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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: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

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

Protein has several cofactor binding sites:
  • [2Fe-2S] clusterBy similarityNote: Binds 2 [2Fe-2S] clusters.By similarity
  • FADBy similarity
  • Mo-molybdopterinBy similarityNote: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi73Iron-sulfur 1By similarity1
Metal bindingi78Iron-sulfur 1By similarity1
Metal bindingi81Iron-sulfur 1By similarity1
Metal bindingi103Iron-sulfur 1By similarity1
Metal bindingi142Iron-sulfur 2By similarity1
Metal bindingi145Iron-sulfur 2By similarity1
Metal bindingi177Iron-sulfur 2By similarity1
Metal bindingi179Iron-sulfur 2By similarity1
Binding sitei374FADBy similarity1
Binding sitei397FADBy similarity1
Binding sitei459FADBy similarity1
Metal bindingi798MolybdenumBy similarity1
Metal bindingi829Molybdenum; via carbonyl oxygenBy similarity1
Binding sitei833SubstrateBy similarity1
Binding sitei911SubstrateBy similarity1
Metal bindingi943Molybdenum; via amide nitrogenBy similarity1
Binding sitei945SubstrateBy similarity1
Binding sitei1041Substrate; via amide nitrogenBy similarity1
Metal bindingi1110Molybdenum; via amide nitrogenBy similarity1
Active sitei1295Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi294 – 301FADBy similarity8
Nucleotide bindingi384 – 388FADBy similarity5

GO - Molecular functioni

GO - Biological processi

  • purine nucleobase catabolic process Source: ASPGD
  • xanthine catabolic process Source: UniProtKB
Complete GO annotation...

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
Proteomesi
  • UP000000560 Componenti: Chromosome V
  • UP000005890 Componenti: Partially assembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001660871 – 1363Xanthine dehydrogenaseAdd BLAST1363

Expressioni

Inductioni

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

Structurei

3D structure databases

ProteinModelPortaliQ12553.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini35 – 1212Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST87
Domaini266 – 450FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST185

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

HOGENOMiHOG000191197.
InParanoidiQ12553.
KOiK00106.
OMAiYITPDIN.
OrthoDBiEOG092C04XY.

Family and domain databases

CDDicd00207. fer2. 1 hit.
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

        10         20         30         40         50
MAPGVLLQPS QSELEAASPP KAAASLLQLT EEWDDTIRFY LNGTKVILDS
60 70 80 90 100
VDPEITLLEY LRGIGLTGTK LGCAEGGCGA CTVVVSQINP TTKKLYHASI
110 120 130 140 150
NACIAPLVAV DGKHVITVEG IGNVKNPHAI QQRLAIGNGS QCGFCTPGIV
160 170 180 190 200
MSLYALLRND PKPSEHAVEE AFDGNLCRCT GYRPILDAAQ SFTSPIGCGK
210 220 230 240 250
ARANGGSGCC MEEQKGTNGC CKGSSEETTE DVKHKFASPD FIEYKPDTEL
260 270 280 290 300
IFPPSLWKHE LRPLAFGNKR KKWYRPVTVQ QLLEIKSIHP DAKLIGGSTE
310 320 330 340 350
TQIEIKFKQM RYGASVYLGD LAELRQFAFH DNYLEIGANI SLTDLESVCD
360 370 380 390 400
QAIERYGSAR GQPFAAIKKQ LRYFAGRQIR NVASPAGNLA TASPISDLNP
410 420 430 440 450
VFVATNTTLV ARSLDKETEI PMTQFFRGYR STALPPDAII SSLRIPTASE
460 470 480 490 500
KGEYLRAYKQ SKRKDDDIAI VNAALRVSLS SSNDVTSVSL VFGGMAPLTV
510 520 530 540 550
SARNAEAFLT GKKFTDPATL EGTMGALEQD FNLKFGVPGG MATYRKSLAL
560 570 580 590 600
GFFYRFYHDV LSQIEARSSD LDNSVVAEIE RAISTGEKDN EASAAYQQRV
610 620 630 640 650
LGRAGPHLSA LKQATGEAQY TDDIPAQKNE LYGCMVLSTK AHAKLLSVNT
660 670 680 690 700
EAALEIPGVI DYVDHKDLPS PRANWWGAPN CDEVFFAVDK VTTAGQPIGM
710 720 730 740 750
ILANTAKAAE EGARAVKVEY EELPVILSIE EAIEAQSFFE RFRYIKNGDP
760 770 780 790 800
ESAFRDADHV FEGVSRMGGQ EHFYLETQAC VAIPKAEDGE MEIWSSTQNP
810 820 830 840 850
TETQSYVAQV TGVAANKIVS RVKRLGGGFG GKETRSVQLA GICATAAAKV
860 870 880 890 900
RRPVRCMLNR DEDIATSGQR HPFYCKWKVG VTREGKLLAL DADVYANGGH
910 920 930 940 950
TQDLSGAVVE RSLSHIDNVY RFPNIYVRGR ICKTNTVSNT AFRGFGGPQG
960 970 980 990 1000
LFFAESIISE VADHLDLQVE QLRILNMYEP GDMTHFNQEL KDWHVPLMYD
1010 1020 1030 1040 1050
QVLQESEYFE RRKAVEEYNR THKWSKRGMA IIPTKFGISF TALFLNQAGA
1060 1070 1080 1090 1100
LVHIYHDGSV LVAHGGVEMG QGLHTKMTMI AAEALGVPLS DVFISETATN
1110 1120 1130 1140 1150
TVANTSSTAA SASSDLNGYA IYNACTQLNE RLKPYREKMP NATLKDLAHA
1160 1170 1180 1190 1200
AYFDRVNLSA QGYYRTPDIG YTWGENKGQM FFYFTQGVTA AEVEIDTLTG
1210 1220 1230 1240 1250
DWTPLRADIK MDVGRTINPS IDYGQIEGAY IQGQGLFTTE ESLWHRTTGQ
1260 1270 1280 1290 1300
IFTKGPGNYK IPGFRDIPQI FNVSLLKDVE WENLRTIQRS RGVGEPPLFM
1310 1320 1330 1340 1350
GSAAFFAIRD ALKAARKEWG VTDVLSLVSP ATPERIRVSC ADPIIERARV
1360
KAEEGEKSFF VAI
Length:1,363
Mass (Da):149,523
Last modified:May 1, 2007 - v2
Checksum:i18D8F50B731EDE4B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti741R → H in CAA58034 (PubMed:7876088).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
EAA62706; EAA62706; AN5613.2.
GeneIDi2871900.
KEGGiani:AN5613.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ12553.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00003457; CADANIAP00003457; CADANIAG00003457.
EAA62706; EAA62706; AN5613.2.
GeneIDi2871900.
KEGGiani:AN5613.2.

Phylogenomic databases

HOGENOMiHOG000191197.
InParanoidiQ12553.
KOiK00106.
OMAiYITPDIN.
OrthoDBiEOG092C04XY.

Family and domain databases

CDDicd00207. fer2. 1 hit.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 120 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.