UniProtKB - Q5FB27 (AOXA_MACFA)
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Protein
Aldehyde oxidase 1
Gene
AOX1
Organism
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Status
Functioni
Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide, N-methylphthalazinium and phthalazine, 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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 113 | MolybdopterinBy similarity | 1 | |
Binding sitei | 151 | MolybdopterinBy similarity | 1 | |
Binding sitei | 345 | FAD; via amide nitrogenBy similarity | 1 | |
Binding sitei | 354 | FADBy similarity | 1 | |
Binding sitei | 358 | FADBy similarity | 1 | |
Binding sitei | 367 | FADBy similarity | 1 | |
Binding sitei | 411 | FAD; via amide nitrogen and carbonyl oxygenBy similarity | 1 | |
Binding sitei | 1047 | Molybdopterin; via carbonyl oxygenBy similarity | 1 | |
Binding sitei | 1203 | MolybdopterinBy similarity | 1 | |
Binding sitei | 1268 | Molybdopterin; via carbonyl oxygenBy similarity | 1 | |
Active sitei | 1270 | Proton acceptor; for azaheterocycle hydroxylase activityBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 264 – 271 | FADBy similarity | 8 |
GO - Molecular functioni
- 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
- aldehyde oxidase activity Source: UniProtKB-EC
- electron transfer activity Source: InterPro
- flavin adenine dinucleotide binding Source: InterPro
- geranial:oxygen oxidoreductase activity Source: UniProtKB-EC
- heptaldehyde:oxygen oxidoreductase activity Source: UniProtKB-EC
- iron ion binding Source: InterPro
- molybdopterin cofactor binding Source: InterPro
- NAD binding Source: InterPro
- oxidoreductase activity, acting on CH-OH group of donors Source: InterPro
Keywordsi
Molecular function | Oxidoreductase |
Ligand | 2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Molybdenum |
Enzyme and pathway databases
BRENDAi | 1.2.3.1. 1793. |
SABIO-RKi | Q5FB27. |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:AOX1 |
Organismi | Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) |
Taxonomic identifieri | 9541 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Cercopithecidae › Cercopithecinae › Macaca |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000166105 | 1 – 1338 | Aldehyde oxidase 1Add BLAST | 1338 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 1068 | PhosphoserineBy similarity | 1 |
Keywords - PTMi
PhosphoproteinExpressioni
Tissue specificityi
Detected at high levels in liver, also detected in lung, kidney, lacrimal gland and olfactory mucosa.1 Publication
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 5 – 92 | 2Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST | 88 | |
Domaini | 236 – 421 | FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST | 186 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 806 – 807 | Molybdopterin bindingBy similarity | 2 | |
Regioni | 1088 – 1091 | Molybdopterin bindingBy similarity | 4 |
Sequence similaritiesi
Belongs to the xanthine dehydrogenase family.Curated
Phylogenomic databases
HOVERGENi | HBG004182. |
KOi | K00157. |
Family and domain databases
InterProi | View protein in InterPro IPR002888. 2Fe-2S-bd. IPR036884. 2Fe-2S-bd_dom_sf. IPR036010. 2Fe-2S_ferredoxin-like_sf. IPR001041. 2Fe-2S_ferredoxin-type. IPR006058. 2Fe2S_fd_BS. IPR000674. Ald_Oxase/Xan_DH_a/b. IPR036856. Ald_Oxase/Xan_DH_a/b_sf. IPR016208. Ald_Oxase/xanthine_DH. IPR014313. Aldehyde_oxidase. IPR008274. AldOxase/xan_DH_Mopterin-bd. IPR037165. AldOxase/xan_DH_Mopterin-bd_sf. IPR005107. CO_DH_flav_C. IPR036683. CO_DH_flav_C_dom_sf. IPR016166. FAD-bd_2. IPR036318. FAD-bd_2-like_sf. IPR002346. Mopterin_DH_FAD-bd. IPR022407. OxRdtase_Mopterin_BS. |
Pfami | View 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. |
PIRSFi | PIRSF000127. Xanthine_DH. 1 hit. |
SMARTi | View protein in SMART SM01008. Ald_Xan_dh_C. 1 hit. SM01092. CO_deh_flav_C. 1 hit. |
SUPFAMi | SSF47741. SSF47741. 1 hit. SSF54292. SSF54292. 1 hit. SSF54665. SSF54665. 1 hit. SSF55447. SSF55447. 1 hit. SSF56003. SSF56003. 1 hit. SSF56176. SSF56176. 1 hit. |
TIGRFAMsi | TIGR02969. mam_aldehyde_ox. 1 hit. |
PROSITEi | View 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. |
i Sequence
Sequence statusi: Complete.
Q5FB27-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 184 | R → G in BAD89382 (Ref. 1) Curated | 1 | |
Sequence conflicti | 275 | M → V in BAD89382 (Ref. 1) Curated | 1 | |
Sequence conflicti | 284 – 286 | VII → GYN in BAD89382 (Ref. 1) Curated | 3 | |
Sequence conflicti | 294 – 302 | LSVVNHTHN → PECCKPYTY in BAD89382 (Ref. 1) Curated | 9 | |
Sequence conflicti | 328 | G → E in BAD89382 (Ref. 1) Curated | 1 | |
Sequence conflicti | 511 | R → K in BAD89382 (Ref. 1) Curated | 1 | |
Sequence conflicti | 541 | R → H in BAD89382 (Ref. 1) Curated | 1 | |
Sequence conflicti | 549 | H → Y in BAD89382 (Ref. 1) Curated | 1 | |
Sequence conflicti | 605 | L → P in BAD89382 (Ref. 1) Curated | 1 | |
Sequence conflicti | 1105 | T → I in BAD89382 (Ref. 1) Curated | 1 | |
Sequence conflicti | 1139 | V → I in BAD89382 (Ref. 1) Curated | 1 | |
Sequence conflicti | 1301 | S → T in BAD89382 (Ref. 1) Curated | 1 | |
Sequence conflicti | 1338 | I → V in BAD89382 (Ref. 1) Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AB201545 mRNA. Translation: BAD89382.1. FJ751935 mRNA. Translation: ACQ73553.1. |
RefSeqi | NP_001271673.1. NM_001284744.1. |
UniGenei | Mfa.7431. |
Genome annotation databases
GeneIDi | 102131116. |
KEGGi | mcf:102131116. |
Similar proteinsi
Entry informationi
Entry namei | AOXA_MACFA | |
Accessioni | Q5FB27Primary (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: | March 28, 2018 | |
This is version 85 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |