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Reviewed, UniProtKB/Swiss-Prot P47990 (XDH_CHICK)

Last modified June 16, 2009. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Xanthine dehydrogenase/oxidase
Including the following 2 domains:
    1- Recommended name:
            Xanthine dehydrogenase
                Short name=XD
              EC=1.17.1.4
    2- Recommended name:
            Xanthine oxidase
                Short name=XO
              EC=1.17.3.2
        Alternative name(s):
            Xanthine oxidoreductase
Gene names
Name: XDH
OrganismGallus gallus (Chicken)
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length1358 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

This enzyme can be converted from the dehydrogenase form (D) to the oxidase form (O) irreversibly by proteolysis or reversibly through the oxidation of sulfhydryl groups.

Catalytic activity

Xanthine + NAD+ + H2O = urate + NADH.

Hypoxanthine + NAD+ + H2O = xanthine + NADH.

Xanthine + H2O + O2 = urate + H2O2.

Cofactor

Binds 2 2Fe-2S clusters.

FAD.

Molybdopterin.

Subunit structure

Homodimer.

Subcellular location

Peroxisome.

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

Sites

Metal binding411Iron-sulfur (2Fe-2S) By similarity
Metal binding471Iron-sulfur (2Fe-2S) By similarity
Metal binding521Iron-sulfur (2Fe-2S) By similarity
Metal binding551Iron-sulfur (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
P47990-1 [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: 7852355] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.

Cross-references

Sequence databases

D13221 mRNA. Translation: BAA02502.1.
IPIIPI00589946.
PIRXOCHDH. A55711.
RefSeqNP_990458.1.
UniGeneGga.43173

3D structure databases

HSSPHSSP built from PDB template 1FO4 based on UniProtKB P80457.
SMRP47990. Positions 7-1357.
ModBaseSearch...

Genome annotation databases

EnsemblENSGALG00000008701. Gallus gallus. [Contig view]
GeneID396025.
KEGGgga:396025.

Phylogenomic databases

HOGENOMP47990.
HOVERGENP47990.

Enzyme and pathway databases

BRENDA1.17.1.4. 4.
1.17.3.2. 4.

Family and domain databases

InterProIPR002888. 2Fe-2S_bd.
IPR006058. 2Fe2S_fd_BS.
IPR000674. Ald_Oxase/Xan_DH_a/b.
IPR016208. Ald_Oxase/xanthine_DH.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
IPR012675. b-grasp_ferredoxin-like.
IPR005107. CO_DH_flav_C.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR001041. Ferredoxin.
IPR002346. Mopterin_DH_FAD-bd.
IPR000572. OxRdtase_Mopterin-bd.
IPR014309. Xanthine_DH_Mopterin-bd_su.
IPR014307. Xanthine_DH_ssu.
[Graphical view]
Gene3DG3DSA:3.30.365.10. Ald_xan_DH_mo_bd. 2 hits.
G3DSA:3.90.1170.50. Aldxan_DH_hamm. 1 hit.
G3DSA:3.30.390.50. CO_DH_flav_C. 1 hit.
G3DSA:3.30.465.10. CO_DH_flavoprot_FAD-bd_sub2. 1 hit.
G3DSA:3.30.43.10. FAD-binding_2_sub1. 1 hit.
G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
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.
ProDomPD186071. 2Fe-2S_bind. 1 hit.
[Graphical view] [Entries sharing at least one domain]
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...

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: June 16, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents