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Protein

Xanthine dehydrogenase

Gene

ry

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 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 similarity1 Publication

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 bindingi43Iron-sulfur 1By similarity1
Metal bindingi48Iron-sulfur 1By similarity1
Metal bindingi51Iron-sulfur 1By similarity1
Metal bindingi73Iron-sulfur 1By similarity1
Metal bindingi113Iron-sulfur 2By similarity1
Metal bindingi116Iron-sulfur 2By similarity1
Metal bindingi148Iron-sulfur 2By similarity1
Metal bindingi150Iron-sulfur 2By similarity1
Binding sitei335FADBy similarity1
Binding sitei358FADBy similarity1
Binding sitei406FAD; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei424FADBy similarity1
Metal bindingi772MolybdenumBy similarity1
Metal bindingi803Molybdenum; via carbonyl oxygenBy similarity1
Binding sitei807SubstrateBy similarity1
Binding sitei885SubstrateBy similarity1
Metal bindingi917Molybdenum; via amide nitrogenBy similarity1
Binding sitei919SubstrateBy similarity1
Metal bindingi1084Molybdenum; via amide nitrogenBy similarity1
Active sitei1267Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi255 – 262FADBy similarity8
Nucleotide bindingi345 – 349FADBy similarity5

GO - Molecular functioni

GO - Biological processi

  • arginine metabolic process Source: FlyBase
  • compound eye pigmentation Source: FlyBase
  • determination of adult lifespan Source: FlyBase
  • glycerophospholipid metabolic process Source: FlyBase
  • purine nucleobase metabolic process Source: FlyBase
  • pyrimidine nucleobase metabolic process Source: FlyBase
  • response to ethanol Source: FlyBase
  • tryptophan metabolic process Source: FlyBase
  • 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

Enzyme and pathway databases

ReactomeiR-DME-74259. Purine catabolism.
R-DME-964975. Vitamins B6 activation to pyridoxal phosphate.

Names & Taxonomyi

Protein namesi
Recommended name:
Xanthine dehydrogenase (EC:1.17.1.4)
Short name:
XD
Alternative name(s):
Protein rosy locus
Gene namesi
Name:ry
Synonyms:XDH
ORF Names:CG7642
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0003308. ry.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: GO_Central
  • microtubule associated complex Source: FlyBase
  • peroxisome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001660791 – 1335Xanthine dehydrogenaseAdd BLAST1335

Proteomic databases

PaxDbiP10351.
PRIDEiP10351.

Expressioni

Gene expression databases

BgeeiFBgn0003308.
GenevisibleiP10351. DM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi66692. 1 interactor.
IntActiP10351. 4 interactors.
STRINGi7227.FBpp0082172.

Structurei

3D structure databases

ProteinModelPortaliP10351.
SMRiP10351.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini4 – 912Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST88
Domaini227 – 416FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST190

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

eggNOGiKOG0430. Eukaryota.
COG4630. LUCA.
COG4631. LUCA.
GeneTreeiENSGT00390000003772.
InParanoidiP10351.
KOiK00106.
OMAiLAQADHT.
OrthoDBiEOG091G01AW.
PhylomeDBiP10351.

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.
IPR022407. OxRdtase_Mopterin_BS.
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.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P10351-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNSVLVFFV NGKKVTEVSP DPECTLLTFL REKLRLCGTK LGCAEGGCGA
60 70 80 90 100
CTVMVSRLDR RANKIRHLAV NACLTPVCSM HGCAVTTVEG IGSTKTRLHP
110 120 130 140 150
VQERLAKAHG SQCGFCTPGI VMSMYALLRN AEQPSMRDLE VAFQGNLCRC
160 170 180 190 200
TGYRPILEGY KTFTKEFACG MGEKCCKVSG KGCGTDAETD DKLFERSEFQ
210 220 230 240 250
PLDPSQEPIF PPELQLSDAF DSQSLIFSSD RVTWYRPTNL EELLQLKAKH
260 270 280 290 300
PAAKLVVGNT EVGVEVKFKH FLYPHLINPT QVKELLEIKE NQDGIYFGAA
310 320 330 340 350
VSLMEIDALL RQRIEQLPES ETRLFQCTVD MLHYFAGKQI RNVACLGGNI
360 370 380 390 400
MTGSPISDMN PVLSAAGAQL EVASFVDGKL QKRSVHMGTG FFTGYRRNVI
410 420 430 440 450
EAHEVLLGIH FRKTTPDQYI VAFKQARRRD DDIAIVNAAI NVRFEEKSNI
460 470 480 490 500
VAEISMAFGG MAPTTVLAPR TSQLMVGQEW SHQLVERVAE SLCTELPLAA
510 520 530 540 550
SAPGGMIAYR RALVVSLFFK AYLAISLKLS KSGITSSDAL PSEERSGAET
560 570 580 590 600
FHTPVLKSAQ LFERVCSDQP ICDPIGRPKV HAAALKQATG EAIYTDDIPR
610 620 630 640 650
MDGEVYLAFV LSTKPRAKIT KLDASEALAL DGVHQFFCYK DLTEHENEVG
660 670 680 690 700
PVFHDEHVFA AGEVHCYGQI VGAIAADNKA LAQRAARLVK VEYEELSPVI
710 720 730 740 750
VTIEQAIEHK SYFPDYPRFV TKGNVEEALA QADHTFEGTC RMGGQEHFYL
760 770 780 790 800
ETHAALAVPR DSDELELFCS TQHPSEVQKL VAHVTALPAH RVVCRAKRLG
810 820 830 840 850
GGFGGKESRG ISVALPVALA AYRMGRPVRC MLDRDEDMLI TGTRHPFLFK
860 870 880 890 900
YKVGFTKEGL ITACDIECYN NAGWSMDLSF SVLERAMFHF ENCYRIPNVR
910 920 930 940 950
VGGWVCKTNL PSNTAFRGFG GPQGMYAGEH IIRDVARIVG RDVVDVMRLN
960 970 980 990 1000
FYKTGDYTHY HQQLEHFPIE RCLEDCLKQS RYDEKRQEIA RFNRENRWRK
1010 1020 1030 1040 1050
RGMAVVPTKY GIAFGVMHLN QAGSLINIYG DGSVLLSHGG VEIGQGLNTK
1060 1070 1080 1090 1100
MIQCAARALG IPSELIHISE TATDKVPNTS PTAASVGSDL NGMAVLDACE
1110 1120 1130 1140 1150
KLNKRLAPIK EALPGGTWKE WINKAYFDRV SLSATGFYAM PGIGYHPETN
1160 1170 1180 1190 1200
PNARTYSYYT NGVGVTVVEI DCLTGDHQVL STDIVMDIGS SLNPAIDIGQ
1210 1220 1230 1240 1250
IEGAFMQGYG LFTLEELMYS PQGMLYSRGP GMYKLPGFAD IPGEFNVSLL
1260 1270 1280 1290 1300
TGAPNPRAVY SSKAVGEPPL FIGSSAFFAI KEAIAAARED QGLSGDFPLE
1310 1320 1330
APSTSARIRI ACQDKFTELL EIPEPGSFTP WNIVP
Length:1,335
Mass (Da):146,927
Last modified:June 20, 2003 - v2
Checksum:i230368EA59B30AD8
GO

Sequence cautioni

The sequence AAM11042 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti106A → P in CAA68409 (Ref. 1) Curated1
Sequence conflicti106A → P no nucleotide entry (PubMed:3036645).Curated1
Sequence conflicti316Q → L in CAA68409 (Ref. 1) Curated1
Sequence conflicti316Q → L no nucleotide entry (PubMed:3036646).Curated1
Sequence conflicti542S → P in CAA68409 (Ref. 1) Curated1
Sequence conflicti542S → P no nucleotide entry (PubMed:3036646).Curated1
Sequence conflicti709H → L in CAA68409 (Ref. 1) Curated1
Sequence conflicti709H → L no nucleotide entry (PubMed:3036646).Curated1
Sequence conflicti730A → S in CAA68409 (Ref. 1) Curated1
Sequence conflicti730A → S no nucleotide entry (PubMed:3036646).Curated1
Sequence conflicti988E → D in CAA68409 (Ref. 1) Curated1
Sequence conflicti988E → D no nucleotide entry (PubMed:3036646).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00308 Genomic DNA. Translation: CAA68409.1.
AE014297 Genomic DNA. Translation: AAF54895.1.
BT015293 mRNA. Translation: AAT94522.1.
AY094689 mRNA. Translation: AAM11042.1. Different initiation.
PIRiS07245.
RefSeqiNP_524337.1. NM_079613.3.
UniGeneiDm.2436.

Genome annotation databases

EnsemblMetazoaiFBtr0082704; FBpp0082172; FBgn0003308.
GeneIDi41605.
KEGGidme:Dmel_CG7642.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00308 Genomic DNA. Translation: CAA68409.1.
AE014297 Genomic DNA. Translation: AAF54895.1.
BT015293 mRNA. Translation: AAT94522.1.
AY094689 mRNA. Translation: AAM11042.1. Different initiation.
PIRiS07245.
RefSeqiNP_524337.1. NM_079613.3.
UniGeneiDm.2436.

3D structure databases

ProteinModelPortaliP10351.
SMRiP10351.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi66692. 1 interactor.
IntActiP10351. 4 interactors.
STRINGi7227.FBpp0082172.

Proteomic databases

PaxDbiP10351.
PRIDEiP10351.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0082704; FBpp0082172; FBgn0003308.
GeneIDi41605.
KEGGidme:Dmel_CG7642.

Organism-specific databases

CTDi41605.
FlyBaseiFBgn0003308. ry.

Phylogenomic databases

eggNOGiKOG0430. Eukaryota.
COG4630. LUCA.
COG4631. LUCA.
GeneTreeiENSGT00390000003772.
InParanoidiP10351.
KOiK00106.
OMAiLAQADHT.
OrthoDBiEOG091G01AW.
PhylomeDBiP10351.

Enzyme and pathway databases

ReactomeiR-DME-74259. Purine catabolism.
R-DME-964975. Vitamins B6 activation to pyridoxal phosphate.

Miscellaneous databases

GenomeRNAii41605.
PROiP10351.

Gene expression databases

BgeeiFBgn0003308.
GenevisibleiP10351. DM.

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.
IPR022407. OxRdtase_Mopterin_BS.
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.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiXDH_DROME
AccessioniPrimary (citable) accession number: P10351
Secondary accession number(s): Q6AWF5, Q8SXC4, Q9VFZ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: June 20, 2003
Last modified: November 30, 2016
This is version 162 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. 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.