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P10351

- XDH_DROME

UniProt

P10351 - XDH_DROME

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Protein

Xanthine dehydrogenase

Gene
ry, XDH, CG7642
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - 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.1 Publication

Catalytic activityi

Xanthine + NAD+ + H2O = urate + NADH.
Hypoxanthine + NAD+ + H2O = xanthine + NADH.

Cofactori

Binds 2 2Fe-2S clusters By similarity.
FAD By similarity.
Binds 1 molybdenum-molybdopterin (Mo-MPT) cofactor per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi43 – 431Iron-sulfur 1 By similarity
Metal bindingi48 – 481Iron-sulfur 1 By similarity
Metal bindingi51 – 511Iron-sulfur 1 By similarity
Metal bindingi73 – 731Iron-sulfur 1 By similarity
Metal bindingi113 – 1131Iron-sulfur 2 By similarity
Metal bindingi116 – 1161Iron-sulfur 2 By similarity
Metal bindingi148 – 1481Iron-sulfur 2 By similarity
Metal bindingi150 – 1501Iron-sulfur 2 By similarity
Binding sitei335 – 3351FAD By similarity
Binding sitei358 – 3581FAD By similarity
Binding sitei406 – 4061FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding sitei424 – 4241FAD By similarity
Metal bindingi772 – 7721Molybdenum By similarity
Metal bindingi803 – 8031Molybdenum; via carbonyl oxygen By similarity
Binding sitei807 – 8071Substrate By similarity
Binding sitei885 – 8851Substrate By similarity
Metal bindingi917 – 9171Molybdenum; via amide nitrogen By similarity
Binding sitei919 – 9191Substrate By similarity
Metal bindingi1084 – 10841Molybdenum; via amide nitrogen By similarity
Active sitei1267 – 12671Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi255 – 2628FAD By similarity
Nucleotide bindingi345 – 3495FAD By similarity

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB
  2. electron carrier activity Source: InterPro
  3. flavin adenine dinucleotide binding Source: UniProtKB
  4. iron ion binding Source: InterPro
  5. molybdopterin cofactor binding Source: UniProtKB
  6. UDP-N-acetylmuramate dehydrogenase activity Source: InterPro
  7. xanthine dehydrogenase activity Source: UniProtKB
  8. xanthine oxidase activity Source: InterPro

GO - Biological processi

  1. arginine metabolic process Source: FlyBase
  2. compound eye pigmentation Source: FlyBase
  3. determination of adult lifespan Source: FlyBase
  4. glycerophospholipid metabolic process Source: FlyBase
  5. purine nucleobase metabolic process Source: FlyBase
  6. pyrimidine nucleobase metabolic process Source: FlyBase
  7. tryptophan metabolic process Source: FlyBase
  8. 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

ReactomeiREACT_180681. Vitamins B6 activation to pyridoxal phosphate.
REACT_207989. Purine catabolism.

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
ProteomesiUP000000803: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0003308. ry.

Subcellular locationi

Peroxisome By similarity

GO - Cellular componenti

  1. microtubule associated complex Source: FlyBase
  2. peroxisome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13351335Xanthine dehydrogenasePRO_0000166079Add
BLAST

Proteomic databases

PaxDbiP10351.

Expressioni

Gene expression databases

BgeeiP10351.

Interactioni

Subunit structurei

Homodimer By similarity.

Protein-protein interaction databases

IntActiP10351. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP10351.
SMRiP10351. Positions 6-165, 193-529, 573-1317.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 91882Fe-2S ferredoxin-typeAdd
BLAST
Domaini227 – 416190FAD-binding PCMH-typeAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG4630.
GeneTreeiENSGT00390000003772.
InParanoidiP10351.
KOiK00106.
OMAiFHMENSY.
OrthoDBiEOG7QRQSZ.
PhylomeDBiP10351.

Family and domain databases

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

MSNSVLVFFV NGKKVTEVSP DPECTLLTFL REKLRLCGTK LGCAEGGCGA     50
CTVMVSRLDR RANKIRHLAV NACLTPVCSM HGCAVTTVEG IGSTKTRLHP 100
VQERLAKAHG SQCGFCTPGI VMSMYALLRN AEQPSMRDLE VAFQGNLCRC 150
TGYRPILEGY KTFTKEFACG MGEKCCKVSG KGCGTDAETD DKLFERSEFQ 200
PLDPSQEPIF PPELQLSDAF DSQSLIFSSD RVTWYRPTNL EELLQLKAKH 250
PAAKLVVGNT EVGVEVKFKH FLYPHLINPT QVKELLEIKE NQDGIYFGAA 300
VSLMEIDALL RQRIEQLPES ETRLFQCTVD MLHYFAGKQI RNVACLGGNI 350
MTGSPISDMN PVLSAAGAQL EVASFVDGKL QKRSVHMGTG FFTGYRRNVI 400
EAHEVLLGIH FRKTTPDQYI VAFKQARRRD DDIAIVNAAI NVRFEEKSNI 450
VAEISMAFGG MAPTTVLAPR TSQLMVGQEW SHQLVERVAE SLCTELPLAA 500
SAPGGMIAYR RALVVSLFFK AYLAISLKLS KSGITSSDAL PSEERSGAET 550
FHTPVLKSAQ LFERVCSDQP ICDPIGRPKV HAAALKQATG EAIYTDDIPR 600
MDGEVYLAFV LSTKPRAKIT KLDASEALAL DGVHQFFCYK DLTEHENEVG 650
PVFHDEHVFA AGEVHCYGQI VGAIAADNKA LAQRAARLVK VEYEELSPVI 700
VTIEQAIEHK SYFPDYPRFV TKGNVEEALA QADHTFEGTC RMGGQEHFYL 750
ETHAALAVPR DSDELELFCS TQHPSEVQKL VAHVTALPAH RVVCRAKRLG 800
GGFGGKESRG ISVALPVALA AYRMGRPVRC MLDRDEDMLI TGTRHPFLFK 850
YKVGFTKEGL ITACDIECYN NAGWSMDLSF SVLERAMFHF ENCYRIPNVR 900
VGGWVCKTNL PSNTAFRGFG GPQGMYAGEH IIRDVARIVG RDVVDVMRLN 950
FYKTGDYTHY HQQLEHFPIE RCLEDCLKQS RYDEKRQEIA RFNRENRWRK 1000
RGMAVVPTKY GIAFGVMHLN QAGSLINIYG DGSVLLSHGG VEIGQGLNTK 1050
MIQCAARALG IPSELIHISE TATDKVPNTS PTAASVGSDL NGMAVLDACE 1100
KLNKRLAPIK EALPGGTWKE WINKAYFDRV SLSATGFYAM PGIGYHPETN 1150
PNARTYSYYT NGVGVTVVEI DCLTGDHQVL STDIVMDIGS SLNPAIDIGQ 1200
IEGAFMQGYG LFTLEELMYS PQGMLYSRGP GMYKLPGFAD IPGEFNVSLL 1250
TGAPNPRAVY SSKAVGEPPL FIGSSAFFAI KEAIAAARED QGLSGDFPLE 1300
APSTSARIRI ACQDKFTELL EIPEPGSFTP WNIVP 1335
Length:1,335
Mass (Da):146,927
Last modified:June 20, 2003 - v2
Checksum:i230368EA59B30AD8
GO

Sequence cautioni

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti106 – 1061A → P in CAA68409. 1 Publication
Sequence conflicti106 – 1061A → P no nucleotide entry 1 Publication
Sequence conflicti316 – 3161Q → L in CAA68409. 1 Publication
Sequence conflicti316 – 3161Q → L no nucleotide entry 1 Publication
Sequence conflicti542 – 5421S → P in CAA68409. 1 Publication
Sequence conflicti542 – 5421S → P no nucleotide entry 1 Publication
Sequence conflicti709 – 7091H → L in CAA68409. 1 Publication
Sequence conflicti709 – 7091H → L no nucleotide entry 1 Publication
Sequence conflicti730 – 7301A → S in CAA68409. 1 Publication
Sequence conflicti730 – 7301A → S no nucleotide entry 1 Publication
Sequence conflicti988 – 9881E → D in CAA68409. 1 Publication
Sequence conflicti988 – 9881E → D no nucleotide entry 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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.
PIRi S07245.
RefSeqi NP_524337.1. NM_079613.3.
UniGenei Dm.2436.

3D structure databases

ProteinModelPortali P10351.
SMRi P10351. Positions 6-165, 193-529, 573-1317.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P10351. 1 interaction.

Proteomic databases

PaxDbi P10351.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0082704 ; FBpp0082172 ; FBgn0003308 .
GeneIDi 41605.
KEGGi dme:Dmel_CG7642.

Organism-specific databases

CTDi 41605.
FlyBasei FBgn0003308. ry.

Phylogenomic databases

eggNOGi COG4630.
GeneTreei ENSGT00390000003772.
InParanoidi P10351.
KOi K00106.
OMAi FHMENSY.
OrthoDBi EOG7QRQSZ.
PhylomeDBi P10351.

Enzyme and pathway databases

Reactomei REACT_180681. Vitamins B6 activation to pyridoxal phosphate.
REACT_207989. Purine catabolism.

Miscellaneous databases

GenomeRNAii 41605.
NextBioi 824612.
PROi P10351.

Gene expression databases

Bgeei P10351.

Family and domain databases

Gene3Di 1.10.150.120. 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.
InterProi IPR002888. 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 ]
Pfami 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 ]
PIRSFi PIRSF000127. Xanthine_DH. 1 hit.
SMARTi SM01008. Ald_Xan_dh_C. 1 hit.
SM01092. CO_deh_flav_C. 1 hit.
[Graphical view ]
SUPFAMi SSF47741. SSF47741. 1 hit.
SSF54292. SSF54292. 1 hit.
SSF54665. SSF54665. 1 hit.
SSF55447. SSF55447. 1 hit.
SSF56003. SSF56003. 1 hit.
SSF56176. SSF56176. 1 hit.
TIGRFAMsi TIGR02963. xanthine_xdhA. 1 hit.
PROSITEi PS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 544-1335.
    Strain: Berkeley.
    Tissue: Head.

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: September 3, 2014
This is version 142 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

External Data

Dasty 3

Similar proteinsi