ID   Q8IT33_9MUSC            Unreviewed;       521 AA.
AC   Q8IT33;
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:AAN34666.1};
DE   Flags: Fragment;
GN   Name=Xdh {ECO:0000313|EMBL:AAN34666.1,
GN   ECO:0000313|FlyBase:FBgn0064109};
OS   Drosophila aldrichi.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=169138 {ECO:0000313|EMBL:AAN34666.1};
RN   [1] {ECO:0000313|EMBL:AAN34666.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=7 {ECO:0000313|EMBL:AAN34666.1};
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; AF543078; AAN34666.1; -; Genomic_DNA.
DR   FlyBase; FBgn0064109; Dald\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:AAN34666.1"
FT   NON_TER         521
FT                   /evidence="ECO:0000313|EMBL:AAN34666.1"
SQ   SEQUENCE   521 AA;  57499 MW;  4E2B43EF81486CC5 CRC64;
     QLTAAYDEES LVFRSDRVTW HRPTQLKELL QLKADHPEAK LIVGNTEVGV EVKFKHFLYP
     VLINPARVPE LLEVRESEEG VYFGAAVSIM DIDAYLRKRI EELPETQTRL FQCVVNMLHY
     FAGKQIRNVA CLGGNIMTGS PISDMNPILT AAGARLEVAS LAGGRXXXRS VYMGEGFFTG
     YRRNVIQADE ILLGIHLQKT TPDDHVVAFK QARRRDDDIA IVNAAVNVKF QAGSNVVERI
     QIAFGGMAPT TVLAPRTSEL MVGQPWSQTL VERVSESLSK ELPLDASAPG GMIAYRRALV
     VSLFFKSYLA ISRKLCDSGI MSPKALPQKE LSGADKFHTP VLRSSQLFER VASDQAKHDP
     IGKPKVHASA LKQATGEAIY TDDIPRMDGE LYLALVLSTK AHAKITKLDA SEALALEGVE
     AFLSATDLTK HENEVGPVFH DEHVFANGVV HCHGQIIGAI VAANQTLAQR AARLVRVEYE
     ELQPVIITIE QAIEHKSYFP HYPRYVTKGD VKQAFAEAAH I
//