ID Q6XPW4_DROBU Unreviewed; 625 AA.
AC Q6XPW4;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Xanthine dehydrogenase {ECO:0000313|EMBL:AAP48814.1};
DE Flags: Fragment;
GN Name=ry {ECO:0000313|FlyBase:FBgn0014705};
GN Synonyms=Xdh {ECO:0000313|EMBL:AAP48814.1};
OS Drosophila buzzatii (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7264 {ECO:0000313|EMBL:AAP48814.1};
RN [1] {ECO:0000313|EMBL:AAP48814.1}
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; AY219209; AAP48814.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6XPW4; -.
DR FlyBase; FBgn0014705; Dbuz\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; 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:AAP48814.1"
FT NON_TER 625
FT /evidence="ECO:0000313|EMBL:AAP48814.1"
SQ SEQUENCE 625 AA; 68850 MW; 13BEFC5D200C8E9C CRC64;
GIVMSMYAVV RNAAKPSMRD LEVAFQGNLC RCTGYRPILE GYKTFTKEFA SGMGDKSCKV
KGKECGGGAN NTDDKLFKRS GFQPFDPSQE PIFPPELQLT AAYDEESLVF RSDRVTWYRP
TRLEELLQLK ADHPEAKLIV GNTEVGVEVK FKHFLYPVLI NPVKVPELLE VCETEDSIYF
GAAVSLMDID AYLRKRIEEM PETQTRLFQC TVDMLHYFAG KQIRNVACLG GNIMTGSPIS
DMNPVLTAAG VRLEVASRAG GRRSVHMGTG FFTGYRRNII EAHETLLGIH FQKTTPDQHV
VAFKQARRRD DDIAIVNSAA NVNFKPGTNV VKSIAIAFGG MAPTTVLAPN TSKLMVGQPW
NHALVERVAE SLCQELPLDA SAPGGMIAYP RALVVSLFFK SYLAISRKLC DAGIMPPDAV
PQKDLSGADK FHTPTLRSSQ LFERVASNQP NHDPIGKPKV HASALKQATG EAIYTDDIPR
MDGELYLAFV LSTKAHAKIT KLDASEALAL EGVEAFFSAQ DLTEHQNEVG PVFHDEHVFA
NGEVHCYGQI IGAIAAANQT LAQRAARLVR VEYSELQPVI VTIEQAIEHK SYFPDYPRFL
TKGDVEKAFA EADHVYANSC RMGGQ
//
