ID   XDH_DROSU               Reviewed;        1344 AA.
AC   P91711;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   27-MAR-2024, entry version 120.
DE   RecName: Full=Xanthine dehydrogenase;
DE            Short=XD;
DE            EC=1.17.1.4;
DE   AltName: Full=Protein rosy locus;
GN   Name=Xdh; Synonyms=ry;
OS   Drosophila subobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7241;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8913749; DOI=10.1093/genetics/144.3.1053;
RA   Comeron J.M., Aguade M.;
RT   "Synonymous substitutions in the Xdh gene of Drosophila: heterogeneous
RT   distribution along the coding region.";
RL   Genetics 144:1053-1062(1996).
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; Y08237; CAA69405.1; -; Genomic_DNA.
DR   AlphaFoldDB; P91711; -.
DR   SMR; P91711; -.
DR   FlyBase; FBgn0013892; Dsub\Xdh.
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   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; 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   3: Inferred from homology;
KW   2Fe-2S; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding; Molybdenum;
KW   NAD; Oxidoreductase; Peroxisome.
FT   CHAIN           1..1344
FT                   /note="Xanthine dehydrogenase"
FT                   /id="PRO_0000166081"
FT   DOMAIN          9..96
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   DOMAIN          236..425
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   ACT_SITE        1276
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
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         53
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P22985"
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         78
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P22985"
FT   BINDING         118
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P22985"
FT   BINDING         121
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P22985"
FT   BINDING         153
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P22985"
FT   BINDING         155
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P22985"
FT   BINDING         264..271
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         344
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         354..358
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         367
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         415
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         433
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         781
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         812
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         816
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         894
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         926
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         928
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         1093
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   1344 AA;  147254 MW;  1DDB5BAC0E4C3175 CRC64;
     MSGQQQATSV LVFFVNGKKV TDTNPDPECT LLTYLRDKLR LCGTKLGCAE GGCGACTVMI
     SRMDRGQHKI RHLAVNACLT PVCAMHGCAV TTVEGIGSTR TRLHPVQERL AKAHGSQCGF
     CTPGIVMSMY ALLRNAEQPS MRDLEVAFQG NLCRCTGYRP ILEGYKTFTK EFLCGMGEKC
     CRVNGKGCGG GDDPESVTDD TLFERSKFQP LDASQEPIFP PELQLSNAYD SESLVFSSER
     VTWYRPTTLQ ELLQLKAAHP AAKLVVGNTE VGVEVKFKHF LYPHLINPTL VAELQEVRES
     EESIYFGAAV SLMEIDALLR QRIEELPEAQ TRLFQCTVDM LHYFAGKQIR NVACLGGNIM
     TGSPISDMNP VLTAAGARLE VASIVEGKIS QRTVHMGTGF FTGYRRNVIE PQEVLLGIHF
     QKTTPDQHVV AFKQARRRDD DIAIVNAAVN VRFEPKSNVV AEISMAFGGM APTTVLAPRT
     SQLMVKQPLD HQLLERVAES LCGELPLAAS APGGMIAYRR ALVVSLIFKA YLAISSKLSE
     AGIIAGDAIP PKERSGAELF HTPTLRSAQL FERVCSDQPV CDPIGRPEVH AAALKQATGE
     AIYTDDIPRM DGELYLGFVL STKPRAKITK LDASAALALE GVHAFFSHKD LTVHENEVGP
     VFHDEHVFAA GEVHCYGQIV GAVAADNKAL AQRASRLVRV EYEDLSPVIV TIEQAIEHGS
     YFPDYPRYVT KGNMAEAFAQ AEHTYEGSCR MGGQEHFYLE THAAVAVPRD SDELELFCST
     QHPSEVQKLV AHVTSLPAHR VVCRAKRLGG GFGGKESRGI SVALPVALAA YRLRRPVRCM
     LDRDEDMLIT GTRHPFLFKY KVAFSSDGLI TACDIECYNN AGWSMDLSFS VLERAMYHFE
     NCYHIPNVRV GGWVCKTNLP SNTAFRGFGG PQGMFAGEHI IRDVARIVGR DVLDVMRLNF
     YRTGDTTHYN QQLEHFPIER CLDDCLTQSR YHERRAEIAK FNRENRWRKR GVAVIPTKYG
     IAFGVMHLNQ AGALLNVYGD GSVLLSHGGV EIGQGLNTKM IQCAARALGI PSELIHISET
     ATDKVPNTSP TAASVGSDIN GMAVLDACEK LNKRLAPIKE ALPQATWQEW INKAYFDRVS
     LSATGFYAMP GIGYHPETNP NARTYSYYTN GVGISVVEID CLTGDHQVLS TDIVMDIGSS
     INPAIDIGQI EGAFMQGYGL FTLEELMYSP QGMLYSRGPG MYKLPGFADI PGEFNVSLLT
     GAPNPRAVYS SKAVGEPPLF IGASAFFAIK EAIAAARQEH GLTGDFPLEA PSTSARIRMA
     CQDKFTNLLE VPEAGSFTPW NIVP
//