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UniProtKB/Swiss-Prot entry Q63Q94


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name HIS2_BURPS
Primary accession number Q63Q94
Secondary accession numbers None
Integrated into Swiss-Prot on April 4, 2006
Sequence was last modified on October 25, 2004 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 23)
Name and origin of the protein
Protein name Phosphoribosyl-ATP pyrophosphatase
Synonyms PRA-PH
EC 3.6.1.31
Gene name
Name: hisE
OrderedLocusNames: BPSL3131
From
Burkholderia pseudomallei (Pseudomonas pseudomallei) [TaxID: 28450] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei group.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K96243;
DOI=10.1073/pnas.0403302101; PubMed=15377794 [NCBI, ExPASy, EBI, Israel, Japan]
Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M., Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A., Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
"Genomic plasticity of the causative agent of melioidosis, Burkholderia pseudomallei.";
Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
BX571965; CAH37141.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_109724.1; -.
3D structure databases
ModBase Q63Q94.
Enzyme and pathway databases
BioCyc BPSE272560:BPSL3131-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004636; Molecular function: phosphoribosyl-ATP diphosphatase activity (inferred from electronic annotation from HAMAP).
GO:0000105; Biological process: histidine biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_01020; -; 1.
PBIL [Tree]
InterPro IPR008179; PRib-ATP_pyrophosphohydrolase.
Graphical view of domain structure.
Pfam PF01503; PRA-PH; 1.
Pfam graphical view of domain structure.
ProDom PD002611; Pra_PH/CH; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR03188; histidine_hisI; 1.
ProtoNet Q63Q94.
Genome annotation databases
GeneID 3091926; -.
GenomeReviews BX571965_GR; BPSL3131.
KEGG bps:BPSL3131; -.
Phylogenomic databases
HOGENOM Q63Q94; -.
Genome annotation databases
CMR Q63Q94; BPSL3131.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Complete proteome; Cytoplasm; Histidine biosynthesis; Hydrolase.
Features
SEVIEWER logo Feature table viewer
KeyFrom To Length Description FTId
CHAIN   1   122  122     Phosphoribosyl-ATP pyrophosphatase. PRO_0000230171
Sequence information
Length: 122 AA [This is the length of the unprocessed precursor] Molecular weight: 13361 Da [This is the MW of the unprocessed precursor] CRC64: 3D2605F29B527D08 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTQSTTEDTL LRLAAVIDSR KGGDPEQSYV SRLFHKGDDA ILKKIGEEAT EVVLAAKDVR 

        70         80         90        100        110        120 
QGGAPSALVG EVADLWFHCL VALSHFDLSP ADVIAELERR EGMSGIEEKA LRKRREREEN 


GG 

Q63Q94 in FASTA format

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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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