ID   Q8ISZ6_DROHY            Unreviewed;       522 AA.
AC   Q8ISZ6;
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:AAN34706.1};
DE   Flags: Fragment;
GN   Name=ry {ECO:0000313|FlyBase:FBgn0021506};
GN   Synonyms=Xdh {ECO:0000313|EMBL:AAN34706.1};
OS   Drosophila hydei (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7224 {ECO:0000313|EMBL:AAN34706.1};
RN   [1] {ECO:0000313|EMBL:AAN34706.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=4 {ECO:0000313|EMBL:AAN34706.1};
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; AF543118; AAN34706.1; -; Genomic_DNA.
DR   FlyBase; FBgn0021506; Dhyd\ry.
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:AAN34706.1"
FT   NON_TER         522
FT                   /evidence="ECO:0000313|EMBL:AAN34706.1"
SQ   SEQUENCE   522 AA;  57405 MW;  562B2CDDEC5663F6 CRC64;
     QLTAAYDEES LIFRSDRVTW HRPTQLQELL RLKADYPNAK LIVGNTEVGV EMKFKNLLYA
     VLINPIKVPE LLELRESEDG VYFGAAVSLM EIDAYLRKRI EELPESRTRL FQSVVDMLHY
     FAGKQIRNVA CLGGNIMTGS PISDMNPLLT AAGVRLDVAS LADGRXXXRS VHMGAGFFTG
     YRRNVIQGHE ILLGIHIPKT TPDQHVIAFK QARRRDDDIS IVNAAVHVSF EPASNVVQRI
     QIAFGGMAPT TVLAPRTSEL MVGQSWSQAL VERVAESLCI ELPLDASAPG GMIAYRRALV
     VSLFFKSFXA ISRKLCDAGI MPPDAVPKAE LSGADVFHTP ALRSAQLFER VASDQPSHDP
     IGKPKVHAAA LKQATGEAIY TDDIPRMDGE LYLALVLSTK AHAKITKLDA SEALALDGVE
     GFFSAKDLTQ HENEVGPVFH DEYVFANDEA HCYGQIIGAI AAANQALAQR AARLVRVEYE
     ELQPVIVTIE QAIEHASYFP DYPRYVTKGD VVQAFAEAAH VY
//