ID   XDH_CALVI               Reviewed;        1353 AA.
AC   P08793;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   27-MAR-2024, entry version 130.
DE   RecName: Full=Xanthine dehydrogenase;
DE            Short=XD;
DE            EC=1.17.1.4;
GN   Name=XDH;
OS   Calliphora vicina (Blue blowfly) (Calliphora erythrocephala).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC   Calliphoridae; Calliphorinae; Calliphora.
OX   NCBI_TaxID=7373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=2516831; DOI=10.1016/0378-1119(89)90432-0;
RA   Houde M., Tiveron M.C., Bregegere F.;
RT   "Divergence of the nucleotide sequences encoding xanthine dehydrogenase in
RT   Calliphora vicina and Drosophila melanogaster.";
RL   Gene 85:391-402(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 208-367.
RX   PubMed=2830167; DOI=10.1016/0378-1119(87)90328-3;
RA   Rocher-Chambonnet C., Berreur P., Houde M., Tiveron M.C., Lepesant J.-A.,
RA   Bregegere F.;
RT   "Cloning and partial characterization of the xanthine dehydrogenase gene of
RT   Calliphora vicina, a distant relative of Drosophila melanogaster.";
RL   Gene 59:201-212(1987).
CC   -!- FUNCTION: Key enzyme in purine degradation. Catalyzes the oxidation of
CC       hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric
CC       acid (By similarity). {ECO:0000250}.
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   -!- 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   -!- 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}.
CC   -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; X07229; CAA30189.1; -; mRNA.
DR   EMBL; X07323; CAA30281.1; -; Genomic_DNA.
DR   EMBL; X07324; CAA30281.1; JOINED; Genomic_DNA.
DR   EMBL; X07325; CAA30281.1; JOINED; Genomic_DNA.
DR   EMBL; M18423; AAA27879.1; -; Genomic_DNA.
DR   PIR; JQ0407; JQ0407.
DR   AlphaFoldDB; P08793; -.
DR   SMR; P08793; -.
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: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; 4.
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:SF100; 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; 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; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding; Molybdenum;
KW   NAD; Oxidoreductase; Peroxisome.
FT   CHAIN           1..1353
FT                   /note="Xanthine dehydrogenase"
FT                   /id="PRO_0000166078"
FT   DOMAIN          17..104
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   DOMAIN          245..434
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   ACT_SITE        1285
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         56
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P22985"
FT   BINDING         61
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P22985"
FT   BINDING         64
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P22985"
FT   BINDING         86
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P22985"
FT   BINDING         126
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P22985"
FT   BINDING         129
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P22985"
FT   BINDING         161
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P22985"
FT   BINDING         163
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P22985"
FT   BINDING         273..280
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         353
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         363..367
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         376
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         424
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         442
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         790
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         821
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         825
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         903
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         935
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         937
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         1102
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   1353 AA;  150209 MW;  7120361C57C3E297 CRC64;
     MTQEHNAAVL DLNPTFSTLI FFVNGKKVID TNPDPECTLL TYLREKLRLC GTKLGCGEGG
     CGACTVMISR IDTLTNRIKH IAVNACLTPV CAMHGSAVTT VEGIGSTRTR LHPVQERLAK
     AHGSQCGFCT PGIVMSMYAL LRNLSQPSMK DLEIAFQGNL CRCTGYRPIL EGYKTFTKEF
     GCAMGDKCCK VNGNKCGEGM ENGGDMVDDK LFEKSEFVPF DPSQEPIFPP ELQLNKDWDS
     QTLVYKGERA TWYRPGNLED LLKIKAQFPE AKLVVGNTEI GVEVKFKHFL YPVLVNPTKV
     KEMIDVQELE DSIYFGASVS LMDIDRILRS SIEKLPEHQT RFFQCAVNML HYFAGKQIRN
     VASLGGNIMT GSPISDMNPV LMAGAVKFKV AKYVEGQIKY REVCMASGFF TGYRKNVIEP
     TEILVGLYFP KTLEHQYVVA FKQAKRRDDD IAIVNAAINV FIDPRSITVD KVYMAFGGMA
     PTTVLATRTA DIMVKQQWNK VLMERVVENL CAELPLAPSA PGGMIAYRRS LVVSLFFKAY
     LTITQQLIKS GILPQDSLPQ EELSGSDVFH TPALKSAQLF EKVSNKQSEC DPIGRPKIHA
     SALKQATGEA IYCDDMPRME NELYLALVLS TKAHAKILSI DASEALAMPG VHAFFSSKDI
     TQHENEVGPV FHDEEVFASD MVYCQGQVIG AIAADNPNFS SKTARKVTIE YEDIKPVIIT
     IEQAIEHKSY FPDYPRFTEI GDVEKAFSEA DHVYEGSCRM GGQEHFYLET HASLAVPRDS
     DEIEIFCSTQ HPSEVQKLVA HVLSTSAHRV VCRAKRLGGG FGGKESRAIA VALPVALACH
     RLRRPIRCML DRDEDMMITG TRHPFLFKYK IAFTSEGRLT GCYIECYNNA GWSMDLSFSV
     LERAMFHFEN CYKIPNIKVG GWVCKTNLPS NTAFRGFGGP QGMFAGEHII RDVARILGKD
     YLEIMKQNFY KEGDITHYQQ KLDNFPIEKC FYDCLQQSNY YQKRKEIEEF NRNHRWRKRG
     ISLVPTKYGI AFGVSHLNQA GALINIYADG SVLLSHGGVE IGQGLHTKMI QCCARALQIP
     IEFIHISETA TDKVPNTSPT AASSGSDLNG MAVLDACEKL NKRLAPIKEA NPNGSWTEWI
     NKAYFERVSL SATGFYRMPD IGYDPVQNPN ALMYNYFTNG VGSSIVEIDC LTGDHQVLST
     DIVMDIGSSL NPAIDIGQIE GAFMQGYGLF TLEEMIYSPQ GVLYSRGPGM YKLPGFADIP
     GEFNVTILTG AANPRAVYSS KAVGEPPLFI GCSVFFAIKE AITSARLMNG LSEDFKLESP
     ATSARIRMAC QDEFTNLIEQ PPAGSYVPWN IVP
//