NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.;
"Complete sequence of chromosome 1 of Burkholderia sp. 383.";
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.

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

CP000151; ABB07133.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_367777.1; -.

3D structure databases

ModBase

Q39K83.

Enzyme and pathway databases

BioCyc

BSP36773:BCEP18194_A3531-MON; -.

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

Q39K83.

Genome annotation databases

GeneID

3748708; -.

GenomeReviews

CP000151_GR; Bcep18194_A3531.

KEGG

bur:Bcep18194_A3531; -.

Phylogenomic databases

HOGENOM

Q39K83; -.

Genome annotation databases

CMR

Q39K83; Bcep18194_A3531.

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`	`1 121`	`121`		`Phosphoribosyl-ATP pyrophosphatase.`	`PRO_0000230173`

Sequence information

Length: 121 AA [This is the length of the unprocessed precursor]

Molecular weight: 13288 Da [This is the MW of the unprocessed precursor]

CRC64: B84C1B5599EE26F8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTQSTEDTLL RLAAVIDSRK GGDPDQSYVS RLFHKGDDAV LKKIGEEATE VVLAAKDVRQ 

        70         80         90        100        110        120 
GGAPTALVGE VADLWFHCLV MLSHFDLSPA DVIAELERRE GLSGIEEKAL RKRREREENG 


G

Q39K83 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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