ID PHNI_ECOLI Reviewed; 354 AA. AC P16687; Q2M6K4; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1991, sequence version 2. DT 24-JAN-2024, entry version 148. DE RecName: Full=Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnI; DE Short=RPnTP synthase subunit PhnI; DE EC=2.7.8.37; DE AltName: Full=Ribose 1-methylphosphonate 5-triphosphate synthase nucleosidase subunit; GN Name=phnI; OrderedLocusNames=b4099, JW4060; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; 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, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=22089136; DOI=10.1038/nature10622; RA Kamat S.S., Williams H.J., Raushel F.M.; RT "Intermediates in the transformation of phosphonates to phosphate by RT bacteria."; RL Nature 480:570-573(2011). RN [7] RP SUBUNIT. RC STRAIN=K12; RX PubMed=21705661; DOI=10.1073/pnas.1104922108; RA Jochimsen B., Lolle S., McSorley F.R., Nabi M., Stougaard J., Zechel D.L., RA Hove-Jensen B.; RT "Five phosphonate operon gene products as components of a multi-subunit RT complex of the carbon-phosphorus lyase pathway."; RL Proc. Natl. Acad. Sci. U.S.A. 108:11393-11398(2011). CC -!- FUNCTION: Together with PhnG, PhnH and PhnL is required for the CC transfer of the ribose triphosphate moiety from ATP to methyl CC phosphonate. PhnI alone has nucleosidase activity, catalyzing the CC hydrolysis of ATP or GTP forming alpha-D-ribose 5-triphosphate and CC adenine or guanine, respectively. {ECO:0000269|PubMed:22089136}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + methylphosphonate = adenine + alpha-D-ribose 1- CC methylphosphonate 5-triphosphate; Xref=Rhea:RHEA:34679, CC ChEBI:CHEBI:16708, ChEBI:CHEBI:30616, ChEBI:CHEBI:68684, CC ChEBI:CHEBI:68823; EC=2.7.8.37; CC Evidence={ECO:0000269|PubMed:22089136}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = adenine + D-ribose 5-triphosphate; CC Xref=Rhea:RHEA:44164, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:91013; CC Evidence={ECO:0000269|PubMed:22089136}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=64 uM for GTP (in the presence of PhnI alone) CC {ECO:0000269|PubMed:22089136}; CC KM=95 uM for ATP (in the presence of PhnI alone) CC {ECO:0000269|PubMed:22089136}; CC KM=80 uM for GTP (in the presence of PhnI, PhnG, PhnH and PhnL) CC {ECO:0000269|PubMed:22089136}; CC KM=56 uM for ATP (in the presence of PhnI, PhnG, PhnH and PhnL) CC {ECO:0000269|PubMed:22089136}; CC Note=kcat is 1.4 sec(-1) for ATP hydrolysis in the presence of PhnI CC alone, and 20 sec(-1) for RPnTP synthesis from ATP in the presence of CC PhnI, PhnG, PhnH and PhnL.; CC -!- SUBUNIT: Forms a complex with PhnG, PhnH, PhnJ and PhnK with the CC suggested composition PhnG(4)H(2)I(2)J(2)K. CC {ECO:0000269|PubMed:21705661}. CC -!- INTERACTION: CC P16687; P16685: phnG; NbExp=14; IntAct=EBI-1127704, EBI-9126715; CC -!- MISCELLANEOUS: The sequence shown is that of strain K12. CC -!- SIMILARITY: Belongs to the PhnI family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J05260; AAA24347.1; -; Genomic_DNA. DR EMBL; D90227; BAA14269.1; -; Genomic_DNA. DR EMBL; U14003; AAA96998.1; -; Genomic_DNA. DR EMBL; U00096; AAC77060.1; -; Genomic_DNA. DR EMBL; AP009048; BAE78102.1; -; Genomic_DNA. DR PIR; B65219; B65219. DR RefSeq; NP_418523.1; NC_000913.3. DR RefSeq; WP_001295388.1; NZ_SSZK01000016.1. DR PDB; 4XB6; X-ray; 1.70 A; C/G=1-354. DR PDB; 7Z15; EM; 1.93 A; C/G=1-354. DR PDB; 7Z16; EM; 2.09 A; C/G=1-354. DR PDB; 7Z17; EM; 2.57 A; C/G=1-354. DR PDB; 7Z18; EM; 1.98 A; C/G=1-354. DR PDB; 7Z19; EM; 2.57 A; C/G=1-354. DR PDBsum; 4XB6; -. DR PDBsum; 7Z15; -. DR PDBsum; 7Z16; -. DR PDBsum; 7Z17; -. DR PDBsum; 7Z18; -. DR PDBsum; 7Z19; -. DR AlphaFoldDB; P16687; -. DR EMDB; EMD-14441; -. DR EMDB; EMD-14443; -. DR EMDB; EMD-14444; -. DR EMDB; EMD-14445; -. DR SMR; P16687; -. DR BioGRID; 4263381; 10. DR BioGRID; 852898; 1. DR ComplexPortal; CPX-1929; PhnGHIJKL complex. DR DIP; DIP-10488N; -. DR IntAct; P16687; 6. DR STRING; 511145.b4099; -. DR PaxDb; 511145-b4099; -. DR EnsemblBacteria; AAC77060; AAC77060; b4099. DR GeneID; 948605; -. DR KEGG; ecj:JW4060; -. DR KEGG; eco:b4099; -. DR PATRIC; fig|1411691.4.peg.2601; -. DR EchoBASE; EB0712; -. DR eggNOG; COG3626; Bacteria. DR HOGENOM; CLU_063686_0_0_6; -. DR InParanoid; P16687; -. DR OMA; AQFTRGY; -. DR OrthoDB; 9790536at2; -. DR PhylomeDB; P16687; -. DR BioCyc; EcoCyc:EG10718-MONOMER; -. DR BioCyc; MetaCyc:EG10718-MONOMER; -. DR SABIO-RK; P16687; -. DR PRO; PR:P16687; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0061694; C:alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase complex; IDA:EcoCyc. DR GO; GO:1904176; C:carbon phosphorus lyase complex; IDA:EcoCyc. DR GO; GO:0061693; F:alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase activity; IDA:EcoCyc. DR GO; GO:0019700; P:organic phosphonate catabolic process; IMP:EcoCyc. DR GO; GO:0019634; P:organic phosphonate metabolic process; IDA:ComplexPortal. DR GO; GO:0015716; P:organic phosphonate transport; IDA:ComplexPortal. DR InterPro; IPR008773; PhnI. DR Pfam; PF05861; PhnI; 1. DR PIRSF; PIRSF007313; PhnI; 1. PE 1: Evidence at protein level; KW 3D-structure; Reference proteome; Transferase. FT CHAIN 1..354 FT /note="Alpha-D-ribose 1-methylphosphonate 5-triphosphate FT synthase subunit PhnI" FT /id="PRO_0000058395" FT VARIANT 264 FT /note="G -> D (in strain: B)" FT VARIANT 351 FT /note="Q -> K (in strain: B)" FT STRAND 2..4 FT /evidence="ECO:0007829|PDB:4XB6" FT HELIX 8..24 FT /evidence="ECO:0007829|PDB:4XB6" FT HELIX 34..40 FT /evidence="ECO:0007829|PDB:4XB6" FT HELIX 42..52 FT /evidence="ECO:0007829|PDB:4XB6" FT HELIX 57..66 FT /evidence="ECO:0007829|PDB:4XB6" FT TURN 67..69 FT /evidence="ECO:0007829|PDB:4XB6" FT HELIX 71..83 FT /evidence="ECO:0007829|PDB:4XB6" FT STRAND 87..90 FT /evidence="ECO:0007829|PDB:4XB6" FT HELIX 96..98 FT /evidence="ECO:0007829|PDB:4XB6" FT STRAND 100..105 FT /evidence="ECO:0007829|PDB:4XB6" FT STRAND 107..111 FT /evidence="ECO:0007829|PDB:4XB6" FT HELIX 131..134 FT /evidence="ECO:0007829|PDB:4XB6" FT HELIX 155..161 FT /evidence="ECO:0007829|PDB:4XB6" FT TURN 178..180 FT /evidence="ECO:0007829|PDB:4XB6" FT HELIX 189..198 FT /evidence="ECO:0007829|PDB:4XB6" FT HELIX 201..212 FT /evidence="ECO:0007829|PDB:4XB6" FT TURN 213..216 FT /evidence="ECO:0007829|PDB:7Z15" FT STRAND 221..234 FT /evidence="ECO:0007829|PDB:4XB6" FT TURN 237..239 FT /evidence="ECO:0007829|PDB:4XB6" FT STRAND 243..260 FT /evidence="ECO:0007829|PDB:4XB6" FT STRAND 263..265 FT /evidence="ECO:0007829|PDB:4XB6" FT STRAND 268..279 FT /evidence="ECO:0007829|PDB:4XB6" FT HELIX 282..293 FT /evidence="ECO:0007829|PDB:4XB6" FT HELIX 296..299 FT /evidence="ECO:0007829|PDB:4XB6" FT HELIX 306..308 FT /evidence="ECO:0007829|PDB:4XB6" FT HELIX 310..315 FT /evidence="ECO:0007829|PDB:4XB6" FT HELIX 319..327 FT /evidence="ECO:0007829|PDB:4XB6" FT HELIX 328..330 FT /evidence="ECO:0007829|PDB:4XB6" FT HELIX 334..349 FT /evidence="ECO:0007829|PDB:4XB6" SQ SEQUENCE 354 AA; 38853 MW; 9E974F01B85CCE81 CRC64; MYVAVKGGEK AIDAAHALQE SRRRGDTDLP ELSVAQIEQQ LNLAVDRVMT EGGIADRELA ALALKQASGD NVEAIFLLRA YRTTLAKLAV SEPLDTTGMR LERRISAVYK DIPGGQLLGP TYDYTHRLLD FTLLANGEAP TLTTADSEQQ PSPHVFSLLA RQGLAKFEED SGAQPDDITR TPPVYPCSRS SRLQQLMRGD EGYLLALAYS TQRGYGRNHP FAGEIRSGYI DVSIVPEELG FAVNVGELLM TECEMVNGFI DPPGEPPHFT RGYGLVFGMS ERKAMAMALV DRALQAPEYG EHATGPAQDE EFVLAHADNV EAAGFVSHLK LPHYVDFQAE LELLKRLQQE QNHG //