D1AVW2 (D1AVW2_STRM9) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Ribose-phosphate pyrophosphokinase HAMAP-Rule MF_00583
Short name=RPPK HAMAP-Rule MF_00583
EC=2.7.6.1 HAMAP-Rule MF_00583

Alternative name(s):
Phosphoribosyl pyrophosphate synthase HAMAP-Rule MF_00583

Gene names

Name:	prs HAMAP-Rule MF_00583
Ordered Locus Names:	Smon_1439

Organism

Streptobacillus moniliformis (strain ATCC 14647 / DSM 12112 / NCTC 10651 / 9901) [Complete proteome] [HAMAP]

Taxonomic identifier

519441 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Fusobacteria › Fusobacteriia › Fusobacteriales › Leptotrichiaceae › Streptobacillus › Streptobacillus moniliformis

Protein attributes

Sequence length	325 AA.
Sequence status	Complete.
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 RuleBase RU004325
Cofactor	Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_00583
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
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00583.
Sequence similarities	Belongs to the ribose-phosphate pyrophosphokinase family. HAMAP-Rule MF_00583 RuleBase RU004324

Ontologies

Keywords
Biological process	Nucleotide biosynthesis HAMAP-Rule MF_00583 RuleBase RU004324
Cellular component	Cytoplasm HAMAP-Rule MF_00583 SAAS SAAS000842
Ligand	ATP-binding HAMAP-Rule MF_00583 Magnesium HAMAP-Rule MF_00583 RuleBase RU004325 Metal-binding HAMAP-Rule MF_00583 RuleBase RU004325 Nucleotide-binding
Molecular function	Kinase HAMAP-Rule MF_00583 RuleBase RU004325 EMBL ACZ01872.1 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
Regions
	Region	216 – 229	14	5-phosphoribose 1-diphosphate binding By similarity HAMAP-Rule MF_00583
Sites
	Metal binding	131	1	Magnesium By similarity HAMAP-Rule MF_00583
	Metal binding	133	1	Magnesium By similarity HAMAP-Rule MF_00583
	Metal binding	142	1	Magnesium By similarity HAMAP-Rule MF_00583
	Metal binding	146	1	Magnesium By similarity HAMAP-Rule MF_00583

Sequences

	Sequence		Length	Mass (Da)
	D1AVW2 [UniParc]. Last modified January 19, 2010. Version 1. Checksum: D31589B4B83D98B9	FASTA	325	35,721
	10 20 30 40 50 60 MYNDHEIKVY AGTSSAKLAA KIAEKLGISL GDRTIIRFAD GETFAKSNET VRGCKVFVIQ 70 80 90 100 110 120 STSKPVNESI MELLVFIDSL KRASATEIIA VIPYYGYARQ DRKAYPREPI TSKLVADLLT 130 140 150 160 170 180 VAGATRVVTM DLHARQIQGF FNIPVDHMEA LPLFAKYFYD KGFNSENAVV VSPDVGGVKR 190 200 210 220 230 240 ARALARSLNL PLAIIDKRRE KANVSEVMNL IGEVKGKKAI LIDDIIDTAG TICNAATALK 250 260 270 280 290 300 NEGALEVYAC AVHPVFSGPA IERLKDSEFN KVIVTDTIEL PEDKKFDKLS IVSTASMFAE 310 320 TIIRIFKEEA ISDLFEVPKN LDVEG

References

[1]

"Complete genome sequence of Streptobacillus moniliformis type strain (9901T)." Nolan M., Gronow S., Lapidus A., Ivanova N., Copeland A., Lucas S., Glavina Del Rio T., Chen F., Tice H., Pitluck S., Cheng J.F., Sims D., Meincke L., Bruce D., Goodwin L., Brettin T., Han C., Detter J.C. , Pati A., Mavromatis K., Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Sproer C., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P. Stand. Genomic Sci. 1:300-307(2009) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 14647 / DSM 12112 / NCTC 10651 / 9901.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001779 Genomic DNA. Translation: ACZ01872.1.
RefSeq	YP_003306749.1. NC_013515.1.
3D structure databases
ProteinModelPortal	D1AVW2.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACZ01872; ACZ01872; Smon_1439.
GeneID	8601191.
KEGG	smf:Smon_1439.
PATRIC	32452704. VBIStrMon53754_1442.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HOG000210449.
KO	K00948.
OMA	YVQIQES.
Enzyme and pathway databases
BioCyc	SMON519441:GHY8-1504-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

D1AVW2_STRM9

Accession

Primary (citable) accession number: D1AVW2

Entry history

Integrated into UniProtKB/TrEMBL:	January 19, 2010
Last sequence update:	January 19, 2010
Last modified:	May 1, 2013
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)