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Reviewed, UniProtKB/Swiss-Prot P22985 (XDH_RAT)

Last modified June 16, 2009. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

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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
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length1331 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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. Interacts with BTN1A1 By similarity.

Subcellular location

Peroxisome.

Induction

By interferon.

Sequence similarities

Belongs to the xanthine dehydrogenase family.

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

Contains 1 FAD-binding PCMH-type domain.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 13311330Xanthine dehydrogenase/oxidase
PRO_0000166086

Regions

Domain4 – 91882Fe-2S ferredoxin-type
Domain228 – 413186FAD-binding PCMH-type

Sites

Metal binding371Iron-sulfur (2Fe-2S) By similarity
Metal binding431Iron-sulfur (2Fe-2S) By similarity
Metal binding481Iron-sulfur (2Fe-2S) By similarity
Metal binding511Iron-sulfur (2Fe-2S) By similarity

Amino acid modifications

Modified residue2211Phosphothreonine By similarity
Glycosylation10731N-linked (GlcNAc...) Potential

Secondary structure

1 ....................................................................................................................................................................................................................... 1331
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P22985-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: BF2586A9C63A0B2C

FASTA1,331146,243
        10         20         30         40         50         60 
MTADELVFFV NGKKVVEKNA DPETTLLVYL RRKLGLCGTK LGCGEGGCGA CTVMISKYDR 

        70         80         90        100        110        120 
LQNKIVHFSV NACLAPICSL HHVAVTTVEG IGNTQKLHPV QERIARSHGS QCGFCTPGIV 

       130        140        150        160        170        180 
MSMYTLLRNQ PEPTVEEIEN AFQGNLCRCT GYRPILQGFR TFAKDGGCCG GSGNNPNCCM 

       190        200        210        220        230        240 
NQTKDQTVSL SPSLFNPEDF KPLDPTQEPI FPPELLRLKD TPQKKLRFEG ERVTWIQAST 

       250        260        270        280        290        300 
MEELLDLKAQ HPDAKLVVGN TEIGIEMKFK NMLFPLIVCP AWIPELNSVV HGPEGISFGA 

       310        320        330        340        350        360 
SCPLSLVESV LAEEIAKLPE QKTEVFRGVM EQLRWFAGKQ VKSVASIGGN IITASPISDL 

       370        380        390        400        410        420 
NPVFMASGAK LTLVSRGTRR TVRMDHTFFP GYRKTLLRPE EILLSIEIPY SKEGEFFSAF 

       430        440        450        460        470        480 
KQASRREDDI AKVTSGMRVL FKPGTIEVQE LSLCFGGMAD RTISALKTTP KQLSKSWNEE 

       490        500        510        520        530        540 
LLQSVCAGLA EELQLAPDAP GGMVEFRRTL TLSFFFKFYL TVLQKLGRAD LEDMCGKLDP 

       550        560        570        580        590        600 
TFASATLLFQ KDPPANVQLF QEVPKDQSEE DMVGRPLPHL AANMQASGEA VYCDDIPRYE 

       610        620        630        640        650        660 
NELSLRLVTS TRAHAKITSI DTSEAKKVPG FVCFLTAEDV PNSNATGLFN DETVFAKDEV 

       670        680        690        700        710        720 
TCVGHIIGAV VADTPEHAQR AARGVKITYE DLPAIITIQD AINNNSFYGS EIKIEKGDLK 

       730        740        750        760        770        780 
KGFSEADNVV SGELYIGGQE HFYLETNCTI AVPKGEAGEM ELFVSTQNTM KTQSFVAKML 

       790        800        810        820        830        840 
GVPDNRIVVR VKRMGGGFGG KETRSTVVST ALALAAHKTG RPVRCMLDRD EDMLITGGRH 

       850        860        870        880        890        900 
PFLAKYKVGF MKTGTVVALE VAHFSNGGNT EDLSRSIMER ALFHMDNAYK IPNIRGTGRI 

       910        920        930        940        950        960 
CKTNLPSNTA FRGFGGPQGM LIAEYWMSEV AITCGLPAEE VRRKNMYKEG DLTHFNQKLE 

       970        980        990       1000       1010       1020 
GFTLPRCWDE CIASSQYLAR KREVEKFNRE NCWKKRGLCI IPTKFGISFT LPFLNQGGAL 

      1030       1040       1050       1060       1070       1080 
VHVYTDGSVL LTHGGTEMGQ GLHTKMVQVA SRALKIPTSK IHISETSTNT VPNTSPTAAS 

      1090       1100       1110       1120       1130       1140 
ASADLNGQGV YEACQTILKR LEPFKKKKPT GPWEAWVMDA YTSAVSLSAT GFYKTPNLGY 

      1150       1160       1170       1180       1190       1200 
SFETNSGNPF HYFSYGVACS EVEIDCLTGD HKNLRTDIVM DVGSSLNPAI DIGQVEGAFV 

      1210       1220       1230       1240       1250       1260 
QGLGLFTMEE LHYSPEGSLH TRGPSTYKIP AFGSIPIEFR VSLLRDCPNK RAIYASKAVG 

      1270       1280       1290       1300       1310       1320 
EPPLFLASSI FFAIKDAIRA ARAQHGDNAK QLFQLDSPAT PEKIRNACVD QFTTLCVTGV 

      1330 
PENCKSWSVR I

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References

[1]"Proteolytic conversion of xanthine dehydrogenase from the NAD-dependent type to the O2-dependent type. Amino acid sequence of rat liver xanthine dehydrogenase and identification of the cleavage sites of the enzyme protein during irreversible conversion by trypsin."
Amaya Y., Yamazaki K., Sato M., Noda K., Nishino T., Nishino T.
J. Biol. Chem. 265:14170-14175(1990) [PubMed: 2387845] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Liver.
[2]"Identification of the rat xanthine dehydrogenase/oxidase promoter."
Chow C.W., Clark M., Rinaldo J., Chalkley R.
Nucleic Acids Res. 22:1846-1854(1994) [PubMed: 8208609] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 1-55.
Strain: Sprague-Dawley.
+Additional computationally mapped references.

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Cross-references

Sequence databases

J05579 mRNA. Translation: AAA42349.1.
U08122, U08120, U08121 Unassigned DNA. Translation: AAA18869.1.
IPIIPI00231694.
RefSeqNP_058850.1.
UniGeneRn.202951

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1WYGX-ray2.60A2-1330[»]
2E3TX-ray2.28A/B1-1331[»]
ModBaseSearch...

Proteomic databases

PRIDEP22985.

Genome annotation databases

EnsemblENSRNOG00000007081. Rattus norvegicus. [Contig view]
GeneID497811.
KEGGrno:497811.

Organism-specific databases

RGD62043. Xdh.

Phylogenomic databases

HOVERGENP22985.

Enzyme and pathway databases

BRENDA1.17.1.4. 248.
1.17.3.2. 248.

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...

Other Resources

NextBio697781.

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Entry information

Entry nameXDH_RAT
AccessionPrimary (citable) accession number: P22985
Secondary accession number(s): Q63157
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 97 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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