Reviewed, UniProtKB/Swiss-Prot Q12553 (XDH_EMENI)

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)

Taxonomic identifier

162425 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	1363 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	Xanthine + NAD+ + H2O = urate + NADH. Hypoxanthine + NAD+ + H2O = xanthine + NADH.
Cofactor	Binds 2 2Fe-2S clusters. FAD. Molybdopterin.
Subcellular location	Peroxisome.
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.

Ontologies

Keywords
Cellular component	Peroxisome
Ligand	2Fe-2S FAD Flavoprotein Iron Iron-sulfur Metal-binding Molybdenum NAD
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW FAD binding Inferred from electronic annotation. Source: InterPro 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 xanthine dehydrogenase activity Inferred from electronic annotation. Source: EC xanthine oxidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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
Sites
	Metal binding	73	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	78	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	81	1	Iron-sulfur (2Fe-2S) By similarity
Experimental info
	Sequence conflict	741	1	R → H in CAA58034. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q12553-1 [UniParc]. Last modified May 1, 2007. Version 2. Checksum: 18D8F50B731EDE4B	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

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]. 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. , 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. Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC 4.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X82827 Genomic DNA. Translation: CAA58034.1. AACD01000098 Genomic DNA. Translation: EAA62706.1.
PIR	A55875.
RefSeq	XP_663217.1.
3D structure databases
HSSP	HSSP built from PDB template 1FO4 based on UniProtKB P80457.
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. IPR000572. OxRdtase_Mopterin-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.
ProDom	PD186071. 2Fe-2S_bind. 1 hit. [Graphical view] [Entries sharing at least one domain]
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...

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:	June 16, 2009
This is version 66 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)