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UniProtKB/Swiss-Prot entry Q8PLG5


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

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Entry information
Entry name HIS2_XANAC
Primary accession number Q8PLG5
Secondary accession numbers None
Integrated into Swiss-Prot on March 15, 2004
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    September 23, 2008 (Entry version 37)
Name and origin of the protein
Protein name Histidine biosynthesis bifunctional protein hisIE
Synonyms None
Includes Phosphoribosyl-AMP cyclohydrolase
     (PRA-CH)
     (EC 3.5.4.19)
Phosphoribosyl-ATP pyrophosphatase
     (PRA-PH)
     (EC 3.6.1.31)
Gene name
Name: hisI
Synonyms: hisIE
OrderedLocusNames: XAC1835
From
Xanthomonas axonopodis pv. citri (Citrus canker) [TaxID: 92829] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; Xanthomonadaceae; Xanthomonas.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=306;
DOI=10.1038/417459a; PubMed=12024217 [NCBI, ExPASy, EBI, Israel, Japan]
da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
"Comparison of the genomes of two Xanthomonas pathogens with differing host specificities.";
Nature 417:459-463(2002).
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
AE011816; AAM36697.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_642161.1; -.
3D structure databases
ModBase Q8PLG5.
Enzyme and pathway databases
BioCyc XAXO190486:XAC1835-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004635; Molecular function: phosphoribosyl-AMP cyclohydrolase activity (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_01019; -; 1.
PBIL [Tree]
InterPro IPR002496; PRA_CycOHase.
IPR008179; PRib-ATP_pyrophosphohydrolase.
Graphical view of domain structure.
Pfam PF01502; PRA-CH; 1.
PF01503; PRA-PH; 1.
Pfam graphical view of domain structure.
ProDom PD002610; PRA_cyclohydro; 1.
PD002611; Pra_PH/CH; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR03188; histidine_hisI; 1.
ProtoNet Q8PLG5.
Genome annotation databases
GeneID 1155906; -.
GenomeReviews AE008923_GR; XAC1835.
KEGG xac:XAC1835; -.
NMPDR fig|190486.1.peg.1805; -.
Phylogenomic databases
HOGENOM Q8PLG5; -.
Genome annotation databases
CMR Q8PLG5; XAC1835.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Complete proteome; Cytoplasm; Histidine biosynthesis; Hydrolase; Multifunctional enzyme.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   206  206     Histidine biosynthesis bifunctional protein hisIE. PRO_0000136450
REGION   1   117  117     Phosphoribosyl-AMP cyclohydrolase. 
REGION   118   206  89     Phosphoribosyl-ATP pyrophosphohydrolase. 
Sequence information
Length: 206 AA [This is the length of the unprocessed precursor] Molecular weight: 22262 Da [This is the MW of the unprocessed precursor] CRC64: 1B04984CEEFBD377 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGSNEVATGD PLATLDWNKG EGLLPVIVQD ADNLRVLMLG YMNAQALAVT QQRGEVTFFS 

        70         80         90        100        110        120 
RSKQRLWTKG ESSGNVLRVV SIQTDCDADT LLVQARPHGP TCHLGRTSCF PSAPGQFLGS 

       130        140        150        160        170        180 
LDALVAERER ERPHGSYTTK LFEQGIRRIA QKVGEEGVET ALAGVVQDDD ALLGESADLL 

       190        200 
YHLIVLLRAR GLGLGDAAAL LESRHQ 

Q8PLG5 in FASTA format

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