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Protein

Aldehyde oxidase 1

Gene

AOX1

Organism
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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 (By similarity).By similarity

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)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

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. 1793.
SABIO-RKQ5FB27.

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
OrganismiMacaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Taxonomic identifieri9541 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL1641357.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13381338Aldehyde oxidase 1PRO_0000166105Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1068 – 10681PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Expressioni

Tissue specificityi

Detected at high levels in liver, also detected in lung, kidney, lacrimal gland and olfactory mucosa.1 Publication

Interactioni

Subunit structurei

Homodimer.By similarity

Chemistry

BindingDBiQ5FB27.

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

HOVERGENiHBG004182.
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.

Q5FB27-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDRASELLFY VNGRKVIEKN VDPETMLLPY LRKKLRLTGT KYGCGGGGCG
60 70 80 90 100
ACTVMISRYN PITNRIRHHP ANACLIPICS LYGTAVTTVE GIGSTHTRIH
110 120 130 140 150
PVQERIAKCH GTQCGFCTPG MVMSIYTLLR NHPEPTLDQL TDALGGNLCR
160 170 180 190 200
CTGYRPIIDA CKTFCETSGC CQSKENGVCC LDQRINGLPE FEEGSKTSPK
210 220 230 240 250
LFAEEEFLPL DPTQELIFPP ELMIMAEKQP QRTRVFGSER MMWFSPVTLK
260 270 280 290 300
ELLEFKFKYP QAPVIMGNTS VGPQMKFKGV FHPVIISPDR IEELSVVNHT
310 320 330 340 350
HNGLTLGAGL SLAQVKDILA DVVQKLPGEK TQTYHALLKH LGTLAGSQIR
360 370 380 390 400
NMASLGGHII SRHPDSDLNP ILAVGNCTLN LLSKEGKRQI PLNEQFLSKC
410 420 430 440 450
PNADLKPQEI LVSVNIPYSR KLEFVSAFRQ AQRQENALAI VNSGMRVFFG
460 470 480 490 500
EGHGIIRELS ISYGGVGPAT ICAKNSCQKL IGRHWNEEML DTACRLVLEE
510 520 530 540 550
VSLSGSAPGG RVEFKRTLII SFLFKFYLEV SQILKKMDPI RYPSLADKHE
560 570 580 590 600
SALEDLHSKH HCSTLKYQHM GPKQHPEDPI GHPIMHLSGV KHATGEAIYC
610 620 630 640 650
DDMPLVDQEL FLTFVTSSRA HAKIVSIDLS EALSMPGVVD VITAEHLSDV
660 670 680 690 700
NSFCFFTEAE EFLATDKVFC VGQLVCAVLA DSEVQAKRAA KQVKIVYQDL
710 720 730 740 750
EPLILTIKEA IQHNSFFEPE RKLEYGNVDE AFKVVDQILE GEIHMGGQEH
760 770 780 790 800
FYMETQSMLV VPKGEDQEMD VYVSTQFPKY IQDIVASTLK LPANKVMCHV
810 820 830 840 850
KRVGGAFGGK AFKTGVIAAV TAFAANKHGR AVRCVLERGE DMLITGGRHP
860 870 880 890 900
YLGKYKAGFM NDGRILALDM EHYSNAGNSL DESLLVIEMG LLKMDNAYKF
910 920 930 940 950
PNLRCRGWAC RTNLPSNTAF RGFGFPQAGL ITESCIMEVA AKCGLSPEKV
960 970 980 990 1000
RMINMYKEID QTPYKQEINA KNLIQCWREC MAVSSYSLRK AAVEKFNAEN
1010 1020 1030 1040 1050
YWKKKGLAMV PLKYPVGLGS RAAGQAAALV HIYLDGSVLV THGGIEMGQG
1060 1070 1080 1090 1100
VHTKMIQVVS RELGMPISNV HLRGTSTETV PNANVSGGSV VADLNGLAVK
1110 1120 1130 1140 1150
DACQTLLKRL EPIISKNPKG TWKDWAQTAF DESISLSAVG YFRGYESDIN
1160 1170 1180 1190 1200
WEKGEGHPFE YFVYGAACSE VEIDCLTGDH KNIRTDIVMD VGCSINPAID
1210 1220 1230 1240 1250
IGQIEGAFIQ GMGLYTIEEL NYSPQGVLHT RGPDQYKIPA ICDTPTEFHI
1260 1270 1280 1290 1300
SLLPPSENSN TLYSSKGLGE SGVFLGCSVF FAIHDAVSAA RRERGLHGPL
1310 1320 1330
SLNSPLTPEK IRMACEDKFT KMIPRDEPGS CVPWNVPI
Length:1,338
Mass (Da):147,691
Last modified:February 19, 2014 - v2
Checksum:iC82ACFAB5FA7019C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti184 – 1841R → G in BAD89382 (Ref. 1) Curated
Sequence conflicti275 – 2751M → V in BAD89382 (Ref. 1) Curated
Sequence conflicti284 – 2863VII → GYN in BAD89382 (Ref. 1) Curated
Sequence conflicti294 – 3029LSVVNHTHN → PECCKPYTY in BAD89382 (Ref. 1) Curated
Sequence conflicti328 – 3281G → E in BAD89382 (Ref. 1) Curated
Sequence conflicti511 – 5111R → K in BAD89382 (Ref. 1) Curated
Sequence conflicti541 – 5411R → H in BAD89382 (Ref. 1) Curated
Sequence conflicti549 – 5491H → Y in BAD89382 (Ref. 1) Curated
Sequence conflicti605 – 6051L → P in BAD89382 (Ref. 1) Curated
Sequence conflicti1105 – 11051T → I in BAD89382 (Ref. 1) Curated
Sequence conflicti1139 – 11391V → I in BAD89382 (Ref. 1) Curated
Sequence conflicti1301 – 13011S → T in BAD89382 (Ref. 1) Curated
Sequence conflicti1338 – 13381I → V in BAD89382 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB201545 mRNA. Translation: BAD89382.1.
FJ751935 mRNA. Translation: ACQ73553.1.
RefSeqiNP_001271673.1. NM_001284744.1.
UniGeneiMfa.7431.

Genome annotation databases

GeneIDi102131116.
KEGGimcf:102131116.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB201545 mRNA. Translation: BAD89382.1.
FJ751935 mRNA. Translation: ACQ73553.1.
RefSeqiNP_001271673.1. NM_001284744.1.
UniGeneiMfa.7431.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiQ5FB27.
ChEMBLiCHEMBL1641357.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi102131116.
KEGGimcf:102131116.

Organism-specific databases

CTDi316.

Phylogenomic databases

HOVERGENiHBG004182.
KOiK00157.

Enzyme and pathway databases

BRENDAi1.2.3.1. 1793.
SABIO-RKQ5FB27.

Miscellaneous databases

PROiQ5FB27.

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

  1. "Molecular cloning and characterization of monkey aldehyde oxidase."
    Hoshino K.
    Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Structure and evolution of vertebrate aldehyde oxidases: from gene duplication to gene suppression."
    Kurosaki M., Bolis M., Fratelli M., Barzago M.M., Pattini L., Perretta G., Terao M., Garattini E.
    Cell. Mol. Life Sci. 70:1807-1830(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, IDENTIFICATION OF PARALOGS.

Entry informationi

Entry nameiAOXA_MACFA
AccessioniPrimary (citable) accession number: Q5FB27
Secondary accession number(s): D6BND8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: February 19, 2014
Last modified: June 8, 2016
This is version 75 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

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.