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Database: UniProt
Entry: Q8ISW3_DROAT
LinkDB: Q8ISW3_DROAT
Original site: Q8ISW3_DROAT 
ID   Q8ISW3_DROAT            Unreviewed;       508 AA.
AC   Q8ISW3;
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:AAN34744.1};
DE   Flags: Fragment;
GN   Name=ry {ECO:0000313|FlyBase:FBgn0020209};
GN   Synonyms=Xdh {ECO:0000313|EMBL:AAN34744.1};
OS   Drosophila athabasca (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7248 {ECO:0000313|EMBL:AAN34744.1};
RN   [1] {ECO:0000313|EMBL:AAN34744.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=2 {ECO:0000313|EMBL:AAN34744.1};
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; AF543156; AAN34744.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ISW3; -.
DR   FlyBase; FBgn0020209; Dath\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; 3.30.390.50; 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:AAN34744.1"
FT   NON_TER         508
FT                   /evidence="ECO:0000313|EMBL:AAN34744.1"
SQ   SEQUENCE   508 AA;  56262 MW;  5E4A2D71365EBAEC CRC64;
     QLTTTYDSES LIFSSERVTW YRPTTLRELL QLKADHPTAK LVVGNTEVGV EVKFKHFLYP
     HLINPTQVSE LLEVRESEES IYFGAAVNLM EIDALLRQRI EELPEAQTRL FQCTVDMLHY
     FAGKQIRNVA CLGGNIMTGS PISDMNPVLT AASARLEVAS LVDGKTSHRT VHMGTGFFTG
     YRRNVIEPHE VLLGIHFQKT TPDQHIVAFK QARRRDDDIA IVNAAVNVRF EPQTNVVAEI
     SMAFGGMAPT TVLAPRTSQL MVKQPLNHQL IERVAESLCG ELPLAASAPG GMIAYRRALV
     VSLFFKAYLS ISRRLSEAGI ISGDAIPPEE HSGAELFHTP TLRSAQLFER VCSEQPVCDP
     IGRPELHAAA LKQATGEAIY TDDIPRMDGE VYLGFVLSTK PRAQITKLDA SEALALEGVH
     AFFSHKDLTE HENEVGPVFH DEHVFAAGEV HCYGQIVGAV AADNKALAQR AARLVRVEYK
     ELTPVIVTIE QAIEHGSYFP DYPRYVNK
//
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