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P10351 (XDH_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Xanthine dehydrogenase

Short name=XD
EC=1.17.1.4
Alternative name(s):
Protein rosy locus
Gene names
Name:ry
Synonyms:XDH
ORF Names:CG7642
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length1335 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

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. Ref.5

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-molybdopterin (Mo-MPT) cofactor per subunit By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Peroxisome By similarity.

Sequence similarities

Belongs to the xanthine dehydrogenase family.

Contains 1 2Fe-2S ferredoxin-type domain.

Contains 1 FAD-binding PCMH-type domain.

Sequence caution

The sequence AAM11042.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentPeroxisome
   Ligand2Fe-2S
FAD
Flavoprotein
Iron
Iron-sulfur
Metal-binding
Molybdenum
NAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processarginine metabolic process

Inferred from mutant phenotype PubMed 18657538. Source: FlyBase

compound eye pigmentation

Traceable author statement PubMed 1783294. Source: FlyBase

determination of adult lifespan

Inferred from mutant phenotype PubMed 17435236. Source: FlyBase

glycerophospholipid metabolic process

Inferred from mutant phenotype PubMed 18657538. Source: FlyBase

purine nucleobase metabolic process

Inferred from mutant phenotype PubMed 18657538. Source: FlyBase

pyrimidine nucleobase metabolic process

Inferred from mutant phenotype PubMed 18657538. Source: FlyBase

tryptophan metabolic process

Inferred from mutant phenotype PubMed 18657538. Source: FlyBase

xanthine catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentmicrotubule associated complex

Inferred from direct assay PubMed 18433294. Source: FlyBase

peroxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function2 iron, 2 sulfur cluster binding

Inferred from sequence or structural similarity. Source: UniProtKB

UDP-N-acetylmuramate dehydrogenase activity

Inferred from electronic annotation. Source: InterPro

electron carrier activity

Inferred from electronic annotation. Source: InterPro

flavin adenine dinucleotide binding

Inferred from sequence or structural similarity. Source: UniProtKB

iron ion binding

Inferred from electronic annotation. Source: InterPro

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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13351335Xanthine dehydrogenase
PRO_0000166079

Regions

Domain4 – 91882Fe-2S ferredoxin-type
Domain227 – 416190FAD-binding PCMH-type
Nucleotide binding255 – 2628FAD By similarity
Nucleotide binding345 – 3495FAD By similarity

Sites

Active site12671Proton acceptor By similarity
Metal binding431Iron-sulfur 1 By similarity
Metal binding481Iron-sulfur 1 By similarity
Metal binding511Iron-sulfur 1 By similarity
Metal binding731Iron-sulfur 1 By similarity
Metal binding1131Iron-sulfur 2 By similarity
Metal binding1161Iron-sulfur 2 By similarity
Metal binding1481Iron-sulfur 2 By similarity
Metal binding1501Iron-sulfur 2 By similarity
Metal binding7721Molybdenum By similarity
Metal binding8031Molybdenum; via carbonyl oxygen By similarity
Metal binding9171Molybdenum; via amide nitrogen By similarity
Metal binding10841Molybdenum; via amide nitrogen By similarity
Binding site3351FAD By similarity
Binding site3581FAD By similarity
Binding site4061FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site4241FAD By similarity
Binding site8071Substrate By similarity
Binding site8851Substrate By similarity
Binding site9191Substrate By similarity

Experimental info

Sequence conflict1061A → P in CAA68409. Ref.1
Sequence conflict1061A → P no nucleotide entry Ref.5
Sequence conflict3161Q → L in CAA68409. Ref.1
Sequence conflict3161Q → L no nucleotide entry Ref.6
Sequence conflict5421S → P in CAA68409. Ref.1
Sequence conflict5421S → P no nucleotide entry Ref.6
Sequence conflict7091H → L in CAA68409. Ref.1
Sequence conflict7091H → L no nucleotide entry Ref.6
Sequence conflict7301A → S in CAA68409. Ref.1
Sequence conflict7301A → S no nucleotide entry Ref.6
Sequence conflict9881E → D in CAA68409. Ref.1
Sequence conflict9881E → D no nucleotide entry Ref.6

Sequences

Sequence LengthMass (Da)Tools
P10351 [UniParc].

Last modified June 20, 2003. Version 2.
Checksum: 230368EA59B30AD8

FASTA1,335146,927
        10         20         30         40         50         60 
MSNSVLVFFV NGKKVTEVSP DPECTLLTFL REKLRLCGTK LGCAEGGCGA CTVMVSRLDR 

        70         80         90        100        110        120 
RANKIRHLAV NACLTPVCSM HGCAVTTVEG IGSTKTRLHP VQERLAKAHG SQCGFCTPGI 

       130        140        150        160        170        180 
VMSMYALLRN AEQPSMRDLE VAFQGNLCRC TGYRPILEGY KTFTKEFACG MGEKCCKVSG 

       190        200        210        220        230        240 
KGCGTDAETD DKLFERSEFQ PLDPSQEPIF PPELQLSDAF DSQSLIFSSD RVTWYRPTNL 

       250        260        270        280        290        300 
EELLQLKAKH PAAKLVVGNT EVGVEVKFKH FLYPHLINPT QVKELLEIKE NQDGIYFGAA 

       310        320        330        340        350        360 
VSLMEIDALL RQRIEQLPES ETRLFQCTVD MLHYFAGKQI RNVACLGGNI MTGSPISDMN 

       370        380        390        400        410        420 
PVLSAAGAQL EVASFVDGKL QKRSVHMGTG FFTGYRRNVI EAHEVLLGIH FRKTTPDQYI 

       430        440        450        460        470        480 
VAFKQARRRD DDIAIVNAAI NVRFEEKSNI VAEISMAFGG MAPTTVLAPR TSQLMVGQEW 

       490        500        510        520        530        540 
SHQLVERVAE SLCTELPLAA SAPGGMIAYR RALVVSLFFK AYLAISLKLS KSGITSSDAL 

       550        560        570        580        590        600 
PSEERSGAET FHTPVLKSAQ LFERVCSDQP ICDPIGRPKV HAAALKQATG EAIYTDDIPR 

       610        620        630        640        650        660 
MDGEVYLAFV LSTKPRAKIT KLDASEALAL DGVHQFFCYK DLTEHENEVG PVFHDEHVFA 

       670        680        690        700        710        720 
AGEVHCYGQI VGAIAADNKA LAQRAARLVK VEYEELSPVI VTIEQAIEHK SYFPDYPRFV 

       730        740        750        760        770        780 
TKGNVEEALA QADHTFEGTC RMGGQEHFYL ETHAALAVPR DSDELELFCS TQHPSEVQKL 

       790        800        810        820        830        840 
VAHVTALPAH RVVCRAKRLG GGFGGKESRG ISVALPVALA AYRMGRPVRC MLDRDEDMLI 

       850        860        870        880        890        900 
TGTRHPFLFK YKVGFTKEGL ITACDIECYN NAGWSMDLSF SVLERAMFHF ENCYRIPNVR 

       910        920        930        940        950        960 
VGGWVCKTNL PSNTAFRGFG GPQGMYAGEH IIRDVARIVG RDVVDVMRLN FYKTGDYTHY 

       970        980        990       1000       1010       1020 
HQQLEHFPIE RCLEDCLKQS RYDEKRQEIA RFNRENRWRK RGMAVVPTKY GIAFGVMHLN 

      1030       1040       1050       1060       1070       1080 
QAGSLINIYG DGSVLLSHGG VEIGQGLNTK MIQCAARALG IPSELIHISE TATDKVPNTS 

      1090       1100       1110       1120       1130       1140 
PTAASVGSDL NGMAVLDACE KLNKRLAPIK EALPGGTWKE WINKAYFDRV SLSATGFYAM 

      1150       1160       1170       1180       1190       1200 
PGIGYHPETN PNARTYSYYT NGVGVTVVEI DCLTGDHQVL STDIVMDIGS SLNPAIDIGQ 

      1210       1220       1230       1240       1250       1260 
IEGAFMQGYG LFTLEELMYS PQGMLYSRGP GMYKLPGFAD IPGEFNVSLL TGAPNPRAVY 

      1270       1280       1290       1300       1310       1320 
SSKAVGEPPL FIGSSAFFAI KEAIAAARED QGLSGDFPLE APSTSARIRI ACQDKFTELL 

      1330 
EIPEPGSFTP WNIVP 

« Hide

References

« Hide 'large scale' references
[1]Riley M.A.
Submitted (FEB-1987) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Canton-S.
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Head.
[5]"Mutations affecting expression of the rosy locus in Drosophila melanogaster."
Lee C.S., Curtis D., Gray M., Bender W.
Genetics 116:55-66(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-231, FUNCTION.
Strain: Canton-S.
[6]"Sequence of the structural gene for xanthine dehydrogenase (rosy locus) in Drosophila melanogaster."
Keith T.P., Riley M.A., Kreitman M., Lewontin R.C., Curtis D., Chambers G.
Genetics 116:67-73(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 199-1335.
Strain: Canton-S.
[7]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 544-1335.
Strain: Berkeley.
Tissue: Head.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00308 Genomic DNA. Translation: CAA68409.1.
AE014297 Genomic DNA. Translation: AAF54895.1.
BT015293 mRNA. Translation: AAT94522.1.
AY094689 mRNA. Translation: AAM11042.1. Different initiation.
PIRS07245.
RefSeqNP_524337.1. NM_079613.3.
UniGeneDm.2436.

3D structure databases

ProteinModelPortalP10351.
SMRP10351. Positions 6-165, 193-529, 573-1317.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP10351. 1 interaction.

Proteomic databases

PaxDbP10351.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0082704; FBpp0082172; FBgn0003308.
GeneID41605.
KEGGdme:Dmel_CG7642.

Organism-specific databases

CTD41605.
FlyBaseFBgn0003308. ry.

Phylogenomic databases

eggNOGCOG4630.
GeneTreeENSGT00390000003772.
InParanoidP10351.
KOK00106.
OMAFHMENSY.
OrthoDBEOG7QRQSZ.
PhylomeDBP10351.

Gene expression databases

BgeeP10351.

Family and domain databases

Gene3D1.10.150.120. 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.
InterProIPR002888. 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]
PfamPF01315. 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]
PIRSFPIRSF000127. Xanthine_DH. 1 hit.
SMARTSM01008. Ald_Xan_dh_C. 1 hit.
SM01092. CO_deh_flav_C. 1 hit.
[Graphical view]
SUPFAMSSF47741. SSF47741. 1 hit.
SSF54292. SSF54292. 1 hit.
SSF54665. SSF54665. 1 hit.
SSF55447. SSF55447. 1 hit.
SSF56003. SSF56003. 1 hit.
SSF56176. SSF56176. 1 hit.
TIGRFAMsTIGR02963. xanthine_xdhA. 1 hit.
PROSITEPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi41605.
NextBio824612.
PROP10351.

Entry information

Entry nameXDH_DROME
AccessionPrimary (citable) accession number: P10351
Secondary accession number(s): Q6AWF5, Q8SXC4, Q9VFZ9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: June 20, 2003
Last modified: July 9, 2014
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

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