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UniProtKB/Swiss-Prot entry Q9PBD1


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

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Entry information
Entry name HIS2_XYLFA
Primary accession number Q9PBD1
Secondary accession numbers None
Integrated into Swiss-Prot on June 6, 2002
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 46)
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: XF_2213
From
Xylella fastidiosa [TaxID: 2371] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; Xanthomonadaceae; Xylella.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=9a5c;
DOI=10.1038/35018003; PubMed=10910347 [NCBI, ExPASy, EBI, Israel, Japan]
Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M., Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S., Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S., Bueno M.R.P., Camargo A.A., Camargo L.E.A., Carraro D.M., Carrer H., Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M., Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H., Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S., Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H., Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D., Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E., Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F., Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N., Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F., Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y., Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O., Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A., de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R., Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B., Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G., Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M., da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z., Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D., Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S., Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C.;
"The genome sequence of the plant pathogen Xylella fastidiosa.";
Nature 406:151-159(2000).
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
AE003849; AAF85012.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR H82584; H82584.
RefSeq NP_299492.1; -.
3D structure databases
ModBase Q9PBD1.
Enzyme and pathway databases
BioCyc XFAS160492:XF2213-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 Q9PBD1.
Genome annotation databases
GeneID 1127766; -.
GenomeReviews AE003849_GR; XF_2213.
KEGG xfa:XF2213; -.
NMPDR fig|160492.1.peg.2199; -.
Phylogenomic databases
HOGENOM Q9PBD1; -.
Genome annotation databases
CMR Q9PBD1; XF_2213.
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_0000136452
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: 22560 Da [This is the MW of the unprocessed precursor] CRC64: 2D436ACB5BB3D369 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MCNEPATSDV ALPDLDWAKG DGLLPVIVQD ADTLRVLMLG YMNSQALEVT QRSRLVTFYS 

        70         80         90        100        110        120 
RSKQRLWTKG ERSGHVLHLV AIDADCDADT LLVQARPRGP TCHLGRTSCF PAAPGQFLGA 

       130        140        150        160        170        180 
LDALVAERER ERPQDSYTTA LFEQGVRRIA QKVGEEGVET ALAGVVQVDD ALLDESADLL 

       190        200 
YHLIVLLRAR GLSLADAVTV LEARHR 

Q9PBD1 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
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