ID   XDH_FELCA               Reviewed;        1331 AA.
AC   Q9MYW6;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 115.
DE   RecName: Full=Xanthine dehydrogenase/oxidase;
DE   Includes:
DE     RecName: Full=Xanthine dehydrogenase;
DE              Short=XD;
DE              EC=1.17.1.4 {ECO:0000250|UniProtKB:P22985};
DE   Includes:
DE     RecName: Full=Xanthine oxidase;
DE              Short=XO;
DE              EC=1.17.3.2 {ECO:0000250|UniProtKB:P22985};
DE     AltName: Full=Xanthine oxidoreductase;
DE              Short=XOR;
GN   Name=XDH;
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=11307944; DOI=10.1292/jvms.63.353;
RA   Tsuchida S., Yamada R., Ikemoto S., Tagawa M.;
RT   "Molecular cloning of a cDNA coding for feline liver xanthine
RT   dehydrogenase.";
RL   J. Vet. Med. Sci. 63:353-355(2001).
CC   -!- FUNCTION: Key enzyme in purine degradation. Catalyzes the oxidation of
CC       hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric
CC       acid. Contributes to the generation of reactive oxygen species.
CC       {ECO:0000250|UniProtKB:P22985}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + NAD(+) + xanthine = H(+) + NADH + urate;
CC         Xref=Rhea:RHEA:16669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17712, ChEBI:CHEBI:17775, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.17.1.4;
CC         Evidence={ECO:0000250|UniProtKB:P22985};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + hypoxanthine + NAD(+) = H(+) + NADH + xanthine;
CC         Xref=Rhea:RHEA:24670, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17368, ChEBI:CHEBI:17712, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.17.1.4;
CC         Evidence={ECO:0000250|UniProtKB:P22985};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O2 + xanthine = H2O2 + urate; Xref=Rhea:RHEA:21132,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:17712, ChEBI:CHEBI:17775; EC=1.17.3.2;
CC         Evidence={ECO:0000250|UniProtKB:P22985};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302; Evidence={ECO:0000250};
CC       Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC       {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000250|UniProtKB:P22985};
CC       Note=Binds 2 [2Fe-2S] clusters per subunit.
CC       {ECO:0000250|UniProtKB:P22985};
CC   -!- ACTIVITY REGULATION: Can be converted from the dehydrogenase form (D)
CC       to the oxidase form (O) irreversibly by proteolysis or reversibly
CC       through the oxidation of sulfhydryl groups. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Interacts with BTN1A1 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Peroxisome
CC       {ECO:0000250}. Secreted {ECO:0000250}.
CC   -!- PTM: Subject to partial proteolysis; this alters the enzyme from the
CC       dehydrogenase form (D) to the oxidase form (O). {ECO:0000250}.
CC   -!- PTM: Contains sulfhydryl groups that are easily oxidized (in vitro);
CC       this alters the enzyme from the dehydrogenase form (D) to the oxidase
CC       form (O). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AF286379; AAF97949.1; -; mRNA.
DR   RefSeq; NP_001009217.1; NM_001009217.1.
DR   AlphaFoldDB; Q9MYW6; -.
DR   SMR; Q9MYW6; -.
DR   STRING; 9685.ENSFCAP00000033363; -.
DR   PaxDb; 9685-ENSFCAP00000004209; -.
DR   GeneID; 493692; -.
DR   KEGG; fca:493692; -.
DR   eggNOG; KOG0430; Eukaryota.
DR   InParanoid; Q9MYW6; -.
DR   OrthoDB; 5485853at2759; -.
DR   Proteomes; UP000011712; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; 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; IEA:InterPro.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; ISS:UniProtKB.
DR   GO; GO:0004854; F:xanthine dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0004855; F:xanthine oxidase activity; ISS:UniProtKB.
DR   GO; GO:0009115; P:xanthine catabolic process; ISS:UniProtKB.
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; 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   InterPro; IPR022407; OxRdtase_Mopterin_BS.
DR   InterPro; IPR014307; Xanthine_DH_ssu.
DR   NCBIfam; TIGR02963; xanthine_xdhA; 1.
DR   PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11908:SF80; XANTHINE DEHYDROGENASE_OXIDASE; 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; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
DR   PROSITE; PS00559; MOLYBDOPTERIN_EUK; 1.
PE   2: Evidence at transcript level;
KW   2Fe-2S; Cytoplasm; Disulfide bond; FAD; Flavoprotein; Iron; Iron-sulfur;
KW   Metal-binding; Molybdenum; NAD; Oxidoreductase; Peroxisome;
KW   Reference proteome; Secreted.
