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O32143

- XDHE_BACSU

UniProt

O32143 - XDHE_BACSU

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Protein

Probable xanthine dehydrogenase subunit E

Gene

pucE

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

Oxidizes hypoxanthine and xanthine to uric acid.1 Publication

Catalytic activityi

Xanthine + NAD+ + H2O = urate + NADH.
Hypoxanthine + NAD+ + H2O = xanthine + NADH.

Cofactori

[2Fe-2S] clusterBy similarityNote: Binds 2 [2Fe-2S] clusters.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi52 – 521Iron-sulfur (2Fe-2S) 1PROSITE-ProRule annotation
Metal bindingi57 – 571Iron-sulfur (2Fe-2S) 1PROSITE-ProRule annotation
Metal bindingi60 – 601Iron-sulfur (2Fe-2S) 1PROSITE-ProRule annotation
Metal bindingi72 – 721Iron-sulfur (2Fe-2S) 1PROSITE-ProRule annotation
Metal bindingi110 – 1101Iron-sulfur (2Fe-2S) 2PROSITE-ProRule annotation
Metal bindingi113 – 1131Iron-sulfur (2Fe-2S) 2PROSITE-ProRule annotation
Metal bindingi145 – 1451Iron-sulfur (2Fe-2S) 2PROSITE-ProRule annotation
Metal bindingi147 – 1471Iron-sulfur (2Fe-2S) 2PROSITE-ProRule annotation

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
  2. electron carrier activity Source: InterPro
  3. metal ion binding Source: UniProtKB-KW
  4. xanthine dehydrogenase activity Source: UniProtKB-EC

GO - Biological processi

  1. hypoxanthine catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Purine metabolism

Keywords - Ligandi

2Fe-2S, Iron, Iron-sulfur, Metal-binding, NAD

Enzyme and pathway databases

BioCyciBSUB:BSU32470-MONOMER.
UniPathwayiUPA00604; UER00661.
UPA00604; UER00662.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable xanthine dehydrogenase subunit E (EC:1.17.1.4)
Short name:
XDHase subunit E
Gene namesi
Name:pucE
Synonyms:yurB
Ordered Locus Names:BSU32470
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU32470. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 173173Probable xanthine dehydrogenase subunit EPRO_0000166101Add
BLAST

Proteomic databases

PaxDbiO32143.

Expressioni

Inductioni

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.

Interactioni

Subunit structurei

Could be composed of four subunits: PucA, PucC, PucD and PucE.

Protein-protein interaction databases

STRINGi224308.BSU32470.

Structurei

3D structure databases

ProteinModelPortaliO32143.
SMRiO32143. Positions 13-170.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 90772Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG2080.
HOGENOMiHOG000166647.
InParanoidiO32143.
KOiK00087.
OMAiQSARSKM.
OrthoDBiEOG6ZSP3F.
PhylomeDBiO32143.

Family and domain databases

Gene3Di1.10.150.120. 1 hit.
3.10.20.30. 1 hit.
InterProiIPR002888. 2Fe-2S-bd.
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR012675. Beta-grasp_dom.
IPR017611. Xanthine_dehydrogenase_esu.
[Graphical view]
PfamiPF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view]
SUPFAMiSSF47741. SSF47741. 1 hit.
SSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR03198. pucE. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O32143-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDIKEAGPFP VKKEQFRMTV NGQAWEVAAV PTTHLSDLLR KEFQLTGTKV
60 70 80 90 100
SCGIGRCGAC SILIDGKLAN ACMTMAYQAD GHSITTIEGL QKEELDMCQT
110 120 130 140 150
AFLEEGGFQC GYCTPGMIIA LKALFRETPQ PSDKDIEEGL AGNLCRCTGY
160 170
GGIMRSACRI RRELNGGRRE SGF
Length:173
Mass (Da):18,838
Last modified:January 1, 1998 - v1
Checksum:i48E7D4CBB76BB321
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB15237.1.
PIRiA70017.
RefSeqiNP_391127.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB15237; CAB15237; BSU32470.
GeneIDi936680.
KEGGibsu:BSU32470.
PATRICi18978468. VBIBacSub10457_3397.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB15237.1 .
PIRi A70017.
RefSeqi NP_391127.1. NC_000964.3.

3D structure databases

ProteinModelPortali O32143.
SMRi O32143. Positions 13-170.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU32470.

Proteomic databases

PaxDbi O32143.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB15237 ; CAB15237 ; BSU32470 .
GeneIDi 936680.
KEGGi bsu:BSU32470.
PATRICi 18978468. VBIBacSub10457_3397.

Organism-specific databases

GenoListi BSU32470. [Micado ]

Phylogenomic databases

eggNOGi COG2080.
HOGENOMi HOG000166647.
InParanoidi O32143.
KOi K00087.
OMAi QSARSKM.
OrthoDBi EOG6ZSP3F.
PhylomeDBi O32143.

Enzyme and pathway databases

UniPathwayi UPA00604 ; UER00661 .
UPA00604 ; UER00662 .
BioCyci BSUB:BSU32470-MONOMER.

Family and domain databases

Gene3Di 1.10.150.120. 1 hit.
3.10.20.30. 1 hit.
InterProi IPR002888. 2Fe-2S-bd.
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR012675. Beta-grasp_dom.
IPR017611. Xanthine_dehydrogenase_esu.
[Graphical view ]
Pfami PF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view ]
SUPFAMi SSF47741. SSF47741. 1 hit.
SSF54292. SSF54292. 1 hit.
TIGRFAMsi TIGR03198. pucE. 1 hit.
PROSITEi PS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiXDHE_BACSU
AccessioniPrimary (citable) accession number: O32143
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: January 1, 1998
Last modified: November 26, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3