ID Q8IT22_DROMO Unreviewed; 521 AA.
AC Q8IT22;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Xanthine dehydrogenase {ECO:0000313|EMBL:AAN34677.1};
DE Flags: Fragment;
GN Name=Xdh {ECO:0000313|EMBL:AAN34677.1};
OS Drosophila mojavensis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7230 {ECO:0000313|EMBL:AAN34677.1};
RN [1] {ECO:0000313|EMBL:AAN34677.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=15081-1351.9 {ECO:0000313|EMBL:AAN34677.1};
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; AF543089; AAN34677.1; -; Genomic_DNA.
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:0004854; F:xanthine dehydrogenase activity; IEA:EnsemblMetazoa.
DR GO; GO:0006525; P:arginine metabolic process; IEA:EnsemblMetazoa.
DR GO; GO:0008340; P:determination of adult lifespan; IEA:EnsemblMetazoa.
DR GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:EnsemblMetazoa.
DR GO; GO:0006144; P:purine nucleobase metabolic process; IEA:EnsemblMetazoa.
DR GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IEA:EnsemblMetazoa.
DR GO; GO:0006568; P:tryptophan metabolic process; IEA:EnsemblMetazoa.
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; 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 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 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 13..202
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAN34677.1"
FT NON_TER 521
FT /evidence="ECO:0000313|EMBL:AAN34677.1"
SQ SEQUENCE 521 AA; 57546 MW; 428BA3BA69A3E8B1 CRC64;
QLTAAYDKES LVFRSDRVTW HRPTQLQELL QLKADHPAAK LIVGNTEVGV EVKFKHFLYP
VLINPTKVPE LLEVRESEEG VYFGAAVSIM EIDAYLRKRI EELPETQTRL FQCVVDMLHY
FAGKQIRNVA CLGGNIMTGS PISDMNPILT AAGARLEVAS LAGGRXXXRT VHMGAGFFTG
YRRNVIXADE ILLGIHLQKT TPDDHVVAFK QARRRDDDIA IVNAAVNVKF QTGSNVVERI
QIAFGGMAPT TVLAPRTSEL MVGQPWSQTL VERVSESLSK ELPLDASAPG GMIAYRRALV
VSLFFKSYLA ISRKLCDSGI MSPQALPQKE LSGADKFHTP ALRSSQLFER VANDQPSHDP
IGKPKVHASA LKQATGEAIY TDDIPRMDGE LYLALVLSTK AHAKITKLDP SEALALEGVE
AFFSANDLTK HENEVGPVFH DEHVFANEVV HCHGQIIGAI VAANQTLAQR AARLVRVEYE
ELQPVIVTIE QAIEHKSYFP HYPRYVTKGD VEQAFAEADH V
//
