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Database: UniProt
Entry: Q12553
LinkDB: Q12553
Original site: Q12553 
ID   XDH_EMENI               Reviewed;        1363 AA.
AC   Q12553; C8VFY5; Q5B1G7;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   19-FEB-2014, entry version 103.
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 (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=biA1;
RX   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 A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
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).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- FUNCTION: Key enzyme in purine degradation. Catalyzes the
CC       oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of
CC       xanthine to uric acid (By similarity).
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 (By similarity).
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- COFACTOR: Binds 1 molybdenum-molybdopterin (Mo-MPT) cofactor per
CC       subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Peroxisome (By similarity).
CC   -!- INDUCTION: By 2-thiouric 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   EMBL; BN001305; CBF81549.1; -; Genomic_DNA.
DR   PIR; A55875; A55875.
DR   RefSeq; XP_663217.1; XM_658125.1.
DR   ProteinModelPortal; Q12553; -.
DR   SMR; Q12553; 35-193.
DR   STRING; 162425.CADANIAP00003457; -.
DR   EnsemblFungi; CADANIAT00003457; CADANIAP00003457; CADANIAG00003457.
DR   GeneID; 2871900; -.
DR   KEGG; ani:AN5613.2; -.
DR   eggNOG; COG4630; -.
DR   HOGENOM; HOG000191197; -.
DR   KO; K00106; -.
DR   OMA; CDETFFA; -.
DR   OrthoDB; EOG76X67F; -.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:UniProtKB.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; ISS:UniProtKB.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; ISS:UniProtKB.
DR   GO; GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0004854; F:xanthine dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0004855; F:xanthine oxidase activity; IEA:InterPro.
DR   GO; GO:0009115; P:xanthine catabolic process; ISS:UniProtKB.
DR   Gene3D; 1.10.150.120; -; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.30.365.10; -; 6.
DR   Gene3D; 3.30.43.10; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.90.1170.50; -; 1.
DR   InterPro; IPR002888; 2Fe-2S-bd.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
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; IPR012675; Beta-grasp_dom.
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; IPR002346; Mopterin_DH_FAD-bd.
DR   InterPro; IPR014307; Xanthine_DH_ssu.
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   SMART; SM01008; Ald_Xan_dh_C; 1.
DR   SMART; SM01092; CO_deh_flav_C; 1.
DR   SUPFAM; SSF47741; SSF47741; 1.
DR   SUPFAM; SSF54292; SSF54292; 1.
DR   SUPFAM; SSF54665; SSF54665; 1.
DR   SUPFAM; SSF55447; SSF55447; 1.
DR   SUPFAM; SSF56003; SSF56003; 1.
DR   SUPFAM; SSF56176; SSF56176; 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.
PE   2: Evidence at transcript level;
KW   2Fe-2S; Complete proteome; FAD; Flavoprotein; Iron; Iron-sulfur;
KW   Metal-binding; Molybdenum; NAD; Oxidoreductase; Peroxisome;
KW   Reference proteome.
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   NP_BIND     294    301       FAD (By similarity).
FT   NP_BIND     384    388       FAD (By similarity).
FT   ACT_SITE   1295   1295       Proton acceptor (By similarity).
FT   METAL        73     73       Iron-sulfur 1 (By similarity).
FT   METAL        78     78       Iron-sulfur 1 (By similarity).
FT   METAL        81     81       Iron-sulfur 1 (By similarity).
FT   METAL       103    103       Iron-sulfur 1 (By similarity).
FT   METAL       142    142       Iron-sulfur 2 (By similarity).
FT   METAL       145    145       Iron-sulfur 2 (By similarity).
FT   METAL       177    177       Iron-sulfur 2 (By similarity).
FT   METAL       179    179       Iron-sulfur 2 (By similarity).
FT   METAL       798    798       Molybdenum (By similarity).
FT   METAL       829    829       Molybdenum; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       943    943       Molybdenum; via amide nitrogen (By
FT                                similarity).
FT   METAL      1110   1110       Molybdenum; via amide nitrogen (By
FT                                similarity).
FT   BINDING     374    374       FAD (By similarity).
FT   BINDING     397    397       FAD (By similarity).
FT   BINDING     459    459       FAD (By similarity).
FT   BINDING     833    833       Substrate (By similarity).
FT   BINDING     911    911       Substrate (By similarity).
FT   BINDING     945    945       Substrate (By similarity).
FT   BINDING    1041   1041       Substrate; via amide nitrogen (By
FT                                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
//
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