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UniProtKB/Swiss-Prot entry Q12553

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name XDH_EMENI
Primary accession number Q12553
Secondary accession number Q5B1G7
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on May 1, 2007 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 61)
Name and origin of the protein
Protein name Xanthine dehydrogenase
Synonyms EC 1.17.1.4
Purine hydroxylase I
Gene name
Name: hxA
ORFNames: AN5613
From
Emericella nidulans (Aspergillus nidulans) [TaxID: 162425] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; Eurotiomycetidae; Eurotiales; Trichocomaceae; Emericella.
Protein existence 2: Evidence at transcript level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=biA1;
DOI=10.1074/jbc.270.8.3534; PubMed=7876088 [NCBI, ExPASy, EBI, Israel, Japan]
Glatigny A., Scazzocchio C.;
"Cloning and molecular characterization of hxA, the gene coding for the xanthine dehydrogenase (purine hydroxylase I) of Aspergillus nidulans.";
J. Biol. Chem. 270:3534-3550(1995).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=FGSC 4;
DOI=10.1038/nature04341; PubMed=16372000 [NCBI, ExPASy, EBI, Israel, Japan]
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae.";
Nature 438:1105-1115(2005).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X82827; CAA58034.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AACD01000098; EAA62706.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A55875; A55875.
RefSeq XP_663217.1; -.
3D structure databases
HSSP P80457; 1FO4. [HSSP ENTRY / PDB]
ModBase Q12553.
Ontologies
GO
GO:0005777; Cellular component: peroxisome (inferred from electronic annotation from UniProtKB-KW).
GO:0051537; Molecular function: 2 iron, 2 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660; Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0030151; Molecular function: molybdenum ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004854; Molecular function: xanthine dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0004855; Molecular function: xanthine oxidase activity (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR002888; 2Fe-2S_bd.
IPR006058; 2Fe2S_fd_BS.
IPR000674; Ald_Oxase/Xan_DHase_a/b.
IPR016208; Ald_Oxase/xanthine_DHase.
IPR008274; AldOxase/xan_DHase_Mopterin-bd.
IPR005107; CO_DHase_flav_C.
IPR016169; CO_DHase_flavot_FAD-bd_sub2.
IPR016167; FAD-bd_2_sub1.
IPR001041; Ferredoxin.
IPR002346; Mopterin_DHase_FAD-bd.
IPR000572; OxRdtase_Mopterin-bd.
IPR014307; Xanthine_DHase_ssu.
Graphical view of domain structure.
Gene3D G3DSA:3.30.365.10; Ald_xan_DH_mo_bd; 2.
G3DSA:3.90.1170.50; Aldxan_DH_hamm; 1.
G3DSA:3.30.390.50; CO_DH_flav_C; 1.
G3DSA:3.30.465.10; CO_DH_flavoprot_FAD-bd_sub2; 1.
G3DSA:3.30.43.10; FAD-binding_2_sub1; 1.
Pfam PF01315; Ald_Xan_dh_C; 1.
PF02738; Ald_Xan_dh_C2; 1.
PF03450; CO_deh_flav_C; 1.
PF00941; FAD_binding_5; 1.
PF00111; Fer2; 1.
PF01799; Fer2_2; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000127; Xanthine_DH; 1.
ProDom PD186071; 2Fe-2S_bind; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR02963; xanthine_xdhA; 1.
PROSITE PS00197; 2FE2S_FER_1; 1.
PS51085; 2FE2S_FER_2; 1.
PS51387; FAD_PCMH; 1.
PS00559; MOLYBDOPTERIN_EUK; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
GeneID 2871900; -.
KEGG ani:AN5613.2; -.
Other
ProtoNet Q12553.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
2Fe-2S; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding; Molybdenum; NAD; Oxidoreductase; Peroxisome.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   1363  1363     Xanthine dehydrogenase. PRO_0000166087
DOMAIN   35    121  87     2Fe-2S ferredoxin-type. 
DOMAIN   266    450  185     FAD-binding PCMH-type. 
METAL   73     73        Iron-sulfur (2Fe-2S) (By similarity). 
METAL   78     78        Iron-sulfur (2Fe-2S) (By similarity). 
METAL   81     81        Iron-sulfur (2Fe-2S) (By similarity). 
CONFLICT   741    741        R -> H (in Ref. 1; CAA58034). 
Sequence information
Length: 1363 AA [This is the length of the unprocessed precursor] Molecular weight: 149523 Da [This is the MW of the unprocessed precursor] CRC64: 18D8F50B731EDE4B [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MAPGVLLQPS QSELEAASPP KAAASLLQLT EEWDDTIRFY LNGTKVILDS VDPEITLLEY 

