ID   XDH_EMENI               Reviewed;        1363 AA.
AC   Q12553; Q5B1G7;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   16-JUN-2009, entry version 66.
DE   RecName: Full=Xanthine dehydrogenase;
DE            EC=1.17.1.4;
DE   AltName: Full=Purine hydroxylase I;
GN   Name=hxA; ORFNames=AN5613;
OS   Emericella nidulans (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Emericella.
OX   NCBI_TaxID=162425;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=biA1;
RX   MEDLINE=95181302; PubMed=7876088; DOI=10.1074/jbc.270.8.3534;
RA   Glatigny A., Scazzocchio C.;
RT   "Cloning and molecular characterization of hxA, the gene coding for
RT   the xanthine dehydrogenase (purine hydroxylase I) of Aspergillus
RT   nidulans.";
RL   J. Biol. Chem. 270:3534-3550(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC 4;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R.,
RA   Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
CC   -!- CATALYTIC ACTIVITY: Xanthine + NAD(+) + H(2)O = urate + NADH.
CC   -!- CATALYTIC ACTIVITY: Hypoxanthine + NAD(+) + H(2)O = xanthine +
CC       NADH.
CC   -!- COFACTOR: Binds 2 2Fe-2S clusters.
CC   -!- COFACTOR: FAD.
CC   -!- COFACTOR: Molybdopterin.
CC   -!- SUBCELLULAR LOCATION: Peroxisome.
CC   -!- INDUCTION: By 2-tiouric acid. Repressed by ammonium.
CC   -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC   -!- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain.
CC   -!- SIMILARITY: Contains 1 FAD-binding PCMH-type domain.
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DR   EMBL; X82827; CAA58034.1; -; Genomic_DNA.
DR   EMBL; AACD01000098; EAA62706.1; -; Genomic_DNA.
DR   PIR; A55875; A55875.
DR   RefSeq; XP_663217.1; -.
DR   HSSP; P80457; 1FO4.
DR   GeneID; 2871900; -.
DR   KEGG; ani:AN5613.2; -.
DR   BRENDA; 1.17.1.4; 3859.
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:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004854; F:xanthine dehydrogenase activity; IEA:EC.
DR   GO; GO:0004855; F:xanthine oxidase activity; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR002888; 2Fe-2S_bd.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR   InterPro; IPR016208; Ald_Oxase/xanthine_DH.
DR   InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd.
DR   InterPro; IPR005107; CO_DH_flav_C.
DR   InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2.
DR   InterPro; IPR016166; FAD-bd_2.
DR   InterPro; IPR016167; FAD-bd_2_sub1.
DR   InterPro; IPR001041; Ferredoxin.
DR   InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR   InterPro; IPR000572; OxRdtase_Mopterin-bd.
DR   InterPro; IPR014307; Xanthine_DH_ssu.
DR   Gene3D; G3DSA:3.30.365.10; Ald_xan_DH_mo_bd; 2.
DR   Gene3D; G3DSA:3.90.1170.50; Aldxan_DH_hamm; 1.
DR   Gene3D; G3DSA:3.30.390.50; CO_DH_flav_C; 1.
DR   Gene3D; G3DSA:3.30.465.10; CO_DH_flavoprot_FAD-bd_sub2; 1.
DR   Gene3D; G3DSA:3.30.43.10; FAD-binding_2_sub1; 1.
DR   Pfam; PF01315; Ald_Xan_dh_C; 1.
DR   Pfam; PF02738; Ald_Xan_dh_C2; 1.
DR   Pfam; PF03450; CO_deh_flav_C; 1.
DR   Pfam; PF00941; FAD_binding_5; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF01799; Fer2_2; 1.
DR   PIRSF; PIRSF000127; Xanthine_DH; 1.
DR   ProDom; PD186071; 2Fe-2S_bind; 1.
DR   TIGRFAMs; TIGR02963; xanthine_xdhA; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
DR   PROSITE; PS00559; MOLYBDOPTERIN_EUK; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   2Fe-2S; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding;
KW   Molybdenum; NAD; Oxidoreductase; Peroxisome.