FT   CHAIN           1..1331
FT                   /note="Xanthine dehydrogenase/oxidase"
FT                   /id="PRO_0000246176"
FT   DOMAIN          4..91
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   DOMAIN          229..412
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   ACT_SITE        1260
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         43
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P22985"
FT   BINDING         48
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P22985"
FT   BINDING         51
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P22985"
FT   BINDING         73
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P22985"
FT   BINDING         113
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P22985"
FT   BINDING         116
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P22985"
FT   BINDING         148
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P22985"
FT   BINDING         150
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P22985"
FT   BINDING         257..264
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         335
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         345..349
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         358
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         402
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         420
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         766
FT                   /ligand="Mo-molybdopterin"
FT                   /ligand_id="ChEBI:CHEBI:71302"
FT                   /ligand_part="Mo"
FT                   /ligand_part_id="ChEBI:CHEBI:28685"
FT                   /evidence="ECO:0000250"
FT   BINDING         797
FT                   /ligand="Mo-molybdopterin"
FT                   /ligand_id="ChEBI:CHEBI:71302"
FT                   /ligand_part="Mo"
FT                   /ligand_part_id="ChEBI:CHEBI:28685"
FT                   /evidence="ECO:0000250"
FT   BINDING         801
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         879
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         911
FT                   /ligand="Mo-molybdopterin"
FT                   /ligand_id="ChEBI:CHEBI:71302"
FT                   /ligand_part="Mo"
FT                   /ligand_part_id="ChEBI:CHEBI:28685"
FT                   /evidence="ECO:0000250"
FT   BINDING         913
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         1009
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         1078
FT                   /ligand="Mo-molybdopterin"
FT                   /ligand_id="ChEBI:CHEBI:71302"
FT                   /ligand_part="Mo"
FT                   /ligand_part_id="ChEBI:CHEBI:28685"
FT                   /evidence="ECO:0000250"
FT   DISULFID        534..991
FT                   /note="In oxidase form"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1331 AA;  146122 MW;  726C4F72C3B5FB09 CRC64;
     MTADELVFFV NGKKVVEKNA DPETTLLAYL RRKLGLSGTK LGCGEGGCGA CTVMLSKYDR
     FQNKIVHFSA NACLAPICSL HHVAVTTVEG IGSTKSRLHP VQERIAKSHG SQCGFCTPGI
     VMSMYTLLRN QPEPTIEEIE DAFQGNLCRC TGYRPILQGF RTFARDGGCC GGSGNDLNCC
     MNQKTDHKIT LSPSLFNPEE FTPLDPTQEP IFPPELLRLK DTPQKQLRFE GERVTWIQAS
     TLQELLDLKA QDPEAKLVVG NTEIGIEMKF KNMLFPKMVC PAWIPEPVEH GPEGISFGAS
     CPLSLVEKTL LDAVANLPAH QTEVFKGVLE QLRWFAGKQV KSVASIGGNI ITASPISDLN
     PVFMASGAKL TIVSTGTRRT VRMDHTFFPA YRKTLLAPEE ILLSIEIPYS REGEYFSAFK
     QASRREDDIA KVTSGMRVLF NPGTAQVKEL ALCYGGMHDR TVSALQTTRK QISNFWNEEL
     LQNVCAGLAE ELSLAPDAPG GMVEFRRTLT LSFFFKFYLT VLQKLGIQNS KDKCGKLDPT
     HASATLLFQK DPPANVQLFQ EVPKGQCEED MVGRPLPHLA AAMQASGEAV YCDDIPRYEN
     ELSLRLVTST RAHAKIKSID TSEAQKVPGF VCFISADDVP GSNITGIGND EMVFAKDKVT
     CIGHIIGAVV TDTREHAQRA AQAVRITYED LPAIITIEDA IAKDSFYEPE LKIEKGNLTK
     GFSEADNIVS GELYIGGQEH FYLETHCTIA VPKGEAGEME LFVSTQNTTK TQSFVANMLG
     VPANRILVRV KRMGGGFGGK ETRSTVVSTA VPLAAYKTGR PVRCMLDRDE DMLITGGRHP
     FLARYKVGFM KTGRVVALKV EHYSNAGNTL DLSQSIMERA LFHMDNCYNI PNIRGTGRIC
     KTNLPSNTAF RGFGGPQGML IAEHWMSEVA VTCGLPAEEV RRKNMYKEGD LTHFNQKLEG
     FTLPRCWEEC LASSQYHARK READKFNEEN CWKKRGLSII PTKFGISFTV PFLNQAGALV
     HVYTDGSVLL THGGTEMGQG LHTKMVQVAS RALKIPTSKI YISETSTNTV PNTSPTAASV
     STDINGQAVY EACQTILKRL EPFKKKNPSG SWEDWVTAAY LDAVSLSATG FYKTPNIGYS
     FETNSGNPFH YFSYGVACSE VEIDCLTGDH KNLRTDIVMD VGSSLNPAID IGQVEGAFVQ
     GLGLFTLEEL HYSPEGSLHT RGPSTYKIPA FGSIPSEFRV SLLRDCPNKK AIYASKAVGE
     PPLFLAASIF FAIKDAICAA RAGNPDCKTK KLFQLNSPAT PEKIRNACVD QFTRLCVTGT
     AESCKPWSVR V
//