ID   G3MWP9_BOVIN            Unreviewed;      1327 AA.
AC   G3MWP9;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 2.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=aldehyde oxidase {ECO:0000256|ARBA:ARBA00013041};
DE            EC=1.2.3.1 {ECO:0000256|ARBA:ARBA00013041};
GN   Name=AOX4 {ECO:0000313|Ensembl:ENSBTAP00000053952.2,
GN   ECO:0000313|VGNC:VGNC:108907};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000053952.2, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000053952.2, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000053952.2,
RC   ECO:0000313|Proteomes:UP000009136};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000053952.2}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000053952.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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         Evidence={ECO:0000256|ARBA:ARBA00000039};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR000127-2};
CC   -!- COFACTOR:
CC       Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000127-3};
CC       Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC       {ECO:0000256|PIRSR:PIRSR000127-3};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|ARBA:ARBA00034078};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000127-3};
CC       Note=Binds 2 [2Fe-2S] clusters. {ECO:0000256|PIRSR:PIRSR000127-3};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00006849}.
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DR   Ensembl; ENSBTAT00000065376.2; ENSBTAP00000053952.2; ENSBTAG00000038878.3.
DR   VEuPathDB; HostDB:ENSBTAG00000038878; -.
DR   VGNC; VGNC:108907; AOX4.
DR   eggNOG; KOG0430; Eukaryota.
DR   GeneTree; ENSGT00950000183114; -.
DR   TreeFam; TF353036; -.
DR   Proteomes; UP000009136; Chromosome 2.
DR   Bgee; ENSBTAG00000038878; Expressed in surface of tongue and 41 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0004031; F:aldehyde oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   CDD; cd00207; fer2; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 1.10.150.120; [2Fe-2S]-binding domain; 1.
DR   Gene3D; 3.90.1170.50; Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead; 1.
DR   Gene3D; 3.30.365.10; Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain; 5.
DR   Gene3D; 3.30.390.50; CO dehydrogenase flavoprotein, C-terminal domain; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 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-like.
DR   InterPro; IPR014313; Aldehyde_oxidase.
DR   InterPro; IPR008274; AldOxase/xan_DH_MoCoBD1.
DR   InterPro; IPR046867; AldOxase/xan_DH_MoCoBD2.
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   NCBIfam; TIGR02969; mam_aldehyde_ox; 1.
DR   PANTHER; PTHR11908:SF88; ALDEHYDE OXIDASE 4; 1.
DR   PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1.
DR   Pfam; PF01315; Ald_Xan_dh_C; 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   Pfam; PF02738; MoCoBD_1; 1.
DR   Pfam; PF20256; MoCoBD_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; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF55447; CO dehydrogenase flavoprotein C-terminal domain-like; 1.
DR   SUPFAM; SSF47741; CO dehydrogenase ISP C-domain like; 1.
DR   SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714, ECO:0000256|PIRSR:PIRSR000127-3};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000127-2};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000127-3};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR000127-
KW   3};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000127-3};
KW   Molybdenum {ECO:0000256|ARBA:ARBA00022505, ECO:0000256|PIRSR:PIRSR000127-
KW   3}; Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009136}.
FT   DOMAIN          229..414
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   ACT_SITE        1258
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-1"
FT   BINDING         39
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         44
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         47
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         69
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         109
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         112
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         144
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         146
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         257..264
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT   BINDING         360
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT   BINDING         422
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT   BINDING         765
FT                   /ligand="Mo-molybdopterin"
FT                   /ligand_id="ChEBI:CHEBI:71302"
FT                   /ligand_part="Mo"
FT                   /ligand_part_id="ChEBI:CHEBI:28685"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         796
FT                   /ligand="Mo-molybdopterin"
FT                   /ligand_id="ChEBI:CHEBI:71302"
FT                   /ligand_part="Mo"
FT                   /ligand_part_id="ChEBI:CHEBI:28685"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         910
FT                   /ligand="Mo-molybdopterin"
FT                   /ligand_id="ChEBI:CHEBI:71302"
FT                   /ligand_part="Mo"
FT                   /ligand_part_id="ChEBI:CHEBI:28685"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         912
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT   BINDING         1077
FT                   /ligand="Mo-molybdopterin"
FT                   /ligand_id="ChEBI:CHEBI:71302"
FT                   /ligand_part="Mo"
FT                   /ligand_part_id="ChEBI:CHEBI:28685"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
SQ   SEQUENCE   1327 AA;  146921 MW;  BA2BD099334CBE03 CRC64;
     MTSFLPDLSL PDLSNNCGIF SPENDSLVII HLTGTKYSCG SGGCGACTVM VSRYDPKTKK
     IHHYPVTACL VPICSLHGAA VTTVEGVGSI KTRIHPVQER LAKCHGTQCG FCSPGMVMSI
     YTLLRNHPEP TPEQITEALG GNLCRCTGYR PIVESGKTFC AESTVCQMKG SGKCCMDQEE
     KSFTSRQEKM CTKLYNEDEF QPFDPTQEPI FPPELIRMAE DPNKRRLTFR GKRTTWITPV
     NLNDLLELKT SFPEAPIIMG NTAVGPSIKF RDEFHPVFIS PLGLQELYFV DSTDDGVTIG
     AGYSLAQLND ALRFIVSEQP KEKTKTYHAL LKHLRTLAGA QIRNMATLGG HVVSRPNYSD
     LNPILAAGNA TINLISKEGK RQIPLDGRFL EKSPEANLKS EETVLSVYIP HSTQWHFVSG
     LRIAQRQENA FAIVNAGMSV KFEDGTDTIK ELQMFYGSVG PTVVSASKTC QQLIGRKWND
     QMLSDACRLV LDEIYIPPDA EGGMVEYRRT LIISLLFKFY LKVRRGLNKM DPHKFPDIPE
     KFVSALEDFP IETPQGIQMF QCVDPHQPPQ DPVGHPVMHQ SAIKHTTGEA VFVDDMPPIS
     QELFLAVVTS TRAHAKIILI DTSAALALPG VVDVITAEDV PGDNSYQGEI FYAQNEVICV
     GQIVCTVAAD TYAHAKEAAK KVRIVYEDLE PRIITIEQAL EHNSFLSAEK KIEQGDVEQA
     FKYVDQIIEG KVHVEGQEHF YMETQTILAI PQEEDKEMVL HLGTQFQTHV QEYVAAALSI
     PRNRIACHTK RAGGAFGGKV SKPALLGAVS AVAAKKTGRP IRFILERGDD MLITAGRHPL
     LGKYKIGFMN NGVIKAADIE YYINGGCSPD ESELVMEFMV LRSENAYYIP NFRCRGRPCK
     TNLPSNTAFR GFGFPQGIVV GEAYITAVAS QCDLTPEQVK EINMYKRTSR TAHKQTFNPE
     PLRRCWKECL EKSSFSARKL AAEEFNKKNY WKKRGLAAVP MKFTVGMPTA FYNQAAALVH
     IYLDGSVLVS HSGCELGQGL HTKMIQVASR ELNIPESYIH LSETNTTTVS NATFTAGSMG
     TDINGKAVQN ACQILKARLE PVIRKNPRGT WEAWISEAYK ESISLSTTGY FKGYQTNMDW
     KKGEGNAFPY FVYGASCSEV EVDCLTGAHK LLRTDIFMDA AFSINPAVDI GQIEGAFVQG
     MGFYTIEELK YSPEGVLYSR GPDDYKIPTV TEIPEEFNVT LVHSQNPIAI YSSKGLGEAG
     MFLGSSVLFA IYDAVAAARR ERGLTKTFTL SSPATPELIR MTCVDQFTDM IPRDDPSTFT
     PWSIHVS
//