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UniProtKB - Q5FB27 (AOXA_MACFA)

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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

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

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 sitei806Molybdopterin; via amide nitrogenBy similarity1
Binding sitei1047Molybdopterin; via amide nitrogenBy similarity1
Binding sitei1203MolybdopterinBy similarity1
Active sitei1270Proton acceptor; for azaheterocycle hydroxylase activityBy similarity1

Regions

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

GO - Molecular functioni

Complete GO annotation...

Keywordsi

Molecular functionOxidoreductase
Ligand2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Molybdenum

Enzyme and pathway databases

BRENDAi1.2.3.1. 1793.
SABIO-RKiQ5FB27.

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Cercopithecidae › Cercopithecinae › Macaca

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1641357.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001661051 – 1338Aldehyde oxidase 1Add BLAST1338

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1068PhosphoserineBy similarity1

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 databases

BindingDBiQ5FB27.

Structurei

3D structure databases

SMRiQ5FB27.
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

Phylogenomic databases

HOVERGENiHBG004182.
KOiK00157.

Family and domain databases

Gene3Di1.10.150.120. 1 hit.
3.10.20.30. 1 hit.
3.30.365.10. 4 hits.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.90.1170.50. 1 hit.
InterProiView protein in InterPro
IPR002888. 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.
PfamiView protein in Pfam
PF01315. 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.
PIRSFiPIRSF000127. Xanthine_DH. 1 hit.
SMARTiView protein in SMART
SM01008. Ald_Xan_dh_C. 1 hit.
SM01092. CO_deh_flav_C. 1 hit.
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.
PROSITEiView protein in PROSITE
PS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.

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)DescriptionActionsGraphical viewLength
Sequence conflicti184R → G in BAD89382 (Ref. 1) Curated1
Sequence conflicti275M → V in BAD89382 (Ref. 1) Curated1
Sequence conflicti284 – 286VII → GYN in BAD89382 (Ref. 1) Curated3
Sequence conflicti294 – 302LSVVNHTHN → PECCKPYTY in BAD89382 (Ref. 1) Curated9
Sequence conflicti328G → E in BAD89382 (Ref. 1) Curated1
Sequence conflicti511R → K in BAD89382 (Ref. 1) Curated1
Sequence conflicti541R → H in BAD89382 (Ref. 1) Curated1
Sequence conflicti549H → Y in BAD89382 (Ref. 1) Curated1
Sequence conflicti605L → P in BAD89382 (Ref. 1) Curated1
Sequence conflicti1105T → I in BAD89382 (Ref. 1) Curated1
Sequence conflicti1139V → I in BAD89382 (Ref. 1) Curated1
Sequence conflicti1301S → T in BAD89382 (Ref. 1) Curated1
Sequence conflicti1338I → V in BAD89382 (Ref. 1) Curated1

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.

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.

Entry informationi

Entry nameiAOXA_MACFA
AccessioniPrimary (citable) accession number: Q5FB27
Secondary accession number(s): D6BND8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: February 19, 2014
Last modified: May 10, 2017
This is version 78 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families