P16690 (PHNN_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribose 1,5-bisphosphate phosphokinase PhnN
EC=2.7.4.23

Alternative name(s):
Ribose 1,5-bisphosphokinase

Gene names

Name:	phnN
Ordered Locus Names:	b4094, JW4055

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	185 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the phosphorylation of ribose 1,5-bisphosphate to 5-phospho-D-ribosyl alpha-1-diphosphate (PRPP). Accepts ATP but not GTP as a phosphoryl donor, and uses ribose 1,5-bisphosphate but not ribose, ribose 1-phosphate, or ribose 5-phosphate as a phosphoryl acceptor. Ref.6 Ref.7
Catalytic activity	ATP + alpha-D-ribose 1,5-bisphosphate = ADP + 5-phospho-alpha-D-ribose 1-diphosphate. Ref.6
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 II): step 3/3. HAMAP-Rule MF_00836
Sequence similarities	Belongs to the ribose 1,5-bisphosphokinase family.

Ontologies

Keywords
Ligand	ATP-binding Nucleotide-binding
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	5-phosphoribose 1-diphosphate biosynthetic process Inferred from direct assay Ref.6. Source: UniProtKB NAD biosynthetic process Inferred from genetic interaction Ref.6. Source: EcoCyc organic phosphonate metabolic process Inferred from direct assay Ref.7. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ribose 1,5-bisphosphate phosphokinase activity Inferred from direct assay Ref.6. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 185	185	Ribose 1,5-bisphosphate phosphokinase PhnN HAMAP-Rule MF_00836		PRO_0000058400
Regions
	Nucleotide binding	10 – 17	8	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	P16690 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: 399ADE57C7975325	FASTA	185	20,730
	10 20 30 40 50 60 MMGKLIWLMG PSGSGKDSLL AELRLREQTQ LLVAHRYITR DASAGSENHI ALSEQEFFTR 70 80 90 100 110 120 AGQNLLALSW HANGLYYGVG VEIDLWLHAG FDVLVNGSRA HLPQARARYQ SALLPVCLQV 130 140 150 160 170 180 SPEILRQRLE NRGRENASEI NARLARAARY TPQDCHTLNN DGSLRQSVDT LLTLIHQKEK HHACL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular biology of carbon-phosphorus bond cleavage. Cloning and sequencing of the phn (psiD) genes involved in alkylphosphonate uptake and C-P lyase activity in Escherichia coli B." Chen C.-M., Ye Q.-Z., Zhu Z., Wanner B.L., Walsh C.T. J. Biol. Chem. 265:4461-4471(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: B.
[2]	"Molecular analysis of the cryptic and functional phn operons for phosphonate use in Escherichia coli K-12." Makino K., Kim S.K., Shinagawa H., Amemura M., Nakata A. J. Bacteriol. 173:2665-2672(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[3]	"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R. Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Escherichia coli phnN, encoding ribose 1,5-bisphosphokinase activity (phosphoribosyl diphosphate forming): dual role in phosphonate degradation and NAD biosynthesis pathways." Hove-Jensen B., Rosenkrantz T.J., Haldimann A., Wanner B.L. J. Bacteriol. 185:2793-2801(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS A RIBOSE 1,5-BISPHOSPHOKINASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.
[7]	"A fluorescent substrate for carbon-phosphorus lyase: towards the pathway for organophosphonate metabolism in bacteria." He S.M., Luo Y., Hove-Jensen B., Zechel D.L. Bioorg. Med. Chem. Lett. 19:5954-5957(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN THE ORGANOPHOSPHONATE METABOLISM.
[8]	"Accumulation of intermediates of the carbon-phosphorus lyase pathway for phosphonate degradation in phn mutants of Escherichia coli." Hove-Jensen B., Rosenkrantz T.J., Zechel D.L., Willemoes M. J. Bacteriol. 192:370-374(2010) [PubMed] [Europe PMC] [Abstract] Cited for: SUBSTRATE SPECIFICITY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J05260 Genomic DNA. Translation: AAA24353.1. D90227 Genomic DNA. Translation: BAA14274.1. U14003 Genomic DNA. Translation: AAA96993.1. U00096 Genomic DNA. Translation: AAC77055.1. AP009048 Genomic DNA. Translation: BAE78097.1.
PIR	F35719.
RefSeq	NP_418518.1. NC_000913.2. YP_492238.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P16690.
SMR	P16690. Positions 2-27.
ModBase	Search...
Protein-protein interaction databases
IntAct	P16690. 33 interactions.
STRING	511145.b4094.
Proteomic databases
PaxDb	P16690.
PRIDE	P16690.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC77055; AAC77055; b4094. BAE78097; BAE78097; BAE78097.
GeneID	12933028. 948608.
KEGG	ecj:Y75_p3982. eco:b4094.
PATRIC	32123747. VBIEscCol129921_4222.
Organism-specific databases
EchoBASE	EB0717.
EcoGene	EG10723. phnN.
Phylogenomic databases
eggNOG	COG3709.
HOGENOM	HOG000037637.
KO	K05774.
OMA	KVINVTA.
ProtClustDB	PRK10078.
Enzyme and pathway databases
BioCyc	EcoCyc:EG10723-MONOMER. ECOL316407:JW4055-MONOMER. MetaCyc:EG10723-MONOMER.
UniPathway	UPA00087; UER00175.
Gene expression databases
Genevestigator	P16690.
Family and domain databases
HAMAP	MF_00836. PhnN.
InterPro	IPR008145. Guanylate_kin/L-typ_Ca_channel. IPR012699. PhnN. [Graphical view]
SMART	SM00072. GuKc. 1 hit. [Graphical view]
TIGRFAMs	TIGR02322. phosphon_PhnN. 1 hit.
PROSITE	PS50052. GUANYLATE_KINASE_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PHNN_ECOLI

Accession

Primary (citable) accession number: P16690
Secondary accession number(s): Q2M6K9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	May 1, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program