NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., Detter J.C., Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P.;
"Complete sequence of chromosome of Dinoroseobacter shibae DFL 12.";
Submitted (SEP-2007) 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

CP000830; ABV94308.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001533909.1; -.

3D structure databases

ModBase

A8LSV9.

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

A8LSV9.

Genome annotation databases

GeneID

5713473; -.

GenomeReviews

CP000830_GR; Dshi_2575.

KEGG

dsh:Dshi_2575; -.

CMR

A8LSV9; Dshi_2575.

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`	`1 102`	`102`		`Phosphoribosyl-ATP pyrophosphatase.`	`PRO_1000084169`

Sequence information

Length: 102 AA [This is the length of the unprocessed precursor]

Molecular weight: 10879 Da [This is the MW of the unprocessed precursor]

CRC64: B3A0A4ED632B1F54 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSVLARLEAT IAARKGADPD SSWTAKLLAK GPEKCAEKFG EEAVEAIIEA VKGDRAKLTS 

        70         80         90        100 
EAADVLYHLL VMLAARDVAL AEVLAELERR EGISGISEKA SR

A8LSV9 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