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UniProtKB/Swiss-Prot entry Q9CLL8

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

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Entry information
Entry name HIS2_PASMU
Primary accession number Q9CLL8
Secondary accession numbers None
Integrated into Swiss-Prot on June 6, 2002
Sequence was last modified on June 1, 2001 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 39)
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: PM1206
From
Pasteurella multocida [TaxID: 747] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; Pasteurellaceae; Pasteurella.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Pm70;
DOI=10.1073/pnas.051634598; PubMed=11248100 [NCBI, ExPASy, EBI, Israel, Japan]
May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
"Complete genomic sequence of Pasteurella multocida Pm70.";
Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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
AE006160; AAK03290.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_246143.1; -.
3D structure databases
ModBase Q9CLL8.
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.
BLOCKS Q9CLL8.
ProtoNet Q9CLL8.
Genome annotation databases
GeneID 1244553; -.
GenomeReviews AE004439_GR; PM1206.
KEGG pmu:PM1206; -.
NMPDR fig|272843.1.peg.1206; -.
Phylogenomic databases
HOGENOM Q9CLL8; -.
Genome annotation databases
CMR Q9CLL8; PM1206.
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   201  201     Histidine biosynthesis bifunctional protein hisIE. PRO_0000136420
REGION   1   111  111     Phosphoribosyl-AMP cyclohydrolase. 
REGION   112   201  90     Phosphoribosyl-ATP pyrophosphohydrolase. 
Sequence information
Length: 201 AA [This is the length of the unprocessed precursor] Molecular weight: 22697 Da [This is the MW of the unprocessed precursor] CRC64: 64420D0F0152FB82 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKINWQKVDN LLPVIIQNVA TCEVLMLGYM NQEALEKTLA EKRVTFFSRT KNRLWTKGET 

        70         80         90        100        110        120 
SGHFLNVVDM SLDCDNDTLL ILVNPIGETC HTGAESCFYQ FEKTTQPDWI FLSKLERLIA 

       130        140        150        160        170        180 
SRKGADPESS YTAQLYAKGT KRIAQKVGEE GVETALAATV KDKAETICEA ADLVYHLTVL 

       190        200 
LQDADLSWSD VIHKLKERHT K
Q9CLL8 in FASTA format

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