P10351 (XDH_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	1335 AA.
Sequence status	Complete.
Protein existence	Evidence 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 ion (molybdopterin) 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 component	Peroxisome
Ligand	2Fe-2S FAD Flavoprotein Iron Iron-sulfur Metal-binding Molybdenum NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	arginine 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 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_component	microtubule associated complex Inferred from direct assay PubMed 18433294. Source: FlyBase peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	2 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1335	1335	Xanthine dehydrogenase		PRO_0000166079
Regions
	Domain	4 – 91	88	2Fe-2S ferredoxin-type
	Domain	227 – 416	190	FAD-binding PCMH-type
	Nucleotide binding	255 – 262	8	FAD By similarity
	Nucleotide binding	345 – 349	5	FAD By similarity
Sites
	Active site	1267	1	Proton acceptor By similarity
	Metal binding	43	1	Iron-sulfur 1 By similarity
	Metal binding	48	1	Iron-sulfur 1 By similarity
	Metal binding	51	1	Iron-sulfur 1 By similarity
	Metal binding	73	1	Iron-sulfur 1 By similarity
	Metal binding	113	1	Iron-sulfur 2 By similarity
	Metal binding	116	1	Iron-sulfur 2 By similarity
	Metal binding	148	1	Iron-sulfur 2 By similarity
	Metal binding	150	1	Iron-sulfur 2 By similarity
	Metal binding	772	1	Molybdenum By similarity
	Metal binding	803	1	Molybdenum; via carbonyl oxygen By similarity
	Metal binding	917	1	Molybdenum; via amide nitrogen By similarity
	Metal binding	1084	1	Molybdenum; via amide nitrogen By similarity
	Binding site	335	1	FAD By similarity
	Binding site	358	1	FAD By similarity
	Binding site	406	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	424	1	FAD By similarity
	Binding site	807	1	Substrate By similarity
	Binding site	885	1	Substrate By similarity
	Binding site	919	1	Substrate By similarity
Experimental info
	Sequence conflict	106	1	A → P in CAA68409. Ref.1
	Sequence conflict	106	1	A → P no nucleotide entry Ref.5
	Sequence conflict	316	1	Q → L in CAA68409. Ref.1
	Sequence conflict	316	1	Q → L no nucleotide entry Ref.6
	Sequence conflict	542	1	S → P in CAA68409. Ref.1
	Sequence conflict	542	1	S → P no nucleotide entry Ref.6
	Sequence conflict	709	1	H → L in CAA68409. Ref.1
	Sequence conflict	709	1	H → L no nucleotide entry Ref.6
	Sequence conflict	730	1	A → S in CAA68409. Ref.1
	Sequence conflict	730	1	A → S no nucleotide entry Ref.6
	Sequence conflict	988	1	E → D in CAA68409. Ref.1
	Sequence conflict	988	1	E → D no nucleotide entry Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P10351 [UniParc]. Last modified June 20, 2003. Version 2. Checksum: 230368EA59B30AD8	FASTA	1,335	146,927
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
PIR	S07245.
RefSeq	NP_524337.1. NM_079613.3.
UniGene	Dm.2436.
3D structure databases
ProteinModelPortal	P10351.
SMR	P10351. Positions 6-165, 193-529, 573-1317.
ModBase	Search...
Protein-protein interaction databases
IntAct	P10351. 1 interaction.
Proteomic databases
PaxDb	P10351.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0082704; FBpp0082172; FBgn0003308.
GeneID	41605.
KEGG	dme:Dmel_CG7642.
Organism-specific databases
CTD	41605.
FlyBase	FBgn0003308. ry.
Phylogenomic databases
eggNOG	COG4630.
GeneTree	ENSGT00390000003772.
InParanoid	P10351.
KO	K00106.
OMA	FKNMLFP.
OrthoDB	EOG418937.
PhylomeDB	P10351.
Gene expression databases
Bgee	P10351.
GermOnline	CG7642. Drosophila melanogaster.
Family and domain databases
Gene3D	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.
InterPro	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]
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.
SMART	SM01008. Ald_Xan_dh_C. 1 hit. SM01092. CO_deh_flav_C. 1 hit. [Graphical view]
SUPFAM	SSF47741. 2Fe-2S_bind. 1 hit. SSF56003. Ald_xan_DH_mo_bd. 1 hit. SSF54665. Aldxan_dh_hamm. 1 hit. SSF55447. CO_deh_flav_C. 1 hit. SSF56176. FAD-binding_2. 1 hit. SSF54292. Ferredoxin. 1 hit.
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. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	41605.
NextBio	824612.

Entry information

Entry name

XDH_DROME

Accession

Primary (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:	May 1, 2013
This is version 133 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project