PHNI_ECOLI
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 03-AUG-2022, entry version 140.
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; 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, 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 PDBsum; 4XB6; -.
DR AlphaFoldDB; P16687; -.
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; P16687; -.
DR PRIDE; P16687; -.
DR EnsemblBacteria; AAC77060; AAC77060; b4099.
DR EnsemblBacteria; BAE78102; BAE78102; BAE78102.
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 PhylomeDB; P16687; -.
DR BioCyc; EcoCyc:EG10718-MON; -.
DR BioCyc; MetaCyc:EG10718-MON; -.
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 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