        70         80         90        100        110        120 
LRGIGLTGTK LGCAEGGCGA CTVVVSQINP TTKKLYHASI NACIAPLVAV DGKHVITVEG 

       130        140        150        160        170        180 
IGNVKNPHAI QQRLAIGNGS QCGFCTPGIV MSLYALLRND PKPSEHAVEE AFDGNLCRCT 

       190        200        210        220        230        240 
GYRPILDAAQ SFTSPIGCGK ARANGGSGCC MEEQKGTNGC CKGSSEETTE DVKHKFASPD 

       250        260        270        280        290        300 
FIEYKPDTEL IFPPSLWKHE LRPLAFGNKR KKWYRPVTVQ QLLEIKSIHP DAKLIGGSTE 

       310        320        330        340        350        360 
TQIEIKFKQM RYGASVYLGD LAELRQFAFH DNYLEIGANI SLTDLESVCD QAIERYGSAR 

       370        380        390        400        410        420 
GQPFAAIKKQ LRYFAGRQIR NVASPAGNLA TASPISDLNP VFVATNTTLV ARSLDKETEI 

       430        440        450        460        470        480 
PMTQFFRGYR STALPPDAII SSLRIPTASE KGEYLRAYKQ SKRKDDDIAI VNAALRVSLS 

       490        500        510        520        530        540 
SSNDVTSVSL VFGGMAPLTV SARNAEAFLT GKKFTDPATL EGTMGALEQD FNLKFGVPGG 

       550        560        570        580        590        600 
MATYRKSLAL GFFYRFYHDV LSQIEARSSD LDNSVVAEIE RAISTGEKDN EASAAYQQRV 

       610        620        630        640        650        660 
LGRAGPHLSA LKQATGEAQY TDDIPAQKNE LYGCMVLSTK AHAKLLSVNT EAALEIPGVI 

       670        680        690        700        710        720 
DYVDHKDLPS PRANWWGAPN CDEVFFAVDK VTTAGQPIGM ILANTAKAAE EGARAVKVEY 

       730        740        750        760        770        780 
EELPVILSIE EAIEAQSFFE RFRYIKNGDP ESAFRDADHV FEGVSRMGGQ EHFYLETQAC 

       790        800        810        820        830        840 
VAIPKAEDGE MEIWSSTQNP TETQSYVAQV TGVAANKIVS RVKRLGGGFG GKETRSVQLA 

       850        860        870        880        890        900 
GICATAAAKV RRPVRCMLNR DEDIATSGQR HPFYCKWKVG VTREGKLLAL DADVYANGGH 

       910        920        930        940        950        960 
TQDLSGAVVE RSLSHIDNVY RFPNIYVRGR ICKTNTVSNT AFRGFGGPQG LFFAESIISE 

       970        980        990       1000       1010       1020 
VADHLDLQVE QLRILNMYEP GDMTHFNQEL KDWHVPLMYD QVLQESEYFE RRKAVEEYNR 

      1030       1040       1050       1060       1070       1080 
THKWSKRGMA IIPTKFGISF TALFLNQAGA LVHIYHDGSV LVAHGGVEMG QGLHTKMTMI 

      1090       1100       1110       1120       1130       1140 
AAEALGVPLS DVFISETATN TVANTSSTAA SASSDLNGYA IYNACTQLNE RLKPYREKMP 

      1150       1160       1170       1180       1190       1200 
NATLKDLAHA AYFDRVNLSA QGYYRTPDIG YTWGENKGQM FFYFTQGVTA AEVEIDTLTG 

      1210       1220       1230       1240       1250       1260 
DWTPLRADIK MDVGRTINPS IDYGQIEGAY IQGQGLFTTE ESLWHRTTGQ IFTKGPGNYK 

      1270       1280       1290       1300       1310       1320 
IPGFRDIPQI FNVSLLKDVE WENLRTIQRS RGVGEPPLFM GSAAFFAIRD ALKAARKEWG 

      1330       1340       1350       1360 
VTDVLSLVSP ATPERIRVSC ADPIIERARV KAEEGEKSFF VAI
Q12553 in FASTA format

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