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UniProtKB/Swiss-Prot entry P62346


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

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Entry information
Entry name HIS2_BACC1
Primary accession number P62346
Secondary accession numbers None
Integrated into Swiss-Prot on July 5, 2004
Sequence was last modified on July 5, 2004 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 32)
Name and origin of the protein
Protein name Phosphoribosyl-ATP pyrophosphatase
Synonyms PRA-PH
EC 3.6.1.31
Gene name
Name: hisE
OrderedLocusNames: BCE_1532
From
Bacillus cereus (strain ATCC 10987) [TaxID: 222523] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; Bacillus cereus group.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1093/nar/gkh258; PubMed=14960714 [NCBI, ExPASy, EBI, Israel, Japan]
Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1.";
Nucleic Acids Res. 32:977-988(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
AE017194; AAS40461.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_977853.1; -.
3D structure databases
SMR P62346; 4-95.
ModBase P62346.
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.
BLOCKS P62346.
ProtoNet P62346.
Genome annotation databases
GeneID 2751481; -.
GenomeReviews AE017194_GR; BCE_1532.
KEGG bca:BCE_1532; -.
NMPDR fig|222523.1.peg.1525; -.
TIGR BCE_1532; -.
Phylogenomic databases
HOGENOM P62346; -.
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   107  107     Phosphoribosyl-ATP pyrophosphatase. PRO_0000136344
Sequence information
Length: 107 AA [This is the length of the unprocessed precursor] Molecular weight: 12467 Da [This is the MW of the unprocessed precursor] CRC64: 1454004A20BE22B2 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKNAFTLLFE TIEERKRNPL PESYTNYLFS KGEDKILKKI GEECTEVIIA SKNNDNEELV 

        70         80         90        100 
KEIVDVLYHC FVLLAEKNIS LEDIMEEVTE RNGKLSRVGD RREIDTL 

P62346 in FASTA format

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