FT   CHAIN         1   1363       Xanthine dehydrogenase.
FT                                /FTId=PRO_0000166087.
FT   DOMAIN       35    121       2Fe-2S ferredoxin-type.
FT   DOMAIN      266    450       FAD-binding PCMH-type.
FT   METAL        73     73       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL        78     78       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL        81     81       Iron-sulfur (2Fe-2S) (By similarity).
FT   CONFLICT    741    741       R -> H (in Ref. 1; CAA58034).
SQ   SEQUENCE   1363 AA;  149523 MW;  18D8F50B731EDE4B CRC64;
     MAPGVLLQPS QSELEAASPP KAAASLLQLT EEWDDTIRFY LNGTKVILDS VDPEITLLEY
     LRGIGLTGTK LGCAEGGCGA CTVVVSQINP TTKKLYHASI NACIAPLVAV DGKHVITVEG
     IGNVKNPHAI QQRLAIGNGS QCGFCTPGIV MSLYALLRND PKPSEHAVEE AFDGNLCRCT
     GYRPILDAAQ SFTSPIGCGK ARANGGSGCC MEEQKGTNGC CKGSSEETTE DVKHKFASPD
     FIEYKPDTEL IFPPSLWKHE LRPLAFGNKR KKWYRPVTVQ QLLEIKSIHP DAKLIGGSTE
     TQIEIKFKQM RYGASVYLGD LAELRQFAFH DNYLEIGANI SLTDLESVCD QAIERYGSAR
     GQPFAAIKKQ LRYFAGRQIR NVASPAGNLA TASPISDLNP VFVATNTTLV ARSLDKETEI
     PMTQFFRGYR STALPPDAII SSLRIPTASE KGEYLRAYKQ SKRKDDDIAI VNAALRVSLS
     SSNDVTSVSL VFGGMAPLTV SARNAEAFLT GKKFTDPATL EGTMGALEQD FNLKFGVPGG
     MATYRKSLAL GFFYRFYHDV LSQIEARSSD LDNSVVAEIE RAISTGEKDN EASAAYQQRV
     LGRAGPHLSA LKQATGEAQY TDDIPAQKNE LYGCMVLSTK AHAKLLSVNT EAALEIPGVI
     DYVDHKDLPS PRANWWGAPN CDEVFFAVDK VTTAGQPIGM ILANTAKAAE EGARAVKVEY
     EELPVILSIE EAIEAQSFFE RFRYIKNGDP ESAFRDADHV FEGVSRMGGQ EHFYLETQAC
     VAIPKAEDGE MEIWSSTQNP TETQSYVAQV TGVAANKIVS RVKRLGGGFG GKETRSVQLA
     GICATAAAKV RRPVRCMLNR DEDIATSGQR HPFYCKWKVG VTREGKLLAL DADVYANGGH
     TQDLSGAVVE RSLSHIDNVY RFPNIYVRGR ICKTNTVSNT AFRGFGGPQG LFFAESIISE
     VADHLDLQVE QLRILNMYEP GDMTHFNQEL KDWHVPLMYD QVLQESEYFE RRKAVEEYNR
     THKWSKRGMA IIPTKFGISF TALFLNQAGA LVHIYHDGSV LVAHGGVEMG QGLHTKMTMI
     AAEALGVPLS DVFISETATN TVANTSSTAA SASSDLNGYA IYNACTQLNE RLKPYREKMP
     NATLKDLAHA AYFDRVNLSA QGYYRTPDIG YTWGENKGQM FFYFTQGVTA AEVEIDTLTG
     DWTPLRADIK MDVGRTINPS IDYGQIEGAY IQGQGLFTTE ESLWHRTTGQ IFTKGPGNYK
     IPGFRDIPQI FNVSLLKDVE WENLRTIQRS RGVGEPPLFM GSAAFFAIRD ALKAARKEWG
     VTDVLSLVSP ATPERIRVSC ADPIIERARV KAEEGEKSFF VAI
//