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 03-APR-2013, entry version 98.
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; Trichocomaceae; Emericella.
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 ion (molybdopterin) per subunit (By
CC 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; HASINAC; -.
DR OrthoDB; EOG4F4WK4; -.
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; 2Fe-2S_bind; 1.
DR SUPFAM; SSF56003; Ald_xan_DH_mo_bd; 1.
DR SUPFAM; SSF54665; Aldxan_dh_hamm; 1.
DR SUPFAM; SSF55447; CO_deh_flav_C; 1.
DR SUPFAM; SSF56176; FAD-binding_2; 1.
DR SUPFAM; SSF54292; Ferredoxin; 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; 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
//
