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P47990 (XDH_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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/oxidase

Including the following 2 domains:

  1. Xanthine dehydrogenase
    Short name=XD
    EC=1.17.1.4
  2. Xanthine oxidase
    Short name=XO
    EC=1.17.3.2
    Alternative name(s):
    Xanthine oxidoreductase
    Short name=XOR
Gene names
Name:XDH
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length1358 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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. Contributes to the generation of reactive oxygen species By similarity.

Catalytic activity

Xanthine + NAD+ + H2O = urate + NADH. Ref.1 Ref.2

Hypoxanthine + NAD+ + H2O = xanthine + NADH. Ref.1 Ref.2

Xanthine + H2O + O2 = urate + H2O2. Ref.1 Ref.2

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. Cytoplasm Ref.2.

Tissue specificity

Detected in liver (at protein level). Ref.2

Sequence similarities

Belongs to the xanthine dehydrogenase family.

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

Contains 1 FAD-binding PCMH-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13581358Xanthine dehydrogenase/oxidase
PRO_0000166083

Regions

Domain8 – 95882Fe-2S ferredoxin-type
Domain255 – 440186FAD-binding PCMH-type
Nucleotide binding283 – 2908FAD By similarity
Nucleotide binding373 – 3775FAD By similarity

Sites

Active site12901Proton acceptor By similarity
Metal binding471Iron-sulfur 1 By similarity
Metal binding521Iron-sulfur 1 By similarity
Metal binding551Iron-sulfur 1 By similarity
Metal binding771Iron-sulfur 1 By similarity
Metal binding1171Iron-sulfur 2 By similarity
Metal binding1201Iron-sulfur 2 By similarity
Metal binding1521Iron-sulfur 2 By similarity
Metal binding1541Iron-sulfur 2 By similarity
Metal binding7961Molybdenum By similarity
Metal binding8271Molybdenum; via carbonyl oxygen By similarity
Metal binding9411Molybdenum; via amide nitrogen By similarity
Metal binding11081Molybdenum; via amide nitrogen By similarity
Binding site3631FAD By similarity
Binding site3861FAD By similarity
Binding site4301FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site4481FAD By similarity
Binding site8311Substrate By similarity
Binding site9091Substrate By similarity
Binding site9431Substrate By similarity
Binding site10391Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
P47990 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 53B049B38704995F

FASTA1,358149,614
        10         20         30         40         50         60 
MAPPETGDEL VFFVNGKKVV EKDVDPETTL LTYLRRKLGL CGTKLGCGEG GCGACTVMIS 

        70         80         90        100        110        120 
KYDPFQKKIL HHTANACLFP ICALHHVAVT TVEGIGNTKS RLHPAQERIA KSHGSQCGFC 

       130        140        150        160        170        180 
TPGIVMSMYT LLRNKPKPKM EDIEDAFQGN LCRCTGYRPI LEGYRTFAVD SNCCGKAANG 

       190        200        210        220        230        240 
TGCCHSKGEN SMNGGCCGGK ANGPGCCMNE KENVTMMSSS LFDSSEFQPL DPTQEPIFPP 

       250        260        270        280        290        300 
ELMTQRNKEQ KQVCFKGERV MWIQPTTLQE LVALKSQYPN AKLVVGNTEV GIEMRLKNML 

       310        320        330        340        350        360 
YPVILAPAWI PEMNAVQQTE TGITFGAACT LSSVEEVLRK AVAELPSYKT EIFQAALEQL 

       370        380        390        400        410        420 
RWFAGPQIRN VAALGGNIMT ASPISDLNPV LMASGSKLTL ISMEGKRTVM MDEKFFTGYR 

       430        440        450        460        470        480 
KTIVKPEEVL LSVEIPYSKE GEYFSAFKQA YRREDDIAIV TCGMRVLFQH GTSRVQEVKL 

       490        500        510        520        530        540 
SYGGMAPTTI LALKTCRELA GRDWNEKLLQ DACRLLAGEM DLSPSAPGGM VEFRRTLTLS 

       550        560        570        580        590        600 
FFFKFYLTVL QKLSKDQNGP NNLCEPVPPN YISATELFHK DPIASTQLFQ EVPRGQLVED 

