Ribose-phosphate pyrophosphokinase - Escherichia coli O157:H7

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P0A719 (KPRS_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 62. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Ribose-phosphate pyrophosphokinase
Short name=RPPK
EC=2.7.6.1

Alternative name(s):
Phosphoribosyl pyrophosphate synthase
Short name=P-Rib-PP synthase
Short name=PRPP synthase

Gene names

Name:	prs
Synonyms:	prsA
Ordered Locus Names:	Z1978, ECs1712

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	315 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP-Rule MF_00583_B
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Pathway	Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1. HAMAP-Rule MF_00583_B
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the ribose-phosphate pyrophosphokinase family.

Ontologies

Keywords
Biological process	Nucleotide biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	5-phosphoribose 1-diphosphate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway nucleoside metabolic process Inferred from electronic annotation. Source: InterPro nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW ribonucleoside monophosphate biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW kinase activity Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: HAMAP ribose phosphate diphosphokinase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 315

314

Ribose-phosphate pyrophosphokinase HAMAP-Rule MF_00583_B

PRO_0000141136

Regions

Region

213 – 226

Binding of phosphoribosylpyrophosphate Potential

Sites

Metal binding

129

Magnesium Potential

Metal binding

131

Magnesium Potential

Metal binding

140

Magnesium Potential

Metal binding

144

Magnesium Potential

Sequences

Sequence

Length

Mass (Da)

Tools

P0A719 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 4D69B7D118F93720
Show »

FASTA

315

34,218

        10         20         30         40         50         60 
MPDMKLFAGN ATPELAQRIA NRLYTSLGDA AVGRFSDGEV SVQINENVRG GDIFIIQSTC 

        70         80         90        100        110        120 
APTNDNLMEL VVMVDALRRA SAGRITAVIP YFGYARQDRR VRSARVPITA KVVADFLSSV 

       130        140        150        160        170        180 
GVDRVLTVDL HAEQIQGFFD VPVDNVFGSP ILLEDMLQLN LDNPIVVSPD IGGVVRARAI 

       190        200        210        220        230        240 
AKLLNDTDMA IIDKRRPRAN VSQVMHIIGD VAGRDCVLVD DMIDTGGTLC KAAEALKERG 

       250        260        270        280        290        300 
AKRVFAYATH PIFSGNAANN LRNSVIDEVV VCDTIPLSDE IKSLPNVRTL TLSGMLAEAI 

       310 
RRISNEESIS AMFEH

« Hide

References

[1]	"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. Blattner F.R. Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]	"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005174 Genomic DNA. Translation: AAG56065.1. BA000007 Genomic DNA. Translation: BAB35135.1.
PIR	H90842.
RefSeq	NP_287453.1. NC_002655.2. NP_309739.1. NC_002695.1.
3D structure databases
ProteinModelPortal	P0A719.
SMR	P0A719. Positions 4-309.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-1221661.
STRING	155864.Z1978.
Proteomic databases
PRIDE	P0A719.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAG56065; AAG56065; Z1978. BAB35135; BAB35135; BAB35135.
GeneID	913151. 960457.
KEGG	ece:Z1978. ecs:ECs1712.
PATRIC	18352676. VBIEscCol44059_1563.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0462.
HOGENOM	HOG000210449.
KO	K00948.
OMA	MQANHPD.
ProtClustDB	PRK01259.
Enzyme and pathway databases
BioCyc	ECOL386585:GJFA-1693-MONOMER.
UniPathway	UPA00087; UER00172.
Family and domain databases
HAMAP	MF_00583_B. RibP_PPkinase_B.
InterPro	IPR000842. PRib_PP_synth_CS. IPR000836. PRibTrfase_dom. IPR005946. Rib-P_diPkinase. [Graphical view]
Pfam	PF00156. Pribosyltran. 1 hit. [Graphical view]
TIGRFAMs	TIGR01251. ribP_PPkin. 1 hit.
PROSITE	PS00114. PRPP_SYNTHASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KPRS_ECO57

Accession

Primary (citable) accession number: P0A719
Secondary accession number(s): P08330, P76828, P78058

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 62 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents