NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1371/journal.pone.0001271; PubMed=18060065 [NCBI, ExPASy, EBI, Israel, Japan]
Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
"Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within plasmids.";
PLoS ONE 2:E1271-E1271(2007).

Comments

CATALYTIC ACTIVITY: 1-(5-phosphoribosyl)-ATP + H₂O = 1-(5-phosphoribosyl)-AMP + diphosphate.
PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9 .
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the PRA-PH family.

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

CP000726; ABS33502.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001383917.1; -.

3D structure databases

ModBase

A7FU84.

Ontologies

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

A7FU84.

Genome annotation databases

GeneID

5394642; -.

GenomeReviews

CP000726_GR; CLB_1594.

KEGG

cba:CLB_1594; -.

CMR

A7FU84; CLB_1594.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amino-acid biosynthesis; Complete proteome; Cytoplasm; Histidine biosynthesis; Hydrolase.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 110`	`110`		`Phosphoribosyl-ATP pyrophosphatase.`	`PRO_1000063335`

Sequence information

Length: 110 AA [This is the length of the unprocessed precursor]

Molecular weight: 13029 Da [This is the MW of the unprocessed precursor]

CRC64: 5D4F7F92B56333B3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNRNNVIDSL FNIIEDRKDK PIEGSYTGYL FEKGLDKILK KVGEESSEVI IAAKNEDEEE 

        70         80         90        100        110 
LIKEICDLTY HIMVLMVEKQ IKLDDIEKEL EKRRERICNK KNERKTIEKL

A7FU84 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

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