       610        620        630        640        650        660 
TVGRPLVHLS AAKQACGEAV YCDDIPHYEN ELYLTLVTST QAHAKILSID ASEAQSVPGF 

       670        680        690        700        710        720 
VCFVSAKDVP GSNITGIAND ETVFAEDVVT CVGHIIGAVI ADTQEHSRRA AKAVKIKYEE 

       730        740        750        760        770        780 
LKPIVTIQEA IEQQSFIKPI KRIKKGDVNK GFEESDHILE GEMHIGGQEH FYLETHCTLA 

       790        800        810        820        830        840 
VPKGEDGEME LFVSTQNLMK TQEFTASALG VPSNRIVVRV KRMGGGFGGK ETRNTILTTV 

       850        860        870        880        890        900 
VAVAAFKTGR PVRCMLDRDE DMLISGGRHP FLGRYKVGFM KNGKIKSLEV SYYSNGGNSA 

       910        920        930        940        950        960 
DLSHGVMDRA LLHLDNSYNI PNVSIMGFIC KTNLSSNTAF RGFGGPQGMM IAECWMSDLA 

       970        980        990       1000       1010       1020 
RKCGLPPEEV RKINLYHEGD LTHFNQKLEG FTLRRCWDEC LSSSNYHARK KLIEEFNKQN 

      1030       1040       1050       1060       1070       1080 
RWKKRGMCII PTKFGISFTV PFLNQAGALV HVYTDGSVLL THGGTEMGQG LHTKMIQVAS 

      1090       1100       1110       1120       1130       1140 
RSLGIPTSKI YISETSTNTV PNTSPTAASV SADINGMAVH NACQTILKRL EPIKQSNLKG 

      1150       1160       1170       1180       1190       1200 
SWEDWIKTAY ENCISLSATG FYRIPDVGYN FETNKGKPFH YFSYGVACSE VEIDCLTGDH 

      1210       1220       1230       1240       1250       1260 
KNIRTDIVMD VGTSLNPAID IGQIEGAFVQ GIGLFTMEEL RYSPEGNLYT RGPGMYKIPA 

      1270       1280       1290       1300       1310       1320 
FGDIPTEFYV SLLRDCPNSK AIYSSKAVGE PPLFLSASVF YAIKDAIYSA REDSGVTEPF 

      1330       1340       1350 
RLDSPATPER IRNACVDTFT KMCPSAEPGT FKPWSVRA

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References

[1]"The structure of chicken liver xanthine dehydrogenase. cDNA cloning and the domain structure."
Satoh A., Amaya Y., Noda K., Nishino T.
J. Biol. Chem. 270:2818-2826(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, CATALYTIC ACTIVITY.
Tissue: Liver.
[2]"Subcellular localization of chicken liver xanthine dehydrogenase. A possible source of cytoplasmic reducing equivalents."
Coolbear K.P., Herzberg G.R., Brosnan J.T.
Biochem. J. 202:555-558(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, CATALYTIC ACTIVITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D13221 mRNA. Translation: BAA02502.1.
IPIIPI00589946.
PIRXOCHDH. A55711.
RefSeqNP_990458.1. NM_205127.1.
UniGeneGga.2494.

3D structure databases

ProteinModelPortalP47990.
SMRP47990. Positions 600-1343.
ModBaseSearch...

Protein-protein interaction databases

STRING9031.ENSGALP00000014144.

Proteomic databases

PaxDbP47990.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396025.
KEGGgga:396025.

Organism-specific databases

CTD7498.

Phylogenomic databases

eggNOGCOG4630.
HOGENOMHOG000191197.
HOVERGENHBG004182.
InParanoidP47990.
KOK00106.

Enzyme and pathway databases

ReactomeREACT_115655. Metabolism.

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.
IPR014309. Xanthine_DH_Mopterin-bd_su.
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. 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.
TIGRFAMsTIGR02963. xanthine_xdhA. 1 hit.
TIGR02965. xanthine_xdhB. 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

NextBio20816087.

Entry information

Entry nameXDH_CHICK
AccessionPrimary (citable) accession number: P47990
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 3, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents