PHNN_ECOLI
ID PHNN_ECOLI Reviewed; 185 AA.
AC P16690; Q2M6K9;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Ribose 1,5-bisphosphate phosphokinase PhnN;
DE EC=2.7.4.23;
DE AltName: Full=Ribose 1,5-bisphosphokinase;
GN Name=phnN; OrderedLocusNames=b4094, JW4055;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B;
RX PubMed=2155230; DOI=10.1016/s0021-9258(19)39587-0;
RA Chen C.-M., Ye Q.-Z., Zhu Z., Wanner B.L., Walsh C.T.;
RT "Molecular biology of carbon-phosphorus bond cleavage. Cloning and
RT sequencing of the phn (psiD) genes involved in alkylphosphonate uptake and
RT C-P lyase activity in Escherichia coli B.";
RL J. Biol. Chem. 265:4461-4471(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1840580; DOI=10.1128/jb.173.8.2665-2672.1991;
RA Makino K., Kim S.K., Shinagawa H., Amemura M., Nakata A.;
RT "Molecular analysis of the cryptic and functional phn operons for
RT phosphonate use in Escherichia coli K-12.";
RL J. Bacteriol. 173:2665-2672(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP FUNCTION AS A RIBOSE 1,5-BISPHOSPHOKINASE, CATALYTIC ACTIVITY, AND
RP SUBSTRATE SPECIFICITY.
RX PubMed=12700258; DOI=10.1128/jb.185.9.2793-2801.2003;
RA Hove-Jensen B., Rosenkrantz T.J., Haldimann A., Wanner B.L.;
RT "Escherichia coli phnN, encoding ribose 1,5-bisphosphokinase activity
RT (phosphoribosyl diphosphate forming): dual role in phosphonate degradation
RT and NAD biosynthesis pathways.";
RL J. Bacteriol. 185:2793-2801(2003).
RN [7]
RP FUNCTION IN THE ORGANOPHOSPHONATE METABOLISM.
RX PubMed=19733071; DOI=10.1016/j.bmcl.2009.08.035;
RA He S.M., Luo Y., Hove-Jensen B., Zechel D.L.;
RT "A fluorescent substrate for carbon-phosphorus lyase: towards the pathway
RT for organophosphonate metabolism in bacteria.";
RL Bioorg. Med. Chem. Lett. 19:5954-5957(2009).
RN [8]
RP SUBSTRATE SPECIFICITY.
RX PubMed=19854894; DOI=10.1128/jb.01131-09;
RA Hove-Jensen B., Rosenkrantz T.J., Zechel D.L., Willemoes M.;
RT "Accumulation of intermediates of the carbon-phosphorus lyase pathway for
RT phosphonate degradation in phn mutants of Escherichia coli.";
RL J. Bacteriol. 192:370-374(2010).
CC -!- FUNCTION: Catalyzes the phosphorylation of ribose 1,5-bisphosphate to
CC 5-phospho-D-ribosyl alpha-1-diphosphate (PRPP). Accepts ATP but not GTP
CC as a phosphoryl donor, and uses ribose 1,5-bisphosphate but not ribose,
CC ribose 1-phosphate, or ribose 5-phosphate as a phosphoryl acceptor.
CC {ECO:0000269|PubMed:12700258, ECO:0000269|PubMed:19733071}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-ribose 1,5-bisphosphate + ATP = 5-phospho-alpha-D-
CC ribose 1-diphosphate + ADP; Xref=Rhea:RHEA:20109, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:58017, ChEBI:CHEBI:68688, ChEBI:CHEBI:456216;
CC EC=2.7.4.23; Evidence={ECO:0000269|PubMed:12700258};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose
CC 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from
CC D-ribose 5-phosphate (route II): step 3/3.
CC -!- SIMILARITY: Belongs to the ribose 1,5-bisphosphokinase family.
CC {ECO:0000305}.
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DR EMBL; J05260; AAA24353.1; -; Genomic_DNA.
DR EMBL; D90227; BAA14274.1; -; Genomic_DNA.
DR EMBL; U14003; AAA96993.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77055.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78097.1; -; Genomic_DNA.
DR PIR; F35719; F35719.
DR RefSeq; NP_418518.1; NC_000913.3.
DR RefSeq; WP_000971886.1; NZ_SSZK01000016.1.
DR AlphaFoldDB; P16690; -.
DR SMR; P16690; -.
DR BioGRID; 4262022; 2.
DR IntAct; P16690; 33.
DR STRING; 511145.b4094; -.
DR PaxDb; P16690; -.
DR PRIDE; P16690; -.
DR EnsemblBacteria; AAC77055; AAC77055; b4094.
DR EnsemblBacteria; BAE78097; BAE78097; BAE78097.
DR GeneID; 948608; -.
DR KEGG; ecj:JW4055; -.
DR KEGG; eco:b4094; -.
DR PATRIC; fig|1411691.4.peg.2606; -.
DR EchoBASE; EB0717; -.
DR eggNOG; COG3709; Bacteria.
DR HOGENOM; CLU_102477_0_0_6; -.
DR InParanoid; P16690; -.
DR OMA; RLIWLTG; -.
DR PhylomeDB; P16690; -.
DR BioCyc; EcoCyc:EG10723-MON; -.
DR BioCyc; MetaCyc:EG10723-MON; -.
DR BRENDA; 2.7.4.23; 2026.
DR UniPathway; UPA00087; UER00175.
DR PRO; PR:P16690; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0033863; F:ribose 1,5-bisphosphate phosphokinase activity; IDA:UniProtKB.
DR GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009435; P:NAD biosynthetic process; IBA:GO_Central.
DR GO; GO:0019634; P:organic phosphonate metabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00836; PhnN; 1.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR012699; PhnN.
DR SMART; SM00072; GuKc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02322; phosphon_PhnN; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..185
FT /note="Ribose 1,5-bisphosphate phosphokinase PhnN"
FT /id="PRO_0000058400"
FT BINDING 10..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 185 AA; 20730 MW; 399ADE57C7975325 CRC64;
MMGKLIWLMG PSGSGKDSLL AELRLREQTQ LLVAHRYITR DASAGSENHI ALSEQEFFTR
AGQNLLALSW HANGLYYGVG VEIDLWLHAG FDVLVNGSRA HLPQARARYQ SALLPVCLQV
SPEILRQRLE NRGRENASEI NARLARAARY TPQDCHTLNN DGSLRQSVDT LLTLIHQKEK
HHACL
