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O32143 (XDHE_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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 (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length173 AA.
Sequence statusComplete.
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; urate from hypoxanthine: step 1/2.

Purine metabolism; hypoxanthine degradation; urate 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) 1 By similarity
Metal binding571Iron-sulfur (2Fe-2S) 1 By similarity
Metal binding601Iron-sulfur (2Fe-2S) 1 By similarity
Metal binding721Iron-sulfur (2Fe-2S) 1 By similarity
Metal binding1101Iron-sulfur (2Fe-2S) 2 By similarity
Metal binding1131Iron-sulfur (2Fe-2S) 2 By similarity
Metal binding1451Iron-sulfur (2Fe-2S) 2 By similarity
Metal binding1471Iron-sulfur (2Fe-2S) 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
O32143 [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL009126 Genomic DNA. Translation: CAB15237.1.
PIRA70017.
RefSeqNP_391127.1. NC_000964.3.

3D structure databases

ProteinModelPortalO32143.
SMRO32143. Positions 13-170.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU32470.

Proteomic databases

PaxDbO32143.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB15237; CAB15237; BSU32470.
GeneID936680.
KEGGbsu:BSU32470.
PATRIC18978468. VBIBacSub10457_3397.

Organism-specific databases

GenoListBSU32470. [Micado]

Phylogenomic databases

eggNOGCOG2080.
HOGENOMHOG000166647.
KOK00087.
OMAGKLANAC.
ProtClustDBCLSK2752501.

Enzyme and pathway databases

BioCycBSUB:BSU32470-MONOMER.
UniPathwayUPA00604; UER00661.
UPA00604; UER00662.

Family and domain databases

Gene3D1.10.150.120. 1 hit.
3.10.20.30. 1 hit.
InterProIPR002888. 2Fe-2S-bd.
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR012675. Beta-grasp_dom.
IPR017611. Xanthine_dehydrogenase_esu.
[Graphical view]
PfamPF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view]
SUPFAMSSF47741. 2Fe-2S_bind. 1 hit.
SSF54292. Ferredoxin. 1 hit.
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: May 1, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents