UniProtKB - H9TB17 (AOXA_CAVPO)
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Protein
Aldehyde oxidase 1
Gene
AOX1
Organism
Cavia porcellus (Guinea pig)
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.2 Publications
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 + H2O2.1 Publication
Retinal + O2 + H2O = retinoate + H2O2.1 Publication
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
Enzyme regulationi
Inhibited by menadione and isovanillin. Not inhibited by allopurinol, a xanthine dehydrogenase potent inhibitor.1 Publication
Kineticsi
- KM=0.41 mM for 6-deoxypenciclovir (at 37 degrees Celsius and pH 7)1 Publication
- KM=0.17 mM for famciclovir (at 37 degrees Celsius and pH 7)1 Publication
- Vmax=209 nmol/min/mg enzyme with 6-deoxypenciclovir as substrate1 Publication
- Vmax=439 nmol/min/mg enzyme with famciclovir as substrate1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 43 | Iron-sulfur 1 (2Fe-2S)By similarity | 1 | |
Metal bindingi | 48 | Iron-sulfur 1 (2Fe-2S)By similarity | 1 | |
Metal bindingi | 51 | Iron-sulfur 1 (2Fe-2S)By similarity | 1 | |
Metal bindingi | 73 | Iron-sulfur 1 (2Fe-2S)By similarity | 1 | |
Binding sitei | 112 | MolybdopterinBy similarity | 1 | |
Metal bindingi | 113 | Iron-sulfur 2 (2Fe-2S)By similarity | 1 | |
Metal bindingi | 116 | Iron-sulfur 2 (2Fe-2S)By similarity | 1 | |
Metal bindingi | 148 | Iron-sulfur 2 (2Fe-2S)By similarity | 1 | |
Metal bindingi | 150 | Iron-sulfur 2 (2Fe-2S)By similarity | 1 | |
Binding sitei | 150 | MolybdopterinBy similarity | 1 | |
Binding sitei | 343 | FAD; via amide nitrogenBy similarity | 1 | |
Binding sitei | 352 | FADBy similarity | 1 | |
Binding sitei | 356 | FADBy similarity | 1 | |
Binding sitei | 365 | FADBy similarity | 1 | |
Binding sitei | 409 | FAD; via amide nitrogen and carbonyl oxygenBy similarity | 1 | |
Binding sitei | 1041 | Molybdopterin; via carbonyl oxygenBy similarity | 1 | |
Binding sitei | 1197 | MolybdopterinBy similarity | 1 | |
Binding sitei | 1262 | Molybdopterin; via carbonyl oxygenBy similarity | 1 | |
Active sitei | 1264 | Proton acceptor; for azaheterocycle hydroxylase activityBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 262 – 269 | FADBy similarity | 8 |
GO - Molecular functioni
- 2 iron, 2 sulfur cluster binding Source: UniProtKB
- aldehyde oxidase activity Source: UniProtKB
- electron transfer activity Source: InterPro
- flavin adenine dinucleotide binding Source: UniProtKB
- geranial:oxygen oxidoreductase activity Source: UniProtKB-EC
- heptaldehyde:oxygen oxidoreductase activity Source: UniProtKB-EC
- iron ion binding Source: UniProtKB
- molybdopterin cofactor binding Source: UniProtKB
- NAD binding Source: InterPro
- oxidoreductase activity, acting on CH-OH group of donors Source: InterPro
- protein homodimerization activity Source: UniProtKB
- retinal oxidase activity Source: UniProtKB
GO - Biological processi
- drug metabolic process Source: UniProtKB
- oxidation-reduction process Source: UniProtKB
Keywordsi
Molecular function | Oxidoreductase |
Ligand | 2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Molybdenum |
Enzyme and pathway databases
SABIO-RKi | H9TB17. |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:AOX1By similarity Synonyms:AO |
Organismi | Cavia porcellus (Guinea pig) |
Taxonomic identifieri | 10141 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Hystricomorpha › Caviidae › Cavia |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000425242 | 1 – 1332 | Aldehyde oxidase 1Add BLAST | 1332 |
Expressioni
Tissue specificityi
Expressed in liver.1 Publication
Interactioni
Subunit structurei
Homodimer.By similarity
GO - Molecular functioni
- protein homodimerization activity Source: UniProtKB
Protein-protein interaction databases
STRINGi | 10141.ENSCPOP00000021102. |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 4 – 91 | 2Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST | 88 | |
Domaini | 234 – 419 | FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST | 186 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 800 – 801 | Molybdopterin bindingBy similarity | 2 | |
Regioni | 1082 – 1085 | Molybdopterin bindingBy similarity | 4 |
Sequence similaritiesi
Belongs to the xanthine dehydrogenase family.Curated
Phylogenomic databases
eggNOGi | KOG0430. Eukaryota. COG4631. LUCA. |
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.
H9TB17-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MEPSTLYFYV NGRRVTEKNV DPETMLLPYL GRNLRLTGTK YGCGGGGCGA
60 70 80 90 100
CTVMVSRYDR GTGQIRHYPA CACLTPLCSL HGAAVTTVEG VGSTRTRLHP
110 120 130 140 150
VQERIAKSHG TQCGFCTPGM VMSLYALLRS HPQPSEEQLL EALAGNLCRC
160 170 180 190 200
TGYRPILDAG KTFCKTSGCC QSKENGVCCL DQGVNGVQEA EGEQTSQELC
210 220 230 240 250
SEEEFVPLDP TQELIFPPEL MILAQKQPQK SRVFTGDRVT WISPVTLKDL
260 270 280 290 300
LEAKAKNPRA PVVMGNTSVG PEMKFKGVFH PVIISPDGIE ELSVIKQGNE
310 320 330 340 350
GLTLGAGLSL AQVQDVLADV VQQLPEEKTQ TLCALLKQLR TLAGSQIRNM
360 370 380 390 400
ASLGGHIMSR HLDSDLNPVL AAASCTLHVP SQEGDRQIPL DEHFLSRSPS
410 420 430 440 450
ADLRPQEVLL SVTIPYSRKW EFVSAFRQAQ RKRSARAIVN VGMRVFFGAG
460 470 480 490 500
DGVISELCIL YGGVGPAIVC ATDACRKLVG RHWTEEMLDE ACRLVLGEVA
510 520 530 540 550
IPGAAPGGRV EFRRTLLVSF LFRFYLQVSQ SLSRMDPGRY PSLVGKYESA
560 570 580 590 600
LEDLCLGHHQ RTFELQSADA KQLPQDPIGR PIMHLSGIKH TTGEAIYCDD
610 620 630 640 650
MPLVDRELSL AFVTSSRAHA AILSMDLSEA LSLPGVVDIV TAEHLGDANS
660 670 680 690 700
FAKETLLATD KVLCVGHLVC AVIADSEVQA KRAAEKVKIV YQDLEPLILT
710 720 730 740 750
IEEAIQHDSF FETERKLESG DVAEAFRTAE QVLEGSIHMG GQEHFYMETQ
760 770 780 790 800
SMLAVPKGED QEIDLYVSTQ FPTYIQEIVA STLKLPVNKV MCHVRRVGGA
810 820 830 840 850
FGGKVGKTAI LAAITAFAAL KHCRAVRCIL ERGEDMLITG GRHPYLGKYK
860 870 880 890 900
VGFRNNGQVV ALDMEHYSNA GSTLDESLMV VEMGLLKMEN AYKFPNLRCR
910 920 930 940 950
GHACKTNLPS NTALRGFGFP QSGLITEACI VEVAARCGLS PEEVREVNMY
960 970 980 990 1000
RGTEQTHYGQ EIHTQRLAQC WSECKAKATF SLRRAAVDRF NAGSPWKKRG
1010 1020 1030 1040 1050
LAMVPLKFPV GLGSVAMGQA AALVHVYLDG SVLLTHGGIE MGQGVHTKMI
1060 1070 1080 1090 1100
QVVSRELKMP MANVHLRGTS TETVPNANVS GGSVVADLNG LAVKDACQTL
1110 1120 1130 1140 1150
LKRLEPIISK NPKGTWKEWA QAAFDQSISL SAIGYFRGYD ADMDWEKGKG
1160 1170 1180 1190 1200
HPFEYFVYGA ACSEVEIDCL TGNHKNIRTD IVMDVGRSIN PALDLGQVEG
1210 1220 1230 1240 1250
AFIQGMGLYT SEELKYGPQG ALYTRGPDQY KIPAVCDVPA ELHVFFLPPS
1260 1270 1280 1290 1300
KNSNTLYSSK GLGESGVFLG CSVLFAIWDA VSAARRERGL PGTLALSCPL
1310 1320 1330
TPEKIRMACE DRFTKMIPRD TPGSYVPWDV VV
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 519 | S → N in AFG18181 (PubMed:23263164).Curated | 1 | |
Sequence conflicti | 677 | E → G in AFG18181 (PubMed:23263164).Curated | 1 | |
Sequence conflicti | 695 | E → G in AFG18181 (PubMed:23263164).Curated | 1 | |
Sequence conflicti | 1137 | R → T in AFG18181 (PubMed:23263164).Curated | 1 | |
Sequence conflicti | 1201 | A → P in AFG18181 (PubMed:23263164).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | JQ280309 mRNA. Translation: AFG18181.1. AAKN02051283 Genomic DNA. No translation available. |
RefSeqi | NP_001295371.1. NM_001308442.1. |
Genome annotation databases
GeneIDi | 100720210. |
Similar proteinsi
Entry informationi
Entry namei | AOXA_CAVPO | |
Accessioni | H9TB17Primary (citable) accession number: H9TB17 Secondary accession number(s): H0WDM9 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 19, 2014 |
Last sequence update: | February 19, 2014 | |
Last modified: | March 28, 2018 | |
This is version 34 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |