Annotation for this protein is in progress - please check future releases for more complete information


DP00450: Xanthine dehydrogenase/oxidaseFASTA viewXML view

General information
DisProt:DP00450
Name:Xanthine dehydrogenase/oxidase
Synonym(s):XDH_BOVIN
Xanthine dehydrogenase [domain 1]
XD
EC=1.17.1.4
Xanthine oxidase [domain 2]
XO
EC=1.17.3.2
Xanthine oxidoreductase
First appeared in release:Release 3.0 (02/17/2006)
UniProt:P80457
UniGene:Bt.5403
SwissProt: XDH_BOVIN
TrEMBL:  
NCBI (GI): 109940048
Source organism:Bos taurus (Bovine)
Sequence length:1332
Percent disordered:9%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MTADELVFFV NGKKVVEKNA DPETTLLAYL RRKLGLRGTK LGCGEGGCGA CTVMLSKYDR - 60
LQDKIIHFSA NACLAPICTL HHVAVTTVEG IGSTKTRLHP VQERIAKSHG SQCGFCTPGI - 120
VMSMYTLLRN QPEPTVEEIE DAFQGNLCRC TGYRPILQGF RTFAKNGGCC GGNGNNPNCC - 180
MNQKKDHTVT LSPSLFNPEE FMPLDPTQEP IFPPELLRLK DVPPKQLRFE GERVTWIQAS - 240
TLKELLDLKA QHPEAKLVVG NTEIGIEMKF KNQLFPMIIC PAWIPELNAV EHGPEGISFG - 300
AACALSSVEK TLLEAVAKLP TQKTEVFRGV LEQLRWFAGK QVKSVASLGG NIITASPISD - 360
LNPVFMASGT KLTIVSRGTR RTVPMDHTFF PSYRKTLLGP EEILLSIEIP YSREDEFFSA - 420
FKQASRREDD IAKVTCGMRV LFQPGSMQVK ELALCYGGMA DRTISALKTT QKQLSKFWNE - 480
KLLQDVCAGL AEELSLSPDA PGGMIEFRRT LTLSFFFKFY LTVLKKLGKD SKDKCGKLDP - 540
TYTSATLLFQ KHPPANIQLF QEVPNGQSKE DTVGRPLPHL AAAMQASGEA VYCDDIPRYE - 600
NELFLRLVTS TRAHAKIKSI DVSEAQKVPG FVCFLSADDI PGSNETGLFN DETVFAKDTV - 660
TCVGHIIGAV VADTPEHAER AAHVVKVTYE DLPAIITIED AIKNNSFYGS ELKIEKGDLK - 720
KGFSEADNVV SGELYIGGQD HFYLETHCTI AIPKGEEGEM ELFVSTQNAM KTQSFVAKML - 780
GVPVNRILVR VKRMGGGFGG KETRSTLVSV AVALAAYKTG HPVRCMLDRN EDMLITGGRH - 840
PFLARYKVGF MKTGTIVALE VDHYSNAGNS RDLSHSIMER ALFHMDNCYK IPNIRGTGRL - 900
CKTNLSSNTA FRGFGGPQAL FIAENWMSEV AVTCGLPAEE VRWKNMYKEG DLTHFNQRLE - 960
GFSVPRCWDE CLKSSQYYAR KSEVDKFNKE NCWKKRGLCI IPTKFGISFT VPFLNQAGAL - 1020
IHVYTDGSVL VSHGGTEMGQ GLHTKMVQVA SKALKIPISK IYISETSTNT VPNSSPTAAS - 1080
VSTDIYGQAV YEACQTILKR LEPFKKKNPD GSWEDWVMAA YQDRVSLSTT GFYRTPNLGY - 1140
SFETNSGNAF HYFTYGVACS EVEIDCLTGD HKNLRTDIVM DVGSSLNPAI DIGQVEGAFV - 1200
QGLGLFTLEE LHYSPEGSLH TRGPSTYKIP AFGSIPTEFR VSLLRDCPNK KAIYASKAVG - 1260
EPPLFLGASV FFAIKDAIRA ARAQHTNNNT KELFRLDSPA TPEKIRNACV DKFTTLCVTG - 1320
APGNCKPWSL RV



Functional narrative    

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.

