AOXB_MACFA
ID AOXB_MACFA Reviewed; 1349 AA.
AC C4NYZ3; G7PL56;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 2.
DT 03-AUG-2022, entry version 63.
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 Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND IDENTIFICATION OF
RP 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22002653; DOI=10.1038/nbt.1992;
RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT "Genome sequencing and comparison of two nonhuman primate animal models,
RT the cynomolgus and Chinese rhesus macaques.";
RL Nat. Biotechnol. 29:1019-1023(2011).
CC -!- FUNCTION: Oxidase with broad substrate specificity, oxidizing aromatic
CC azaheterocycles, such as phthalazine, as well as aldehydes, such as
CC benzaldehyde and retinal. {ECO:0000250|UniProtKB:Q5SGK3}.
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:0000250|UniProtKB:Q5SGK3}.
CC -!- TISSUE SPECIFICITY: Only detected at very few levels in nasal mucosa.
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; FJ746636; ACQ73552.1; -; mRNA.
DR EMBL; CM001287; EHH55065.1; -; Genomic_DNA.
DR AlphaFoldDB; C4NYZ3; -.
DR SMR; C4NYZ3; -.
DR STRING; 9541.XP_005573934.1; -.
DR PRIDE; C4NYZ3; -.
DR eggNOG; KOG0430; Eukaryota.
DR Proteomes; UP000009130; Chromosome 12.
DR Proteomes; UP000233100; Unplaced.
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: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 2: Evidence at transcript level;
KW 2Fe-2S; Cytoplasm; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding;
KW Molybdenum; Oxidoreductase; Reference proteome.
FT CHAIN 1..1349
FT /note="Aldehyde oxidase 2"
FT /id="PRO_0000425244"
FT DOMAIN 8..96
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 240..425
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT ACT_SITE 1280
FT /note="Proton acceptor; for azaheterocycle hydroxylase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:O54754"
FT BINDING 47
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 52
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 55
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 268..275
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 349
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 358
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 362
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 371
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 415
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 816..817
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 1098..1101
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 1213
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 1278
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT CONFLICT 2
FT /note="R -> C (in Ref. 1; ACQ73552)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="Missing (in Ref. 1; ACQ73552)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="R -> P (in Ref. 1; ACQ73552)"
FT /evidence="ECO:0000305"
FT CONFLICT 548..550
FT /note="Missing (in Ref. 1; ACQ73552)"
FT /evidence="ECO:0000305"
FT CONFLICT 675
FT /note="V -> A (in Ref. 1; ACQ73552)"
FT /evidence="ECO:0000305"
FT CONFLICT 708
FT /note="E -> K (in Ref. 1; ACQ73552)"
FT /evidence="ECO:0000305"
FT CONFLICT 1124
FT /note="I -> V (in Ref. 1; ACQ73552)"
FT /evidence="ECO:0000305"
FT CONFLICT 1265
FT /note="S -> P (in Ref. 1; ACQ73552)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1349 AA; 148845 MW; C97CB8EE664A08B8 CRC64;
MRCASRSDEL VFFVNGRKVM ERNVDPEGTL LTFLRKNLRL TGTKYACGRG GCGACTVMVS
KHDPVSRKIQ RHFSVTACLM PICSLYGAAV TTVEGVGSIK TRLHPVQERI AKSHGTQCGF
CTPGMVMSMY TLLRNHPQPS EEQLTEALGG NLCRCTGYRP ILESGRTFCM ESNSCQQKGT
GKCCLDWGEN DSSRLGKKNE ICTKLFAKEE FQSLDPTQEL IFPPELLRMA ENPEKRTLTF
YGERVTWISP GTLKDLLELK VKHPEAPLVV GNTSLGPAMK SQRQFHPVLL SPARISELSM
VTKTSDGLTI GAGCSLAQTQ DILAERIAEL PEEKTQTYRA LLKHLRSLAG QQIRNMASLG
GHVISRHCCS DLNPVLAVSN ATLNLISAEG TRQIPLNEHF LAGLASADLK PEEILESVHI
PHSQKWEFVS AFRQAQCQQN ALPHVNAGMR VLLKEGTDSI EDLSIAYGGV GAATISAHRS
CQQLLGRRWN ELMLDEACRL LLDEVSLPGS APGGRVEFKR TLVVSFLFKF YLEVLQELKK
LVKLFSVAVG ADSRHRSEVS DQFLSALEDF PVTIPQGVQT YQNVDPHQPL QDPVGRPIMH
LSALKHATGE AMFCDDIPVV DKELFMALVT SSRAHAKIIS IDVSKALELP EVVDVITAED
IPGTNGAEGD KLLAVEEVTC VGQIICAVVA ETDVQAKRAT EKIEITYEDL EPVIFTIKDA
IKHNSFLCPE KKLEQGNVEE AFEKVDQTIE GEVHVGGQEH FYMETQRVLV IPKTEDKELD
IYVSTQDPAH VQKTVSSTLN IPINRITCHV KRVGGGFGGK VGKPAVFGAI AAVGAIKTGH
PIRLVLDRED DMLITGGRHP LFGKYKVGFT NNGRIKALDI ECYINGGCTL DDSELVTEFL
ILKLENAYKI RNLRFRGRAC MTNLPSNTAF RGFGFPQGAL VTESCITAVA AKCGLPPEKI
REKNMYKTVD KTIYKQAFNP ETLIRCWNEC LDKSSFHSRR MQVEEFNKKN YWKKKGIAII
PMKFSVGFAA TSYHQAAALV HIYTDGSVLV THGGNELGQG IHTKMLQVAS RELKIPMSCI
HISETSTATV PNTIATAASV GADVNGRAVQ NACQILLKRL EPIIKKHPEG TWENWIEAAF
EQRISLSATG YFRGYKAFMD WEKGVGDPFP YYVYGAACSE VEIDCLTGAH KKIRTDIIMD
ACCSLNPAID IGQIEGSFIQ GMGLYTTEEL KYSPEGILYS RSPDEYKIPT ITDVPEEFNV
SLLPSSQTPL TIYSSKGLGE SGMFLGSSVF FAIADAVATV RRERDIAEDF MVQSPATPER
VRMACADRFT KMIPRDDPET FKPWSIPIA
