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Protein
Submitted name:

Xanthine dehydrogenase

Gene

xdhA

Organism
Rhodobacter capsulatus (Rhodopseudomonas capsulata)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
  2. electron carrier activity Source: InterPro
  3. flavin adenine dinucleotide binding Source: InterPro
  4. metal ion binding Source: UniProtKB-KW
  5. UDP-N-acetylmuramate dehydrogenase activity Source: InterPro
  6. xanthine dehydrogenase activity Source: InterPro
  7. xanthine oxidase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseImported

Keywords - Ligandi

2Fe-2SCombined sources, FADCombined sources, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Nucleotide-bindingCombined sources

Enzyme and pathway databases

SABIO-RKO54050.

Names & Taxonomyi

Protein namesi
Submitted name:
Xanthine dehydrogenaseImported (EC:1.1.1.204Imported)
Gene namesi
Name:xdhAImported
OrganismiRhodobacter capsulatus (Rhodopseudomonas capsulata)Imported
Taxonomic identifieri1061 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JROX-ray2.70A/C/E/G1-462[»]
1JRPX-ray3.00A/C/E/G1-462[»]
2W3RX-ray2.90A/C/E/G1-462[»]
2W3SX-ray2.60A/C/E/G1-462[»]
2W54X-ray3.30A/C/E/G1-462[»]
2W55X-ray3.40A/C/E/G1-462[»]
ProteinModelPortaliO54050.
SMRiO54050. Positions 1-462.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO54050.

Family & Domainsi

Sequence similaritiesi

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

Family and domain databases

Gene3Di1.10.150.120. 1 hit.
3.10.20.30. 1 hit.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
InterProiIPR002888. 2Fe-2S-bd.
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
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.
IPR012175. Xanth_DH_ssu_bac.
IPR014307. Xanthine_DH_ssu.
[Graphical view]
PfamiPF03450. CO_deh_flav_C. 1 hit.
PF00941. FAD_binding_5. 1 hit.
PF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view]
PIRSFiPIRSF036557. XdhA_RC. 1 hit.
SMARTiSM01092. CO_deh_flav_C. 1 hit.
[Graphical view]
SUPFAMiSSF47741. SSF47741. 1 hit.
SSF54292. SSF54292. 1 hit.
SSF55447. SSF55447. 1 hit.
SSF56176. SSF56176. 1 hit.
TIGRFAMsiTIGR02963. xanthine_xdhA. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O54050-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEIAFLLNGE TRRVRIEDPT QSLLELLRAE GLTGTKEGCN EGDCGACTVM
60 70 80 90 100
IRDAAGSRAV NACLMMLPQI AGKALRTIEG IAAPDGRLHP VQQAMIDHHG
110 120 130 140 150
SQCGFCTPGF IVSMAAAHDR DRKDYDDLLA GNLCRCTGYA PILRAAEAAA
160 170 180 190 200
GEPPADWLQA DAAFTLAQLS SGVRGQTAPA FLPETSDALA DWYLAHPEAT
210 220 230 240 250
LIAGGTDVSL WVTKALRDLP EVAFLSHCKD LAQIRETPDG YGIGAGVTIA
260 270 280 290 300
ALRAFAEGPH PALAGLLRRF ASEQVRQVAT IGGNIANGSP IGDGPPALIA
310 320 330 340 350
MGASLTLRRG QERRRMPLED FFLEYRKQDR RPGEFVESVT LPKSAPGLRC
360 370 380 390 400
YKLSKRFDQD ISAVCGCLNL TLKGSKIETA RIAFGGMAGV PKRAAAFEAA
410 420 430 440 450
LIGQDFREDT IAAALPLLAQ DFTPLSDMRA SAAYRMNAAQ AMALRYVREL
460
SGEAVAVLEV MP
Length:462
Mass (Da):49,293
Last modified:June 1, 1998 - v1
Checksum:iC98DC831531377E9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001013 Genomic DNA. Translation: CAA04469.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001013 Genomic DNA. Translation: CAA04469.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JROX-ray2.70A/C/E/G1-462[»]
1JRPX-ray3.00A/C/E/G1-462[»]
2W3RX-ray2.90A/C/E/G1-462[»]
2W3SX-ray2.60A/C/E/G1-462[»]
2W54X-ray3.30A/C/E/G1-462[»]
2W55X-ray3.40A/C/E/G1-462[»]
ProteinModelPortaliO54050.
SMRiO54050. Positions 1-462.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKO54050.

Miscellaneous databases

EvolutionaryTraceiO54050.

Family and domain databases

Gene3Di1.10.150.120. 1 hit.
3.10.20.30. 1 hit.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
InterProiIPR002888. 2Fe-2S-bd.
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
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.
IPR012175. Xanth_DH_ssu_bac.
IPR014307. Xanthine_DH_ssu.
[Graphical view]
PfamiPF03450. CO_deh_flav_C. 1 hit.
PF00941. FAD_binding_5. 1 hit.
PF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view]
PIRSFiPIRSF036557. XdhA_RC. 1 hit.
SMARTiSM01092. CO_deh_flav_C. 1 hit.
[Graphical view]
SUPFAMiSSF47741. SSF47741. 1 hit.
SSF54292. SSF54292. 1 hit.
SSF55447. SSF55447. 1 hit.
SSF56176. SSF56176. 1 hit.
TIGRFAMsiTIGR02963. xanthine_xdhA. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Xanthine dehydrogenase from the phototrophic purple bacterium Rhodobacter capsulatus is more similar to its eukaryotic counterparts than to prokaryotic molybdenum enzymes."
    Leimkuhler S., Kern M., Solomon P., McEwan A., Schwarz G., Mendal R.R., Klipp W.
    Mol. Microbiol. 27:853-869(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: B10Imported.
  2. Leimkuhler S.
    Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: B10Imported.
  3. "Crystal structures of the active and alloxanthine-inhibited forms of xanthine dehydrogenase from Rhodobacter capsulatus."
    Truglio J.J., Theis K., Leimkuhler S., Rappa R., Rajagopalan K.V., Kisker C.
    Structure 10:115-125(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH FAD AND IRON-SULFUR (2FE-2S), ACTIVE SITE.
  4. "Mechanism of Substrate and Inhibitor Binding of Rhodobacter capsulatus Xanthine Dehydrogenase."
    Dietzel U., Kuper J., Doebbler J.A., Schulte A., Truglio J.J., Leimkuhler S., Kisker C.
    J. Biol. Chem. 284:8768-8776(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH FAD AND IRON-SULFUR (2FE-2S).

Entry informationi

Entry nameiO54050_RHOCA
AccessioniPrimary (citable) accession number: O54050
Entry historyi
Integrated into UniProtKB/TrEMBL: June 1, 1998
Last sequence update: June 1, 1998
Last modified: January 7, 2015
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.