Region 1: 1-2 Region 2: 166-191 Region 4: 166-223 Region 3: 532-536 Region 5: 529-570 Region 6: 1316-1332

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered
Name: 
Location:1 - 2
Length:2
Region sequence:

MT

Modification type: Complex
PDB:  
Structural/functional type: Function arises from the disordered state
Functional classes:  
Functional subclasses: Electron transfer
Detection methods:
  1. X-ray crystallography
References:
  1. Enroth C, Eger BT, Okamoto K, Nishino T, Pai EF. "Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion." Proc Natl Acad Sci U S A. 2000; 97(20): 10723-8. PubMed: 11005854
Comments:
 



Region 2
Type:Disordered
Name: 
Location:166 - 191
Length:26
Region sequence:

NGGCCGGNGNNPNCCMNQKKDHTVTL

Modification type: Complex
PDB:  
Structural/functional type: Function arises from the disordered state
Functional classes: Entropic chain
Functional subclasses: Electron transfer
Flexible linkers/spacers
Detection methods:
  1. X-ray crystallography
References:
  1. Enroth C, Eger BT, Okamoto K, Nishino T, Pai EF. "Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion." Proc Natl Acad Sci U S A. 2000; 97(20): 10723-8. PubMed: 11005854
Comments:
 



Region 3
Type:Disordered
Name: 
Location:532 - 536
Length:5
Region sequence:

KDKCG

Modification type: Complex
PDB:  
Structural/functional type: Function arises from the disordered state
Functional classes: Modification site
Entropic chain
Functional subclasses: Electron transfer
Flexible linkers/spacers
Detection methods:
  1. X-ray crystallography
References:
  1. Enroth C, Eger BT, Okamoto K, Nishino T, Pai EF. "Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion." Proc Natl Acad Sci U S A. 2000; 97(20): 10723-8. PubMed: 11005854
Comments:
 



Region 4
Type:Disordered
Name: 
Location:166 - 223
Length:58
Region sequence:

NGGCCGGNGNNPNCCMNQKKDHTVTLSPSLFNPEEFMPLDPTQEPIFPPELLRLKDVP

Modification type: Complex
PDB:  
Structural/functional type: Function arises from the disordered state
Functional classes: Modification site
Entropic chain
Functional subclasses: Electron transfer
Flexible linkers/spacers
Detection methods:
  1. X-ray crystallography
References:
There are no documents referencing this region.
Comments:
Information migrated from DP00451.


Region 5
Type:Disordered
Name: 
Location:529 - 570
Length:42
Region sequence:

KDSKDKCGKLDPTYTSATLLFQKHPPANIQLFQEVPNGQSKE

Modification type: Complex
PDB:  
Structural/functional type: Function arises from the disordered state
Functional classes: Modification site
Entropic chain
Functional subclasses: Electron transfer
Flexible linkers/spacers
Detection methods:
  1. X-ray crystallography
References:
There are no documents referencing this region.
Comments:
Information migrated from DP00451.


Region 6
Type:Disordered
Name: 
Location:1316 - 1332
Length:17
Region sequence:

LCVTGAPGNCKPWSLRV

Modification type: Complex
PDB:  
Structural/functional type: Function arises from the disordered state
Functional classes:  
Functional subclasses: Electron transfer
Substrate/ligand binding
Detection methods:
  1. X-ray crystallography
References:
There are no documents referencing this region.
Comments:
Information migrated from DP00451.


References

  1. Berglund L, Rasmussen JT, Andersen MD, Rasmussen MS, Petersen TE. "Purification of the bovine xanthine oxidoreductase from milk fat globule membranes and cloning of complementary deoxyribonucleic acid." J Dairy Sci. 1996; 79(2): 198-204. PubMed: 8708081



Comments


Xanthine oxidoreductases catalyze the last two steps in the formation of urate, oxidation of hypoxanthine to xanthine, and xanthine to uric acid. These are synthesized as xanthine dehydrogenase which can be reversibly converted to xanthine oxidase by oxidation of sulfhydryl residues or irreversibly by proteolysis. See DP00451 for xanthine oxidase.


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