XDH_FELCA
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 03-AUG-2022, entry version 107.
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.ENSFCAP00000004209; -.
DR PRIDE; Q9MYW6; -.
DR GeneID; 493692; -.
DR KEGG; fca:493692; -.
DR CTD; 7498; -.
DR eggNOG; KOG0430; Eukaryota.
DR InParanoid; Q9MYW6; -.
DR OrthoDB; 48717at2759; -.
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:0016491; F:oxidoreductase activity; IBA:GO_Central.
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; 3.30.43.10; -; 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; 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 InterPro; IPR022407; OxRdtase_Mopterin_BS.
DR InterPro; IPR014307; Xanthine_DH_ssu.
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; TIGR02963; xanthine_xdhA; 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
