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Reviewed, UniProtKB/Swiss-Prot P80457 (XDH_BOVIN)

Last modified June 16, 2009. Version 88. 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 · Web resources · 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
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length1332 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.

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 Ref.3
Chain2 – 13321331Xanthine dehydrogenase/oxidase
PRO_0000166082

Regions

Domain4 – 91882Fe-2S ferredoxin-type
Domain229 – 414186FAD-binding PCMH-type

Sites

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

Amino acid modifications

Glycosylation10731N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict1881T → TQ in CAA67117. Ref.2
Sequence conflict1991E → K in CAA67117. Ref.2
Sequence conflict3661M → V in CAA67117. Ref.2
Sequence conflict5521D → H in CAA58497. Ref.1
Sequence conflict9581R → K in CAA67117. Ref.2
Sequence conflict9761Q → E in CAA67117. Ref.2
Sequence conflict1039 – 10402GQ → E in CAA67117. Ref.2
Sequence conflict12441L → V in CAA67117. Ref.2
Sequence conflict12681A → P in CAA67117. Ref.2
Sequence conflict1279 – 12813RAA → ARG in CAA67117. Ref.2

Secondary structure

1 ..................................................................................................................................................................................................................... 1332
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P80457-1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 744BA523471948B7

FASTA1,332146,790
        10         20         30         40         50         60 
MTADELVFFV NGKKVVEKNA DPETTLLAYL RRKLGLRGTK LGCGEGGCGA CTVMLSKYDR 

        70         80         90        100        110        120 
LQDKIIHFSA NACLAPICTL HHVAVTTVEG IGSTKTRLHP VQERIAKSHG SQCGFCTPGI 

       130        140        150        160        170        180 
VMSMYTLLRN QPEPTVEEIE DAFQGNLCRC TGYRPILQGF RTFAKNGGCC GGNGNNPNCC 

       190        200        210        220        230        240 
MNQKKDHTVT LSPSLFNPEE FMPLDPTQEP IFPPELLRLK DVPPKQLRFE GERVTWIQAS 

       250        260        270        280        290        300 
TLKELLDLKA QHPEAKLVVG NTEIGIEMKF KNQLFPMIIC PAWIPELNAV EHGPEGISFG 

       310        320        330        340        350        360 
AACALSSVEK TLLEAVAKLP TQKTEVFRGV LEQLRWFAGK QVKSVASLGG NIITASPISD 

       370        380        390        400        410        420 
LNPVFMASGT KLTIVSRGTR RTVPMDHTFF PSYRKTLLGP EEILLSIEIP YSREDEFFSA 

       430        440        450        460        470        480 
FKQASRREDD IAKVTCGMRV LFQPGSMQVK ELALCYGGMA DRTISALKTT QKQLSKFWNE 

       490        500        510        520        530        540 
KLLQDVCAGL AEELSLSPDA PGGMIEFRRT LTLSFFFKFY LTVLKKLGKD SKDKCGKLDP 

       550        560        570        580        590        600 
TYTSATLLFQ KDPPANIQLF QEVPNGQSKE DTVGRPLPHL AAAMQASGEA VYCDDIPRYE 

       610        620        630        640        650        660 
NELFLRLVTS TRAHAKIKSI DVSEAQKVPG FVCFLSADDI PGSNETGLFN DETVFAKDTV 

       670        680        690        700        710        720 
TCVGHIIGAV VADTPEHAER AAHVVKVTYE DLPAIITIED AIKNNSFYGS ELKIEKGDLK 

       730        740        750        760        770        780 
KGFSEADNVV SGELYIGGQD HFYLETHCTI AIPKGEEGEM ELFVSTQNAM KTQSFVAKML 

       790        800        810        820        830        840 
GVPVNRILVR VKRMGGGFGG KETRSTLVSV AVALAAYKTG HPVRCMLDRN EDMLITGGRH 

       850        860        870        880        890        900 
PFLARYKVGF MKTGTIVALE VDHYSNAGNS RDLSHSIMER ALFHMDNCYK IPNIRGTGRL 

       910        920        930        940        950        960 
CKTNLSSNTA FRGFGGPQAL FIAENWMSEV AVTCGLPAEE VRWKNMYKEG DLTHFNQRLE 

