Xanthine dehydrogenase - Emericella nidulans

Names and origin

Protein names

Recommended name:
    Xanthine dehydrogenase
    EC=1.17.1.4
Alternative name(s):
    Purine hydroxylase I

Gene names

Name:	hxA
ORF Names:	AN5613

Organism

Emericella nidulans (Aspergillus nidulans) [Complete proteome]

Taxonomic identifier

162425 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

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Protein attributes

Sequence length	1363 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

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General annotation (Comments)

Function	Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid By similarity.
Catalytic activity	Xanthine + NAD⁺ + H₂O = urate + NADH. Hypoxanthine + NAD⁺ + H₂O = xanthine + NADH.
Cofactor	Binds 2 2Fe-2S clusters By similarity. FAD By similarity. Binds 1 molybdenum ion (molybdopterin) per subunit By similarity.
Subcellular location	Peroxisome By similarity.
Induction	By 2-tiouric acid. Repressed by ammonium.
Sequence similarities	Belongs to the xanthine dehydrogenase family. Contains 1 2Fe-2S ferredoxin-type domain. Contains 1 FAD-binding PCMH-type domain.

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Ontologies

Keywords
Cellular component	Peroxisome
Ligand	2Fe-2S FAD Flavoprotein Iron Iron-sulfur Metal-binding Molybdenum NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW xanthine catabolic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	2 iron, 2 sulfur cluster binding Inferred from sequence or structural similarity. Source: UniProtKB FAD binding Inferred from sequence or structural similarity. Source: UniProtKB electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW molybdenum ion binding Inferred from electronic annotation. Source: UniProtKB-KW molybdopterin cofactor binding Inferred from sequence or structural similarity. Source: UniProtKB xanthine dehydrogenase activity Inferred from sequence or structural similarity. Source: UniProtKB xanthine oxidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1363

1363

Xanthine dehydrogenase

PRO_0000166087

Regions

Domain

35 – 121

87

2Fe-2S ferredoxin-type

Domain

266 – 450

185

FAD-binding PCMH-type

Nucleotide binding

294 – 301

8

FAD By similarity

Nucleotide binding

384 – 388

5

FAD By similarity

Sites

Active site

1295

1

Proton acceptor By similarity

Metal binding

73

1

Iron-sulfur 1 By similarity

Metal binding

78

1

Iron-sulfur 1 By similarity

Metal binding

81

1

Iron-sulfur 1 By similarity

Metal binding

103

1

Iron-sulfur 1 By similarity

Metal binding

142

1

Iron-sulfur 2 By similarity

Metal binding

145

1

Iron-sulfur 2 By similarity

Metal binding

177

1

Iron-sulfur 2 By similarity

Metal binding

179

1

Iron-sulfur 2 By similarity

Metal binding

798

1

Molybdenum By similarity

Metal binding

829

1

Molybdenum; via carbonyl oxygen By similarity

Metal binding

943

1

Molybdenum; via amide nitrogen By similarity

Metal binding

1110

1

Molybdenum; via amide nitrogen By similarity

Binding site

374

1

FAD By similarity

Binding site

397

1

FAD By similarity

Binding site

459

1

FAD By similarity

Binding site

833

1

Substrate By similarity

Binding site

911

1

Substrate By similarity

Binding site

945

1

Substrate By similarity

Binding site

1041

1

Substrate; via amide nitrogen By similarity

Experimental info

Sequence conflict

741

1

R → H in CAA58034. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

Q12553-1 [UniParc].

Last modified May 1, 2007. Version 2.
Checksum: 18D8F50B731EDE4B
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FASTA

1,363

149,523

        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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 7876088] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION. Strain: biA1.
[2]	"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." 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. Birren B.W. Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC A4 / M139.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	X82827 Genomic DNA. Translation: CAA58034.1. AACD01000098 Genomic DNA. Translation: EAA62706.1.
PIR	A55875.
RefSeq	XP_663217.1.
3D structure databases
SMR	Q12553. Positions 35-193, 601-1339.
ModBase	Search...
Genome annotation databases
GeneID	2871900.
KEGG	ani:AN5613.2.
Enzyme and pathway databases
BRENDA	1.17.1.4. 3859.
Family and domain databases
InterPro	IPR002888. 2Fe-2S_bd. IPR006058. 2Fe2S_fd_BS. IPR000674. Ald_Oxase/Xan_DH_a/b. IPR016208. Ald_Oxase/xanthine_DH. IPR008274. AldOxase/xan_DH_Mopterin-bd. IPR005107. CO_DH_flav_C. IPR016169. CO_DH_flavot_FAD-bd_sub2. IPR016166. FAD-bd_2. IPR016167. FAD-bd_2_sub1. IPR001041. Ferredoxin. IPR002346. Mopterin_DH_FAD-bd. IPR014307. Xanthine_DH_ssu. [Graphical view]
Gene3D	G3DSA:3.30.365.10. Ald_xan_DH_mo_bd. 2 hits. G3DSA:3.90.1170.50. Aldxan_DH_hamm. 1 hit. G3DSA:3.30.390.50. CO_DH_flav_C. 1 hit. G3DSA:3.30.465.10. CO_DH_flavoprot_FAD-bd_sub2. 1 hit. G3DSA:3.30.43.10. FAD-binding_2_sub1. 1 hit.
Pfam	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]
PIRSF	PIRSF000127. Xanthine_DH. 1 hit.
TIGRFAMs	TIGR02963. xanthine_xdhA. 1 hit.
PROSITE	PS00197. 2FE2S_FER_1. 1 hit. PS51085. 2FE2S_FER_2. 1 hit. PS51387. FAD_PCMH. 1 hit. PS00559. MOLYBDOPTERIN_EUK. False negative. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

XDH_EMENI

Accession

Primary (citable) accession number: Q12553
Secondary accession number(s): Q5B1G7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 1, 2007
Last modified:	February 9, 2010
This is version 71 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents