XDH_CHICK
ID XDH_CHICK Reviewed; 1358 AA.
AC P47990;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Xanthine dehydrogenase/oxidase;
DE Includes:
DE RecName: Full=Xanthine dehydrogenase;
DE Short=XD;
DE EC=1.17.1.4 {ECO:0000269|PubMed:6953967, ECO:0000269|PubMed:7852355};
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND CATALYTIC
RP ACTIVITY.
RC TISSUE=Liver;
RX PubMed=7852355; DOI=10.1074/jbc.270.6.2818;
RA Satoh A., Amaya Y., Noda K., Nishino T.;
RT "The structure of chicken liver xanthine dehydrogenase. cDNA cloning and
RT the domain structure.";
RL J. Biol. Chem. 270:2818-2826(1995).
RN [2]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND CATALYTIC ACTIVITY.
RX PubMed=6953967; DOI=10.1042/bj2020555;
RA Coolbear K.P., Herzberg G.R., Brosnan J.T.;
RT "Subcellular localization of chicken liver xanthine dehydrogenase. A
RT possible source of cytoplasmic reducing equivalents.";
RL Biochem. J. 202:555-558(1982).
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:P47989}.
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; Evidence={ECO:0000269|PubMed:6953967,
CC ECO:0000269|PubMed:7852355};
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; Evidence={ECO:0000269|PubMed:6953967,
CC ECO:0000269|PubMed:7852355};
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}. Cytoplasm
CC {ECO:0000269|PubMed:6953967}.
CC -!- TISSUE SPECIFICITY: Detected in liver (at protein level).
CC {ECO:0000269|PubMed:6953967}.
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; D13221; BAA02502.1; -; mRNA.
DR PIR; A55711; XOCHDH.
DR RefSeq; NP_990458.1; NM_205127.1.
DR AlphaFoldDB; P47990; -.
DR SMR; P47990; -.
DR STRING; 9031.ENSGALP00000014144; -.
DR PaxDb; P47990; -.
DR PRIDE; P47990; -.
DR GeneID; 396025; -.
DR KEGG; gga:396025; -.
DR CTD; 7498; -.
DR VEuPathDB; HostDB:geneid_396025; -.
DR eggNOG; KOG0430; Eukaryota.
DR InParanoid; P47990; -.
DR OrthoDB; 48717at2759; -.
DR PhylomeDB; P47990; -.
DR Reactome; R-GGA-421178; Urate synthesis.
DR PRO; PR:P47990; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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:0070674; F:hypoxanthine dehydrogenase activity; TAS:Reactome.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum 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:0034418; P:urate biosynthetic process; TAS:Reactome.
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; IPR014309; Xanthine_DH_Mopterin-bd_su.
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 TIGRFAMs; TIGR02965; xanthine_xdhB; 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 1: Evidence at protein level;
KW 2Fe-2S; Cytoplasm; Direct protein sequencing; FAD; Flavoprotein; Iron;
KW Iron-sulfur; Metal-binding; Molybdenum; NAD; Oxidoreductase; Peroxisome;
KW Reference proteome.
FT CHAIN 1..1358
FT /note="Xanthine dehydrogenase/oxidase"
FT /id="PRO_0000166083"
FT DOMAIN 8..95
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 255..440
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT ACT_SITE 1290
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 52
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 55
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 77
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 117
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 120
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 152
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 154
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 283..290
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 363
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 373..377
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 386
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 430
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 448
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
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:0000250"
FT BINDING 827
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 831
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 909
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 941
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 943
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1039
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1108
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"
SQ SEQUENCE 1358 AA; 149614 MW; 53B049B38704995F CRC64;
MAPPETGDEL VFFVNGKKVV EKDVDPETTL LTYLRRKLGL CGTKLGCGEG GCGACTVMIS
KYDPFQKKIL HHTANACLFP ICALHHVAVT TVEGIGNTKS RLHPAQERIA KSHGSQCGFC
TPGIVMSMYT LLRNKPKPKM EDIEDAFQGN LCRCTGYRPI LEGYRTFAVD SNCCGKAANG
TGCCHSKGEN SMNGGCCGGK ANGPGCCMNE KENVTMMSSS LFDSSEFQPL DPTQEPIFPP
ELMTQRNKEQ KQVCFKGERV MWIQPTTLQE LVALKSQYPN AKLVVGNTEV GIEMRLKNML
YPVILAPAWI PEMNAVQQTE TGITFGAACT LSSVEEVLRK AVAELPSYKT EIFQAALEQL
RWFAGPQIRN VAALGGNIMT ASPISDLNPV LMASGSKLTL ISMEGKRTVM MDEKFFTGYR
KTIVKPEEVL LSVEIPYSKE GEYFSAFKQA YRREDDIAIV TCGMRVLFQH GTSRVQEVKL
SYGGMAPTTI LALKTCRELA GRDWNEKLLQ DACRLLAGEM DLSPSAPGGM VEFRRTLTLS
FFFKFYLTVL QKLSKDQNGP NNLCEPVPPN YISATELFHK DPIASTQLFQ EVPRGQLVED
TVGRPLVHLS AAKQACGEAV YCDDIPHYEN ELYLTLVTST QAHAKILSID ASEAQSVPGF
VCFVSAKDVP GSNITGIAND ETVFAEDVVT CVGHIIGAVI ADTQEHSRRA AKAVKIKYEE
LKPIVTIQEA IEQQSFIKPI KRIKKGDVNK GFEESDHILE GEMHIGGQEH FYLETHCTLA
VPKGEDGEME LFVSTQNLMK TQEFTASALG VPSNRIVVRV KRMGGGFGGK ETRNTILTTV
VAVAAFKTGR PVRCMLDRDE DMLISGGRHP FLGRYKVGFM KNGKIKSLEV SYYSNGGNSA
DLSHGVMDRA LLHLDNSYNI PNVSIMGFIC KTNLSSNTAF RGFGGPQGMM IAECWMSDLA
RKCGLPPEEV RKINLYHEGD LTHFNQKLEG FTLRRCWDEC LSSSNYHARK KLIEEFNKQN
RWKKRGMCII PTKFGISFTV PFLNQAGALV HVYTDGSVLL THGGTEMGQG LHTKMIQVAS
RSLGIPTSKI YISETSTNTV PNTSPTAASV SADINGMAVH NACQTILKRL EPIKQSNLKG
SWEDWIKTAY ENCISLSATG FYRIPDVGYN FETNKGKPFH YFSYGVACSE VEIDCLTGDH
KNIRTDIVMD VGTSLNPAID IGQIEGAFVQ GIGLFTMEEL RYSPEGNLYT RGPGMYKIPA
FGDIPTEFYV SLLRDCPNSK AIYSSKAVGE PPLFLSASVF YAIKDAIYSA REDSGVTEPF
RLDSPATPER IRNACVDTFT KMCPSAEPGT FKPWSVRA
