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Reviewed, UniProtKB/Swiss-Prot O32143 (XDHE_BACSU)

Last modified June 16, 2009. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
    Probable xanthine dehydrogenase subunit E
      Short name=XDHase subunit E
    EC=1.17.1.4
Gene names
Name: pucE
Synonyms: yurB
Ordered Locus Names: BSU32470
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length173 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Oxidizes hypoxanthine and xanthine to uric acid. Ref.2

Catalytic activity

Xanthine + NAD+ + H2O = urate + NADH.

Hypoxanthine + NAD+ + H2O = xanthine + NADH.

Cofactor

Binds 2 2Fe-2S clusters By similarity.

Pathway

Purine metabolism; hypoxanthine degradation; uric acid from hypoxanthine: step 1/2.

Purine metabolism; hypoxanthine degradation; uric acid from hypoxanthine: step 2/2.

Subunit structure

Could be composed of four subunits: pucA, pucC, pucD and pucE.

Induction

Expression is very low in excess nitrogen (glutamate plus ammonia) and is induced during limiting-nitrogen conditions (glutamate). Expression decreases when allantoin is added during limiting-nitrogen conditions.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 173173Probable xanthine dehydrogenase subunit E
PRO_0000166101

Regions

Domain14 – 90772Fe-2S ferredoxin-type

Sites

Metal binding521Iron-sulfur (2Fe-2S) Potential
Metal binding571Iron-sulfur (2Fe-2S) Potential
Metal binding601Iron-sulfur (2Fe-2S) Potential
Metal binding721Iron-sulfur (2Fe-2S) Potential
Metal binding1101Iron-sulfur (2Fe-2S) Potential
Metal binding1131Iron-sulfur (2Fe-2S) Potential
Metal binding1451Iron-sulfur (2Fe-2S) Potential
Metal binding1471Iron-sulfur (2Fe-2S) Potential

Sequences

Sequence LengthMass (Da)Tools
O32143-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 48E7D4CBB76BB321

FASTA17318,838
        10         20         30         40         50         60 
MDIKEAGPFP VKKEQFRMTV NGQAWEVAAV PTTHLSDLLR KEFQLTGTKV SCGIGRCGAC 

        70         80         90        100        110        120 
SILIDGKLAN ACMTMAYQAD GHSITTIEGL QKEELDMCQT AFLEEGGFQC GYCTPGMIIA 

       130        140        150        160        170 
LKALFRETPQ PSDKDIEEGL AGNLCRCTGY GGIMRSACRI RRELNGGRRE SGF 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[2]"Functional analysis of 14 genes that constitute the purine catabolic pathway in Bacillus subtilis and evidence for a novel regulon controlled by the PucR transcription activator."
Schultz A.C., Nygaard P., Saxild H.H.
J. Bacteriol. 183:3293-3302(2001) [PubMed: 11344136] [Abstract]
Cited for: FUNCTION.
Strain: 168.

Cross-references

Sequence databases

AL009126 Genomic DNA. Translation: CAB15237.1.
PIRA70017.
RefSeqNP_391127.1.

3D structure databases

HSSPHSSP built from PDB template 1HLR based on UniProtKB Q46509.
ModBaseSearch...

Genome annotation databases

GeneID936680.
GenomeReviewsGene locus BSU32470 in contig AL009126_GR.
KEGGbsu:BSU32470.
NMPDRfig|224308.1.peg.3253.

Organism-specific databases

SubtiListBG13988. pucE. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMO32143.
OMAO32143. MAVWANG.

Enzyme and pathway databases

BioCycBSUB224308:BSU3244-MON.
BRENDA1.17.1.4. 150.

Family and domain databases

InterProIPR002888. 2Fe-2S_bd.
IPR006058. 2Fe2S_fd_BS.
IPR001041. Ferredoxin.
IPR017611. Xanthine_dehydrogenase_esu.
[Graphical view]
PfamPF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view]
ProDomPD186071. 2Fe-2S_bind. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR03198. pucE. 1 hit.
PROSITEPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXDHE_BACSU
AccessionPrimary (citable) accession number: O32143
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: January 1, 1998
Last modified: June 16, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

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