182.
InParanoidiP48034.
KOiK00157.

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.

P48034-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGGSELLFY VNGRKVTEKN VDPETMLLPY LRKKLRLTGT KYGCGGGGCG
60 70 80 90 100
ACTVMISRYN PITKKIRHYP ANACLTPICS LYGAAVTTVE GIGSTKTRIH
110 120 130 140 150
PVQERIAKCH GTQCGFCTPG MVMSLYTLLR NHPEPTLTQL NDALGGNLCR
160 170 180 190 200
CTGYRPIINA CKTFCKTSGC CQSKENGVCC LDQGMNGLPE FEEGNETSLK
210 220 230 240 250
LFSEEEFLPL DPTQELIFPP ELMTMAEKKT QKTRIFGSDR MTWISPVTLK
260 270 280 290 300
ELLEAKVKYP QAPVVMGNTS VGPDMKFKGI FHPVIISPDR IEELSVVNYT
310 320 330 340 350
DNGLTLGAAV SLAEVKDILA NVTRKLPEEK TQMYHALLKH LETLAGPQIR
360 370 380 390 400
NMASLGGHIV SRHPDSDLNP LLAVGNCTLN LLSKEGRRQI PLNEQFLRKC
410 420 430 440 450
PSADLKPEEI LISVNIPYSR KWEFVSAFRQ AQRQQNALAI VNSGMRVCFG
460 470 480 490 500
KGDGIIRELS IAYGGVGPTT ILANNSCQKL IGRPWNEEML DAACRLILDE
510 520 530 540 550
VSLPGSAPGG RVEFKRTLIV SFLFKFYLEV SQILKGMDLV HYPSLASKYE
560 570 580 590 600
SALEDLHSRH YWSTLKYQNA DLKQLSQDPI GHPIMHLSGI KHATGEAIYC
610 620 630 640 650
DDMPVVDREL FLTFVTSSRA HAKIVSIDVS AALSLPGVVD ILTGEHLPGI
660 670 680 690 700
NTTFGFLTDA DQLLSTDEVS CVGQLVCAVI ADSEVQARRA AQQVKIVYQD
710 720 730 740 750
LEPVILTIEE AIQNKSFFEP ERKLEYGNVD EAFKMVDQIL EGEIHMGGQE
760 770 780 790 800
HFYMETQSML VVPKGEDREI DVYVSAQFPK YIQDITASVL KVSANKVMCH
810 820 830 840 850
VKRVGGAFGG KVTKTGVLAA ITAFAANKHG RPVRCILERG EDILITGGRH
860 870 880 890 900
PYLGKYKAGF MNDGRILALD MEHYNNAGAF LDESLFVIEM GLLKLENAYK
910 920 930 940 950
FPNLRCRGWA CRTNLPSNTA LRGFGFPQAG LITEACITEV AAKCGLPPEK
960 970 980 990 1000
VRMINMYKEI DQTPYKQEIN TKNLTQCWKE CMATSSYTLR KAAVEKFNSE
1010 1020 1030 1040 1050
NYWKKKGLAM VPLKYPIGLG SVAAGQAAAL VHIYLDGSVL VTHGGIEMGQ
1060 1070 1080 1090 1100
GVHTKMIQVV SRELRMPLSS IHLRGTSTET IPNTNPSGGS VVADLNGLAV
1110 1120 1130 1140 1150
KDACQTLLKR LKPIISKNPK GTWKDWAQAA FNESISLSAT GYFRGYESNI
1160 1170 1180 1190 1200
NWETGEGHPF EYFVYGAACS EVEIDCLTGA HKNIRTDIVM DVGYSINPAL
1210 1220 1230 1240 1250
DVGQIEGAFI QGMGLYTIEE LNYSPQGVLY TRGPNQYKIP AICDIPMELH
1260 1270 1280 1290 1300
ISFLPPSENS NTLYSSKGLG ESGIFLGCSV FFAIHDAIRA ARQERGLPGP
1310 1320 1330
LRLNSPLTPE KIRMACEDKF TKMIPRDEPG SYVPWSVPI
Length:1,339
Mass (Da):147,611
Last modified:October 1, 1996 - v2
Checksum:i3CA7FF9D2B06F655
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti5S → A in AAI05266 (Ref. 2) Curated1
Sequence conflicti185M → I in AAI05266 (Ref. 2) Curated1
Sequence conflicti804V → I in AAI05266 (Ref. 2) Curated1
Sequence conflicti1060V → A in AAI05266 (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X87251 mRNA. Translation: CAA60701.1.
BC105265 mRNA. Translation: AAI05266.1.
PIRiS46980.
RefSeqiNP_788841.1. NM_176668.3.
UniGeneiBt.45005.

Genome annotation databases

GeneIDi338074.
KEGGibta:338074.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X87251 mRNA. Translation: CAA60701.1.
BC105265 mRNA. Translation: AAI05266.1.
PIRiS46980.
RefSeqiNP_788841.1. NM_176668.3.
UniGeneiBt.45005.

3D structure databases

ProteinModelPortaliP48034.
SMRiP48034.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000012827.

Proteomic databases

PaxDbiP48034.
PeptideAtlasiP48034.
PRIDEiP48034.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi338074.
KEGGibta:338074.

Organism-specific databases

CTDi316.

Phylogenomic databases

eggNOGiKOG0430. Eukaryota.
COG4630. LUCA.
COG4631. LUCA.
HOGENOMiHOG000191197.
HOVERGENiHBG004182.
InParanoidiP48034.
KOiK00157.

Enzyme and pathway databases

BRENDAi1.2.3.1. 908.

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...

Entry informationi

Entry nameiAOXA_BOVIN
AccessioniPrimary (citable) accession number: P48034
Secondary accession number(s): Q3MHE7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.