       970        980        990       1000       1010       1020 
GFSVPRCWDE CLKSSQYYAR KSEVDKFNKE NCWKKRGLCI IPTKFGISFT VPFLNQAGAL 

      1030       1040       1050       1060       1070       1080 
IHVYTDGSVL VSHGGTEMGQ GLHTKMVQVA SKALKIPISK IYISETSTNT VPNSSPTAAS 

      1090       1100       1110       1120       1130       1140 
VSTDIYGQAV YEACQTILKR LEPFKKKNPD GSWEDWVMAA YQDRVSLSTT GFYRTPNLGY 

      1150       1160       1170       1180       1190       1200 
SFETNSGNAF HYFTYGVACS EVEIDCLTGD HKNLRTDIVM DVGSSLNPAI DIGQVEGAFV 

      1210       1220       1230       1240       1250       1260 
QGLGLFTLEE LHYSPEGSLH TRGPSTYKIP AFGSIPTEFR VSLLRDCPNK KAIYASKAVG 

      1270       1280       1290       1300       1310       1320 
EPPLFLGASV FFAIKDAIRA ARAQHTNNNT KELFRLDSPA TPEKIRNACV DKFTTLCVTG 

      1330 
APGNCKPWSL RV

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References

[1]"Purification of the bovine xanthine oxidoreductase from milk fat globule membranes and cloning of complementary deoxyribonucleic acid."
Berglund L., Rasmussen J.T., Andersen M.D., Rasmussen M.S., Petersen T.E.
J. Dairy Sci. 79:198-204(1996) [PubMed: 8708081] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Mammary gland.
[2]"The xanthine oxidoreductase gene: structure and regulation."
Terao M., Kurosaki M., Zanotta S., Garattini E.
Biochem. Soc. Trans. 25:791-796(1997) [PubMed: 9388547] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[3]"Properties of rabbit liver aldehyde oxidase and the relationship of the enzyme to xanthine oxidase and dehydrogenase."
Turner N.A., Doyle W.A., Ventom A.M., Bray R.C.
Eur. J. Biochem. 232:646-657(1995) [PubMed: 7556219] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-23; 186-205 AND 552-562.
Tissue: Milk.
[4]"Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion."
Enroth C., Eger B.T., Okamoto K., Nishino T., Nishino T., Pai E.F.
Proc. Natl. Acad. Sci. U.S.A. 97:10723-10728(2000) [PubMed: 11005854] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
+Additional computationally mapped references.

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Cross-references

Sequence databases

X83508 mRNA. Translation: CAA58497.1.
X98491 mRNA. Translation: CAA67117.1.
IPIIPI00695367.
PIRS65135.
RefSeqNP_776397.1.
UniGeneBt.5403

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1FIQX-ray2.50A1-219[»]
B220-569[»]
C570-1332[»]
1FO4X-ray2.10A/B1-1332[»]
1N5XX-ray2.80A/B1-1332[»]
1V97X-ray1.94A/B1-1332[»]
1VDVX-ray1.98A/B1-1332[»]
3B9JX-ray2.30A/I1-219[»]
B/J220-569[»]
C/K570-1332[»]
3BDJX-ray2.00A/B1-1332[»]
3ETRX-ray2.20A/L2-165[»]
B/M224-528[»]
C/N571-1325[»]
3EUBX-ray2.602/A/J/S1-165[»]
3/B/K/T224-528[»]
4/C/L/U571-1332[»]
DisProtDP00450.
DP00451.
ModBaseSearch...

Genome annotation databases

EnsemblENSBTAG00000012519. Bos taurus. [Contig view]
GeneID280960.
KEGGbta:280960.

Phylogenomic databases

HOVERGENP80457.

Enzyme and pathway databases

BRENDA1.17.1.4. 251.
1.17.3.2. 251.

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.
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.
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...

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Entry information

Entry nameXDH_BOVIN
AccessionPrimary (citable) accession number: P80457
Secondary accession number(s): Q95325
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 88 of the entry and version 4 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 · Web resources · Cross-references · Entry information · Relevant documents