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Database: UniProt
Entry: Q86PG6_9MUSC
LinkDB: Q86PG6_9MUSC
Original site: Q86PG6_9MUSC 
ID   Q86PG6_9MUSC            Unreviewed;       625 AA.
AC   Q86PG6;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=Xanthine dehydrogenase {ECO:0000313|EMBL:AAO26037.1};
DE   Flags: Fragment;
GN   Name=Xdh {ECO:0000313|FlyBase:FBgn0042042};
GN   Synonyms=xdh {ECO:0000313|EMBL:AAO26037.1};
OS   Drosophila koepferae.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=41375 {ECO:0000313|EMBL:AAO26037.1};
RN   [1] {ECO:0000313|EMBL:AAO26037.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=14595098; DOI=10.1093/molbev/msh006;
RA   Piccinali R., Aguade M., Hasson E.;
RT   "Comparative molecular population genetics of the Xdh locus in the
RT   cactophilic sibling species Drosophila buzzatii and D. koepferae.";
RL   Mol. Biol. Evol. 21:141-152(2004).
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; AY219202; AAO26037.1; -; Genomic_DNA.
DR   FlyBase; FBgn0042042; Dkoe\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; 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; 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; IPR002888; 2Fe-2S-bd.
DR   InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
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; IPR037165; AldOxase/xan_DH_Mopterin-bd_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   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; PF01799; Fer2_2; 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; 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; 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          110..296
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAO26037.1"
FT   NON_TER         625
FT                   /evidence="ECO:0000313|EMBL:AAO26037.1"
SQ   SEQUENCE   625 AA;  69120 MW;  CACD4465100466F8 CRC64;
     GIVMSMYALL RNAXKPSMRD LEVAFQGNLC RCTGYRPILE GYKTFTKEFA CGMGDKCCKV
     SGKECGGGVN NTDDELFKSS EFQPFDPSQE PIFPPELQLT AVYDEESLVF RSDRVAWYRP
     TRLEELLQLK ADHPEAKLIV GNTEVGVEVK FKHFLYPVLI NPVKVPELLE VCETEDSIYF
     GAAVSLMDID AYLRKRIEVL PETQTRLFQC TVDMLHYFAG KQIRNVACLG GNIMTGSPIS
     DMNTVLTAAG VRLDVASRAG GRRSVHMGTG FFTGYRRNII EDHETLLGIH FQKTTPDXHM
     VAFKQARRRD DDITIVNSTV NVNFKPGTNV VKSIAIAFGG MAPTTVLAPN TSKLMVGQPW
     NQALVERVAE SLCQELPLSA SAPGGMIAYR RALVVSLFFK SYLAISRKLC DAGIXPPBAV
     PQKDLSGADK FHTPTMRSSQ LFERVASNQA THDPIGKPKV HVSALKQATG EAIYTDDIPR
     MDGELYLAFV LSTKAHAKIT KLDASEALAL EGVEAFFSAQ DLTEHQNEVG PVFHDEYVFA
     NGEVHCYGQI IGAIAAANQT LAQRAARLVR VEYLELQPVI VTIEQAIEHK SYFPDYPRFL
     TKGDVEKAFA EADHVYESSC RMGGQ
//
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