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Q12553

- XDH_EMENI

UniProt

Q12553 - XDH_EMENI

Protein

Xanthine dehydrogenase

Gene

hxA

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 2 (01 May 2007)
      Previous versions | rss
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    Functioni

    Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid By similarity.By similarity

    Catalytic activityi

    Xanthine + NAD+ + H2O = urate + NADH.
    Hypoxanthine + NAD+ + H2O = xanthine + NADH.

    Cofactori

    Binds 2 2Fe-2S clusters.By similarity
    FAD.By similarity
    Binds 1 molybdenum-molybdopterin (Mo-MPT) cofactor per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi73 – 731Iron-sulfur 1By similarity
    Metal bindingi78 – 781Iron-sulfur 1By similarity
    Metal bindingi81 – 811Iron-sulfur 1By similarity
    Metal bindingi103 – 1031Iron-sulfur 1By similarity
    Metal bindingi142 – 1421Iron-sulfur 2By similarity
    Metal bindingi145 – 1451Iron-sulfur 2By similarity
    Metal bindingi177 – 1771Iron-sulfur 2By similarity
    Metal bindingi179 – 1791Iron-sulfur 2By similarity
    Binding sitei374 – 3741FADBy similarity
    Binding sitei397 – 3971FADBy similarity
    Binding sitei459 – 4591FADBy similarity
    Metal bindingi798 – 7981MolybdenumBy similarity
    Metal bindingi829 – 8291Molybdenum; via carbonyl oxygenBy similarity
    Binding sitei833 – 8331SubstrateBy similarity
    Binding sitei911 – 9111SubstrateBy similarity
    Metal bindingi943 – 9431Molybdenum; via amide nitrogenBy similarity
    Binding sitei945 – 9451SubstrateBy similarity
    Binding sitei1041 – 10411Substrate; via amide nitrogenBy similarity
    Metal bindingi1110 – 11101Molybdenum; via amide nitrogenBy similarity
    Active sitei1295 – 12951Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi294 – 3018FADBy similarity
    Nucleotide bindingi384 – 3885FADBy similarity

    GO - Molecular functioni

    1. 2 iron, 2 sulfur cluster binding Source: UniProtKB
    2. electron carrier activity Source: InterPro
    3. flavin adenine dinucleotide binding Source: UniProtKB
    4. iron ion binding Source: InterPro
    5. molybdopterin cofactor binding Source: UniProtKB
    6. UDP-N-acetylmuramate dehydrogenase activity Source: InterPro
    7. xanthine dehydrogenase activity Source: UniProtKB
    8. xanthine oxidase activity Source: InterPro

    GO - Biological processi

    1. purine nucleobase catabolic process Source: ASPGD
    2. xanthine catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Molybdenum, NAD

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Xanthine dehydrogenase (EC:1.17.1.4)
    Alternative name(s):
    Purine hydroxylase I
    Gene namesi
    Name:hxA
    ORF Names:AN5613
    OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
    Taxonomic identifieri227321 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000000560: Chromosome V

    Subcellular locationi

    Peroxisome By similarity

    GO - Cellular componenti

    1. peroxisome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13631363Xanthine dehydrogenasePRO_0000166087Add
    BLAST

    Expressioni

    Inductioni

    By 2-thiouric acid. Repressed by ammonium.1 Publication

    Interactioni

    Protein-protein interaction databases

    STRINGi162425.CADANIAP00003457.

    Structurei

    3D structure databases

    ProteinModelPortaliQ12553.
    SMRiQ12553. Positions 35-193.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini35 – 121872Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
    BLAST
    Domaini266 – 450185FAD-binding PCMH-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the xanthine dehydrogenase family.Curated
    Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
    Contains 1 FAD-binding PCMH-type domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG4630.
    HOGENOMiHOG000191197.
    KOiK00106.
    OMAiCDETFFA.
    OrthoDBiEOG76X67F.

    Family and domain databases

    Gene3Di1.10.150.120. 1 hit.
    3.10.20.30. 1 hit.
    3.30.365.10. 6 hits.
    3.30.43.10. 1 hit.
    3.30.465.10. 1 hit.
    3.90.1170.50. 1 hit.
    InterProiIPR002888. 2Fe-2S-bd.
    IPR001041. 2Fe-2S_ferredoxin-type.
    IPR006058. 2Fe2S_fd_BS.
    IPR000674. Ald_Oxase/Xan_DH_a/b.
    IPR016208. Ald_Oxase/xanthine_DH.
    IPR008274. AldOxase/xan_DH_Mopterin-bd.
    IPR012675. Beta-grasp_dom.
    IPR005107. CO_DH_flav_C.
    IPR016169. CO_DH_flavot_FAD-bd_sub2.
    IPR016166. FAD-bd_2.
    IPR016167. FAD-bd_2_sub1.
    IPR002346. Mopterin_DH_FAD-bd.
    IPR014307. Xanthine_DH_ssu.
    [Graphical view]
    PfamiPF01315. Ald_Xan_dh_C. 1 hit.
    PF02738. Ald_Xan_dh_C2. 1 hit.
    PF03450. CO_deh_flav_C. 1 hit.
    PF00941. FAD_binding_5. 1 hit.
    PF00111. Fer2. 1 hit.
    PF01799. Fer2_2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000127. Xanthine_DH. 1 hit.
    SMARTiSM01008. Ald_Xan_dh_C. 1 hit.
    SM01092. CO_deh_flav_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF47741. SSF47741. 1 hit.
    SSF54292. SSF54292. 1 hit.
    SSF54665. SSF54665. 1 hit.
    SSF55447. SSF55447. 1 hit.
    SSF56003. SSF56003. 1 hit.
    SSF56176. SSF56176. 1 hit.
    TIGRFAMsiTIGR02963. xanthine_xdhA. 1 hit.
    PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
    PS51085. 2FE2S_FER_2. 1 hit.
    PS51387. FAD_PCMH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q12553-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPGVLLQPS QSELEAASPP KAAASLLQLT EEWDDTIRFY LNGTKVILDS     50
    VDPEITLLEY LRGIGLTGTK LGCAEGGCGA CTVVVSQINP TTKKLYHASI 100
    NACIAPLVAV DGKHVITVEG IGNVKNPHAI QQRLAIGNGS QCGFCTPGIV 150
    MSLYALLRND PKPSEHAVEE AFDGNLCRCT GYRPILDAAQ SFTSPIGCGK 200
    ARANGGSGCC MEEQKGTNGC CKGSSEETTE DVKHKFASPD FIEYKPDTEL 250
    IFPPSLWKHE LRPLAFGNKR KKWYRPVTVQ QLLEIKSIHP DAKLIGGSTE 300
    TQIEIKFKQM RYGASVYLGD LAELRQFAFH DNYLEIGANI SLTDLESVCD 350
    QAIERYGSAR GQPFAAIKKQ LRYFAGRQIR NVASPAGNLA TASPISDLNP 400
    VFVATNTTLV ARSLDKETEI PMTQFFRGYR STALPPDAII SSLRIPTASE 450
    KGEYLRAYKQ SKRKDDDIAI VNAALRVSLS SSNDVTSVSL VFGGMAPLTV 500
    SARNAEAFLT GKKFTDPATL EGTMGALEQD FNLKFGVPGG MATYRKSLAL 550
    GFFYRFYHDV LSQIEARSSD LDNSVVAEIE RAISTGEKDN EASAAYQQRV 600
    LGRAGPHLSA LKQATGEAQY TDDIPAQKNE LYGCMVLSTK AHAKLLSVNT 650
    EAALEIPGVI DYVDHKDLPS PRANWWGAPN CDEVFFAVDK VTTAGQPIGM 700
    ILANTAKAAE EGARAVKVEY EELPVILSIE EAIEAQSFFE RFRYIKNGDP 750
    ESAFRDADHV FEGVSRMGGQ EHFYLETQAC VAIPKAEDGE MEIWSSTQNP 800
    TETQSYVAQV TGVAANKIVS RVKRLGGGFG GKETRSVQLA GICATAAAKV 850
    RRPVRCMLNR DEDIATSGQR HPFYCKWKVG VTREGKLLAL DADVYANGGH 900
    TQDLSGAVVE RSLSHIDNVY RFPNIYVRGR ICKTNTVSNT AFRGFGGPQG 950
    LFFAESIISE VADHLDLQVE QLRILNMYEP GDMTHFNQEL KDWHVPLMYD 1000
    QVLQESEYFE RRKAVEEYNR THKWSKRGMA IIPTKFGISF TALFLNQAGA 1050
    LVHIYHDGSV LVAHGGVEMG QGLHTKMTMI AAEALGVPLS DVFISETATN 1100
    TVANTSSTAA SASSDLNGYA IYNACTQLNE RLKPYREKMP NATLKDLAHA 1150
    AYFDRVNLSA QGYYRTPDIG YTWGENKGQM FFYFTQGVTA AEVEIDTLTG 1200
    DWTPLRADIK MDVGRTINPS IDYGQIEGAY IQGQGLFTTE ESLWHRTTGQ 1250
    IFTKGPGNYK IPGFRDIPQI FNVSLLKDVE WENLRTIQRS RGVGEPPLFM 1300
    GSAAFFAIRD ALKAARKEWG VTDVLSLVSP ATPERIRVSC ADPIIERARV 1350
    KAEEGEKSFF VAI 1363
    Length:1,363
    Mass (Da):149,523
    Last modified:May 1, 2007 - v2
    Checksum:i18D8F50B731EDE4B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti741 – 7411R → H in CAA58034. (PubMed:7876088)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X82827 Genomic DNA. Translation: CAA58034.1.
    AACD01000098 Genomic DNA. Translation: EAA62706.1.
    BN001305 Genomic DNA. Translation: CBF81549.1.
    PIRiA55875.
    RefSeqiXP_663217.1. XM_658125.1.

    Genome annotation databases

    EnsemblFungiiCADANIAT00003457; CADANIAP00003457; CADANIAG00003457.
    GeneIDi2871900.
    KEGGiani:AN5613.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X82827 Genomic DNA. Translation: CAA58034.1 .
    AACD01000098 Genomic DNA. Translation: EAA62706.1 .
    BN001305 Genomic DNA. Translation: CBF81549.1 .
    PIRi A55875.
    RefSeqi XP_663217.1. XM_658125.1.

    3D structure databases

    ProteinModelPortali Q12553.
    SMRi Q12553. Positions 35-193.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 162425.CADANIAP00003457.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANIAT00003457 ; CADANIAP00003457 ; CADANIAG00003457 .
    GeneIDi 2871900.
    KEGGi ani:AN5613.2.

    Phylogenomic databases

    eggNOGi COG4630.
    HOGENOMi HOG000191197.
    KOi K00106.
    OMAi CDETFFA.
    OrthoDBi EOG76X67F.

    Family and domain databases

    Gene3Di 1.10.150.120. 1 hit.
    3.10.20.30. 1 hit.
    3.30.365.10. 6 hits.
    3.30.43.10. 1 hit.
    3.30.465.10. 1 hit.
    3.90.1170.50. 1 hit.
    InterProi IPR002888. 2Fe-2S-bd.
    IPR001041. 2Fe-2S_ferredoxin-type.
    IPR006058. 2Fe2S_fd_BS.
    IPR000674. Ald_Oxase/Xan_DH_a/b.
    IPR016208. Ald_Oxase/xanthine_DH.
    IPR008274. AldOxase/xan_DH_Mopterin-bd.
    IPR012675. Beta-grasp_dom.
    IPR005107. CO_DH_flav_C.
    IPR016169. CO_DH_flavot_FAD-bd_sub2.
    IPR016166. FAD-bd_2.
    IPR016167. FAD-bd_2_sub1.
    IPR002346. Mopterin_DH_FAD-bd.
    IPR014307. Xanthine_DH_ssu.
    [Graphical view ]
    Pfami PF01315. Ald_Xan_dh_C. 1 hit.
    PF02738. Ald_Xan_dh_C2. 1 hit.
    PF03450. CO_deh_flav_C. 1 hit.
    PF00941. FAD_binding_5. 1 hit.
    PF00111. Fer2. 1 hit.
    PF01799. Fer2_2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000127. Xanthine_DH. 1 hit.
    SMARTi SM01008. Ald_Xan_dh_C. 1 hit.
    SM01092. CO_deh_flav_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47741. SSF47741. 1 hit.
    SSF54292. SSF54292. 1 hit.
    SSF54665. SSF54665. 1 hit.
    SSF55447. SSF55447. 1 hit.
    SSF56003. SSF56003. 1 hit.
    SSF56176. SSF56176. 1 hit.
    TIGRFAMsi TIGR02963. xanthine_xdhA. 1 hit.
    PROSITEi PS00197. 2FE2S_FER_1. 1 hit.
    PS51085. 2FE2S_FER_2. 1 hit.
    PS51387. FAD_PCMH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and molecular characterization of hxA, the gene coding for the xanthine dehydrogenase (purine hydroxylase I) of Aspergillus nidulans."
      Glatigny A., Scazzocchio C.
      J. Biol. Chem. 270:3534-3550(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
      Strain: biA1.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
    3. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
      Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
      , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
      Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENOME REANNOTATION.
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

    Entry informationi

    Entry nameiXDH_EMENI
    AccessioniPrimary (citable) accession number: Q12553
    Secondary accession number(s): C8VFY5, Q5B1G7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 1, 2007
    Last modified: October 1, 2014
    This is version 105 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3