ID   Q8IT13_9MUSC            Unreviewed;       521 AA.
AC   Q8IT13;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=Xanthine dehydrogenase {ECO:0000313|EMBL:AAN34686.1};
DE   Flags: Fragment;
GN   Name=Xdh {ECO:0000313|EMBL:AAN34686.1,
GN   ECO:0000313|FlyBase:FBgn0063979};
OS   Drosophila spenceri.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=209069 {ECO:0000313|EMBL:AAN34686.1};
RN   [1] {ECO:0000313|EMBL:AAN34686.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=2 {ECO:0000313|EMBL:AAN34686.1};
RX   PubMed=12524344;
RA   Begun D.J., Whitley P.;
RT   "Molecular population genetics of Xdh and the evolution of base composition
RT   in Drosophila.";
RL   Genetics 162:1725-1735(2002).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
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DR   EMBL; AF543098; AAN34686.1; -; Genomic_DNA.
DR   FlyBase; FBgn0063979; Dspn\Xdh.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 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; 1.
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; 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; 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   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   SMART; SM01008; Ald_Xan_dh_C; 1.
DR   SMART; SM01092; CO_deh_flav_C; 1.
DR   SUPFAM; SSF55447; CO dehydrogenase flavoprotein C-terminal domain-like; 1.
DR   SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Peroxisome {ECO:0000256|ARBA:ARBA00023140}.
FT   DOMAIN          13..202
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAN34686.1"
FT   NON_TER         521
FT                   /evidence="ECO:0000313|EMBL:AAN34686.1"
SQ   SEQUENCE   521 AA;  57361 MW;  D9F7C8FDC7AF1C42 CRC64;
     QLTAAYDEES LIFRSDRVIW HRPTQLQELL QLKADHPAAK LIVGNTEVGV EVKFKHFLYP
     VLINPVKVPE LLEVCESEEG VYFGAAVSVM EIDAYLRRRI EELPKTQTRL FQCVVDMLHY
     FAGKQIRNVA CLGGNIMTGS PISDMNPVLT AAGARLELAS LARGRXXXRS VHMGAGFFTG
     YRRNVIQADE ILLGIHLQKT TPDDHVVAFK QARRRDDDIA IVNAAVCVSF QAGSNVVDRV
     QMAFGGMAPT TVLAPRSSEL LVGQPWSQAL VERVSESLCK ELPLDASAPG GMIAYRRALV
     VSLFFKSYLA ISRKLCDTGI LSSQAVPQKE LSGADKFHTP VLRSSQLFKR VASDQASHDP
     IGKPKVHAAA LKQATGEAIY TDDIPRMDGE LYLALVLSTK AHAKITKLDA SEALALEGVE
     AFFSAEDLTK HENEVGPVFH DEYVFANGVV HCHGQIIGAI VAANQTLAQR AARLVRVEYE
     ELHPVIVTIE QAIEHNSYFP HYPRYVTKGD VKQAFAEATH I
//