AOXB_MOUSE
ID AOXB_MOUSE Reviewed; 1345 AA.
AC Q5SGK3; B9EKC6;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Aldehyde oxidase 2;
DE EC=1.2.3.1;
DE AltName: Full=Aldehyde oxidase homolog 3;
DE AltName: Full=Azaheterocycle hydroxylase 2;
DE EC=1.17.3.-;
GN Name=Aox2; Synonyms=Aoh3, Aox3l1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION
RP AS OXIDASE, SUBSTRATE SPECIFICITY, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=CD-1; TISSUE=Olfactory epithelium;
RX PubMed=15383531; DOI=10.1074/jbc.m408734200;
RA Kurosaki M., Terao M., Barzago M.M., Bastone A., Bernardinello D.,
RA Salmona M., Garattini E.;
RT "The aldehyde oxidase gene cluster in mice and rats. Aldehyde oxidase
RT homologue 3, a novel member of the molybdo-flavoenzyme family with
RT selective expression in the olfactory mucosa.";
RL J. Biol. Chem. 279:50482-50498(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP TISSUE SPECIFICITY, AND IDENTIFICATION OF PARALOGS.
RX PubMed=23263164; DOI=10.1007/s00018-012-1229-5;
RA Kurosaki M., Bolis M., Fratelli M., Barzago M.M., Pattini L., Perretta G.,
RA Terao M., Garattini E.;
RT "Structure and evolution of vertebrate aldehyde oxidases: from gene
RT duplication to gene suppression.";
RL Cell. Mol. Life Sci. 70:1807-1830(2013).
CC -!- FUNCTION: Oxidase with broad substrate specificity, oxidizing aromatic
CC azaheterocycles, such as phthalazine, as well as aldehydes, such as
CC benzaldehyde and retinal. Cannot use hypoxanthine as substrate.
CC {ECO:0000269|PubMed:15383531}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + O2 = a carboxylate + H(+) + H2O2;
CC Xref=Rhea:RHEA:16829, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17478,
CC ChEBI:CHEBI:29067; EC=1.2.3.1;
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000250|UniProtKB:O54754};
CC Note=Binds 2 [2Fe-2S] clusters per subunit.
CC {ECO:0000250|UniProtKB:O54754};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:O54754};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:O54754};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC Evidence={ECO:0000250|UniProtKB:O54754};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000250|UniProtKB:O54754};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O54754}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15383531}.
CC -!- TISSUE SPECIFICITY: Expressed in olfactory mucosa epithelium (at
CC protein level). Detected in skin. {ECO:0000269|PubMed:15383531,
CC ECO:0000269|PubMed:23263164}.
CC -!- MISCELLANEOUS: AOX genes evolved from a xanthine oxidoreductase
CC ancestral precursor via a series of gene duplication and
CC suppression/deletion events. Different animal species contain a
CC different complement of AOX genes encoding an equivalent number of AOX
CC isoenzymes. In mammals, the two extremes are represented by certain
CC rodents such as mice and rats, which are endowed with 4 AOX genes, and
CC by humans, whose genome is characterized by a single active gene
CC (PubMed:23263164). {ECO:0000305|PubMed:23263164}.
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AY187018; AAO38750.2; -; mRNA.
DR EMBL; AY665589; AAV68256.1; -; mRNA.
DR EMBL; AC121091; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC163498; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC150826; AAI50827.1; -; mRNA.
DR CCDS; CCDS35576.1; -.
DR RefSeq; NP_001008419.1; NM_001008419.2.
DR AlphaFoldDB; Q5SGK3; -.
DR SMR; Q5SGK3; -.
DR BioGRID; 229391; 1.
DR STRING; 10090.ENSMUSP00000110006; -.
DR iPTMnet; Q5SGK3; -.
DR PhosphoSitePlus; Q5SGK3; -.
DR jPOST; Q5SGK3; -.
DR MaxQB; Q5SGK3; -.
DR PaxDb; Q5SGK3; -.
DR PeptideAtlas; Q5SGK3; -.
DR PRIDE; Q5SGK3; -.
DR ProteomicsDB; 296261; -.
DR Ensembl; ENSMUST00000114366; ENSMUSP00000110006; ENSMUSG00000079554.
DR GeneID; 213043; -.
DR KEGG; mmu:213043; -.
DR UCSC; uc007bbp.1; mouse.
DR CTD; 213043; -.
DR MGI; MGI:3529596; Aox2.
DR VEuPathDB; HostDB:ENSMUSG00000079554; -.
DR eggNOG; KOG0430; Eukaryota.
DR GeneTree; ENSGT00950000183114; -.
DR HOGENOM; CLU_001681_1_2_1; -.
DR InParanoid; Q5SGK3; -.
DR OMA; EGTWENW; -.
DR OrthoDB; 48717at2759; -.
DR PhylomeDB; Q5SGK3; -.
DR TreeFam; TF353036; -.
DR BRENDA; 1.2.3.1; 3474.
DR BioGRID-ORCS; 213043; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Aox2; mouse.
DR PRO; PR:Q5SGK3; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q5SGK3; protein.
DR Bgee; ENSMUSG00000079554; Expressed in spermatocyte and 19 other tissues.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0004031; F:aldehyde oxidase activity; ISS:UniProtKB.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISS:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR GO; GO:0043546; F:molybdopterin cofactor binding; ISS:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0006805; P:xenobiotic metabolic process; ISS:UniProtKB.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR002888; 2Fe-2S-bd.
DR InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR InterPro; IPR016208; Ald_Oxase/xanthine_DH.
DR InterPro; IPR014313; Aldehyde_oxidase.
DR InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd.
DR InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR005107; CO_DH_flav_C.
DR InterPro; IPR036683; CO_DH_flav_C_dom_sf.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR PANTHER; PTHR11908; PTHR11908; 1.
DR Pfam; PF01315; Ald_Xan_dh_C; 1.
DR Pfam; PF02738; Ald_Xan_dh_C2; 1.
DR Pfam; PF03450; CO_deh_flav_C; 1.
DR Pfam; PF00941; FAD_binding_5; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF01799; Fer2_2; 1.
DR PIRSF; PIRSF000127; Xanthine_DH; 1.
DR SMART; SM01008; Ald_Xan_dh_C; 1.
DR SMART; SM01092; CO_deh_flav_C; 1.
DR SUPFAM; SSF47741; SSF47741; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR SUPFAM; SSF54665; SSF54665; 1.
DR SUPFAM; SSF55447; SSF55447; 1.
DR SUPFAM; SSF56003; SSF56003; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR TIGRFAMs; TIGR02969; mam_aldehyde_ox; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Cytoplasm; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding;
KW Molybdenum; Oxidoreductase; Reference proteome.
FT CHAIN 1..1345
FT /note="Aldehyde oxidase 2"
FT /id="PRO_0000425245"
FT DOMAIN 9..96
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 238..423
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT ACT_SITE 1276
FT /note="Proton acceptor; for azaheterocycle hydroxylase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:O54754"
FT BINDING 48
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 53
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 56
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 78
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 117
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 118
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 121
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 153
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 155
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 155
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 266..273
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 347
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 356
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 360
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 369
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 413
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 812..813
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 1094..1097
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 1209
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 1274
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT CONFLICT 202
FT /note="K -> E (in Ref. 3; AAI50827)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1345 AA; 147913 MW; 6D3FA441A3F6F92C CRC64;
MPCPAQISDD LEFFVNGRKV TEKNVDPEVT LLAFLRKNLC LTGTKDACGT GGCGACTVMV
SQHDPVCKKT RHFSVMACLV PLCSLHGAAV TTVEGVGSIK TRLHPVQERI AKSHGTQCGF
CTPGMVMSIY TLLRNHPQPS EEQLMEALGG NLCRCTGYRP ILESGRTFCM EPDGCPQKGT
GQCCLDQKES DSSGSKSDIC TKLFVKDEFQ PLDPTQELIF PPELLRMAEN PEKQTLTFYG
ERITWIAPGT LQELLVLKAK YPEAPLISGN TALGPAMKSQ GHFYPVLLSP ARIPDLRMVT
KTSGGLTIGA CCSLAQVKDI LAESISELPQ EKTQTYRALL KHLRSLAGQQ IRNMASLGGH
VISRHCYSDL NPILSVGNTT LNLLSEEGPR QIPLSGHFLA GLASADLKPE EILGSVYIPH
SQKREFVSAF RQAQCHQNAL PDVNAGMRVL FREGTDVIEE LSIAYGGVGP TTVSAQRSCQ
QLLGRRWNAL MLDEACRLLL DEVSLPGSAL GGKVEFRRTL IVSLFFKFYL EVLQELKADQ
KLPPESTDSQ RYPEIADRFL SSLGDFQVTL PRGVQTYQRV DSHQPLQDPV GRPIMHLSGL
KHATGEAVFC DDIPRVDKEL FMALVTSTRA HARIISIDSS EVLDLPGVVD VITAEDIPGN
NGEEDDKLLA VDKVLCVGQV ICAVVAETDV QAKRATEKIK ITYEDLKPVI FTIEDAIKHN
SFLCPEKKLE QGNIEEAFEN VDQVAEGTVH VGGQEHFYME TQRVLVIPKT EDKELDMYVS
TQDPAHVQKT VSSTLNIPIS RITCHVKRVG GGFGGKVGRP AVFGAIAAVG AVKTGHPIRL
VLDREDDMLI TGGRHPLFAK YKVGFMNSGR IKALDIECYI NGGCTLDDSE LVTEFLVLKL
ENAYKIRNLR LRGRACMTNL PSNTAFRGFG FPQGALVTES CITAVAAKCG LPPEKIREKN
MYKTVDKTIY KQAFNPDPLI RCWNECLDKS SFHIRRTRVD EFNKKSYWKK RGIAIVPMKF
SVGFAATSYH QAAALVHIYT DGSVLVAHGG NELGQGIHTK MLQVASRELK IPLSYLHICE
TSTTTVPNTI ATAASVGADV NGRAVQNACQ ILLKRLEPVI KKNPEGTWRD WIEAAFEKRI
SLSATGYFRG YKAFMDWEKG EGDPFPYYVY GAACSEVEID CLTGAHKKIR TDIVMDACCS
LNPAIDIGQI EGAFIQGMGL YTTEELLYSP EGVLYSRSPD KYKIPTVTDV PEQFNVSLLP
SSQTPLTLYS SKGLGESGMF LGSSVFFAIV DAVAAARRQR DIAEDFTVKS PATPEWVRMA
CADRFTDMIP RDDPKTFKPW SIPIA
