ID Q8ISY5_9MUSC Unreviewed; 514 AA.
AC Q8ISY5;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Xanthine dehydrogenase {ECO:0000313|EMBL:AAN34719.1};
DE Flags: Fragment;
GN Name=ry {ECO:0000313|FlyBase:FBgn0021382};
GN Synonyms=Xdh {ECO:0000313|EMBL:AAN34719.1};
OS Drosophila lummei.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=40371 {ECO:0000313|EMBL:AAN34719.1};
RN [1] {ECO:0000313|EMBL:AAN34719.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=15010-1011.5 {ECO:0000313|EMBL:AAN34719.1};
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; AF543131; AAN34719.1; -; Genomic_DNA.
DR FlyBase; FBgn0021382; Dlum\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:AAN34719.1"
FT NON_TER 514
FT /evidence="ECO:0000313|EMBL:AAN34719.1"
SQ SEQUENCE 514 AA; 56519 MW; 406D53B6BDBC1AA7 CRC64;
QLTAAYDEES LIFRSDRVTW HRPTQLQELL QLKADHPAAK LIVGNTEVGV EVKFKHFLYP
VLINPTKVPE LLELRESDEG IYFGAAVSLM EIDAYLRKRI EELPESQTRF FQCAVDMLHY
FAGKQIRNVA CLGGNIMTGS PISDMNPVLT AAGARLEVAS LTGGXXXXRS VHMGSGFFTG
YRRNVIQPHE ILLGIHFQKT KPDQHVVAFK QARRRDDDIA IVNAAVNVSF EPGSNVVQRI
QMAFGGMAPT TVLAPRTSDL MVGQSWNQAL VERVAESLCA ELPLDASAPG GMIAYRRALV
VSLFFKSYLA ISRKLCDAGI MPPDAVPKAE LSGADSFHTP VLRSAQLFER VASEQPSQDP
IGKPKVHAAA LKQATGEAIY TDDIPRMDGE LYLGFVLSTK AHARIIKLDA SEALALNGVH
AFFSANDLTE HENEVGPVFH DEHVFAAGQV HCYGQIVGAI AAENQTLAQR AARLVRVEYE
ELQPVIVTIE QAIEHQSYYP DYPRYVTKGD VASA
//
