AOX1
entrez
316
canonical
uniprot
Q06278
canonical
ensembl
ENSG00000138356
resolver
ensp
ENSP00000363832
resolver
ensp
ENSP00000524964
resolver
enst
ENST00000374700
resolver
genesymbol
AOX1
resolver
genesymbol_syn
AO
resolver
hgnc
HGNC:553
resolver
uniprot
O14765
resolver
uniprot
Q53RR8
resolver
uniprot
Q53TV3
resolver
uniprot
Q9BYF0
resolver
uniprot
Q9UPG6
resolver
uniprot_entry
AOXA_HUMAN
resolver
uniprot_sec
O14765
resolver
uniprot_sec
Q53RR8
resolver
uniprot_sec
Q53TV3
resolver
uniprot_sec
Q9BYF0
resolver
uniprot_sec
Q9UPG6
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by raloxifene; for small substrates, the inhibitor raloxifene presents an uncompetitive inhibition profile while bulky substrates are more prone to compete with the inhibitor raloxifene (PubMed:14709625, PubMed:26842593, PubMed:34415167). Also inhibited by thioridazine, a non-competitive type of inhibition (PubMed:26322824, PubMed:34415167). Also inhibited by estradiol, ethinyl estradiol, hydralazine, menadione and isovanillin. Not inhibited by allopurinol, a xanthine dehydrogenase potent inhibitor (PubMed:22031625, PubMed:22522748, PubMed:22996261, PubMed:9224775). {ECO:0000269|PubMed:14709625, ECO:0000269|PubMed:22031625, ECO:0000269|PubMed:22522748, ECO:0000269|PubMed:22996261, ECO:0000269|PubMed:26322824, ECO:0000269|PubMed:26842593, ECO:0000269|PubMed:34415167, ECO:0000269|PubMed:9224775}.
uniprot
proteins
amino_acid_sequence
MDRASELLFYVNGRKVIEKNVDPETMLLPYLRKKLRLTGTKYGCGGGGCGACTVMISRYNPITKRIRHHPANACLIPICSLYGAAVTTVEGIGSTHTRIHPVQERIAKCHGTQCGFCTPGMVMSIYTLLRNHPEPTLDQLTDALGGNLCRCTGYRPIIDACKTFCKTSGCCQSKENGVCCLDQGINGLPEFEEGSKTSPKLFAEEEFLPLDPTQELIFPPELMIMAEKQSQRTRVFGSERMMWFSPVTLKELLEFKFKYPQAPVIMGNTSVGPEVKFKGVFHPVIISPDRIEELSVVNHAYNGLTLGAGLSLAQVKDILADVVQKLPEEKTQMYHALLKHLGTLAGSQIRNMASLGGHIISRHPDSDLNPILAVGNCTLNLLSKEGKRQIPLNEQFLSKCPNADLKPQEILVSVNIPYSRKWEFVSAFRQAQRQENALAIVNSGMRVFFGEGDGIIRELCISYGGVGPATICAKNSCQKLIGRHWNEQMLDIACRLILNEVSLLGSAPGGKVEFKRTLIISFLFKFYLEVSQILKKMDPVHYPSLADKYESALEDLHSKHHCSTLKYQNIGPKQHPEDPIGHPIMHLSGVKHATGEAIYCDDMPLVDQELFLTFVTSSRAHAKIVSIDLSEALSMPGVVDIMTAEHLSDVNSFCFFTEAEKFLATDKVFCVGQLVCAVLADSEVQAKRAAKRVKIVYQDLEPLILTIEESIQHNSSFKPERKLEYGNVDEAFKVVDQILEGEIHMGGQEHFYMETQSMLVVPKGEDQEMDVYVSTQFPKYIQDIVASTLKLPANKVMCHVRRVGGAFGGKVLKTGIIAAVTAFAANKHGRAVRCVLERGEDMLITGGRHPYLGKYKAGFMNDGRILALDMEHYSNAGASLDESLFVIEMGLLKMDNAYKFPNLRCRGWACRTNLPSNTAFRGFGFPQAALITESCITEVAAKCGLSPEKVRIINMYKEIDQTPYKQEINAKNLIQCWRECMAMSSYSLRKVAVEKFNAENYWKKKGLAMVPLKFPVGLGSRAAGQAAALVHIYLDGSVLVTHGGIEMGQGVHTKMIQVVSRELRMPMSNVHLRGTSTETVPNANISGGSVVADLNGLAVKDACQTLLKRLEPIISKNPKGTWKDWAQTAFDESINLSAVGYFRGYESDMNWEKGEGQPFEYFVYGAACSEVEIDCLTGDHKNIRTDIVMDVGCSINPAIDIGQIEGAFIQGMGLYTIEELNYSPQGILHTRGPDQYKIPAICDMPTELHIALLPPSQNSNTLYSSKGLGESGVFLGCSVFFAIHDAVSAARQERGLHGPLTLNSPLTPEKIRMACEDKFTKMIPRDEPGSYVPWNVPI
uniprot
proteins
ec_number
1.17.3.-
uniprot
proteins
ec_number
1.2.3.1
uniprot
proteins
ec_number
1.2.3.8
uniprot
proteins
ec_number
1.2.3.9
uniprot
proteins
function
FUNCTION: Primarily catalyzes oxidation reactions of a broad range of drug and xenobiotic substrates and participates in their metabolism through oxidative biotransformation (PubMed:14709625, PubMed:20444863, PubMed:22279051, PubMed:22996261, PubMed:23857892, PubMed:26322824, PubMed:26842593, PubMed:34415167, PubMed:7786031, PubMed:9224775). Oxidizes at least three structural types of substrates: aldehydes such as benzaldehyde, retinal, pyridoxal, and vanillin; aromatic azaheterocyclic compounds such as phthalazine, quinazoline and phenanthridine; and quaternary azaheterocyclic compounds such as 1-methylnicotinamide and nicotine imine (PubMed:14709625, PubMed:22279051, PubMed:22996261, PubMed:23857892, PubMed:26322824, PubMed:26842593, PubMed:34415167, PubMed:7786031, PubMed:9224775). Converts aldehydes to carboxylic acids, aromatic and quaternary azaheterocyclic compounds to lactams, typically by using molecular oxygen as the terminal electron acceptor and producing hydrogen peroxide as a by-product (PubMed:14709625, PubMed:22279051, PubMed:22996261, PubMed:23857892, PubMed:26322824, PubMed:26842593, PubMed:34415167, PubMed:7786031, PubMed:9224775). Under some conditions, especially with electron-deficient substrates or limited oxygen, can also catalyze reduction reactions using N-methylnicotinamide, 2-hydroxypyrimidine or benzaldehyde as electron donor substrate (Probable) (PubMed:15720138). These reductive activities include N-O bond reductions in nitro groups (e.g., imidacloprid, IMI), hydroxamic acids, and oxazoles (e.g., zonisamide), as well as N-S bond reductions of sulfoxides (e.g., sulindac) (By similarity). {ECO:0000250|UniProtKB:Q5FB27, ECO:0000269|PubMed:14709625, ECO:0000269|PubMed:15720138, ECO:0000269|PubMed:20444863, ECO:0000269|PubMed:22279051, ECO:0000269|PubMed:22996261, ECO:0000269|PubMed:23857892, ECO:0000269|PubMed:26322824, ECO:0000269|PubMed:26842593, ECO:0000269|PubMed:34415167, ECO:0000269|PubMed:7786031, ECO:0000269|PubMed:9224775, ECO:0000305|PubMed:14709625}.
uniprot
proteins
mass_dalton
147918
uniprot
proteins
mutagenesis
MUTAGEN 44; /note="C->W: Disrupts protein stability."; /evidence="ECO:0000269|PubMed:26842593"; MUTAGEN 1269; /note="G->R: No effect on dimerization. Loss of oxidase activity."; /evidence="ECO:0000269|PubMed:26842593
uniprot
proteins
protein_family
Xanthine dehydrogenase family
uniprot
proteins
pubmed
11302742
uniprot
proteins
pubmed
14709625
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15720138
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
17022944
uniprot
proteins
pubmed
18066686
uniprot
proteins
pubmed
18671973
uniprot
proteins
pubmed
20444863
uniprot
proteins
pubmed
22031625
uniprot
proteins
pubmed
22279051
uniprot
proteins
pubmed
22335465
uniprot
proteins
pubmed
22522748
uniprot
proteins
pubmed
22996261
uniprot
proteins
pubmed
23857892
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
26322824
uniprot
proteins
pubmed
26842593
uniprot
proteins
pubmed
27406959
uniprot
proteins
pubmed
34415167
uniprot
proteins
pubmed
7786031
uniprot
proteins
pubmed
8248161
uniprot
proteins
pubmed
9224775
uniprot
proteins
sequence_length
1338
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18671973, ECO:0000269|PubMed:20444863, ECO:0000269|PubMed:23857892}.
uniprot
proteins