PHNL_ECOLI
ID PHNL_ECOLI Reviewed; 226 AA.
AC P16679; Q2M6K7;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL;
DE Short=RPnTP synthase subunit PhnL;
DE EC=2.7.8.37;
GN Name=phnL; OrderedLocusNames=b4096, JW4057;
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 / W3110 / ATCC 27325 / DSM 5911;
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, AND CATALYTIC ACTIVITY.
RC STRAIN=K12;
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 PhnI is required for the
CC transfer of the ribose triphosphate moiety from ATP to methyl
CC phosphonate. {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 -!- SIMILARITY: Belongs to the ABC transporter superfamily. {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; AAA24350.1; -; Genomic_DNA.
DR EMBL; D90227; BAA14272.1; -; Genomic_DNA.
DR EMBL; U14003; AAA96995.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77057.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78099.1; -; Genomic_DNA.
DR PIR; D35719; D35719.
DR RefSeq; NP_418520.1; NC_000913.3.
DR RefSeq; WP_000611405.1; NZ_SSZK01000016.1.
DR AlphaFoldDB; P16679; -.
DR SMR; P16679; -.
DR BioGRID; 4262019; 4.
DR BioGRID; 852905; 1.
DR ComplexPortal; CPX-1929; PhnGHIJKL complex.
DR IntAct; P16679; 4.
DR STRING; 511145.b4096; -.
DR PaxDb; P16679; -.
DR PRIDE; P16679; -.
DR EnsemblBacteria; AAC77057; AAC77057; b4096.
DR EnsemblBacteria; BAE78099; BAE78099; BAE78099.
DR GeneID; 948612; -.
DR KEGG; ecj:JW4057; -.
DR KEGG; eco:b4096; -.
DR PATRIC; fig|1411691.4.peg.2604; -.
DR EchoBASE; EB0715; -.
DR eggNOG; COG4778; Bacteria.
DR HOGENOM; CLU_000604_1_22_6; -.
DR InParanoid; P16679; -.
DR OMA; MHLRDGI; -.
DR PhylomeDB; P16679; -.
DR BioCyc; EcoCyc:PHNL-MON; -.
DR BioCyc; MetaCyc:PHNL-MON; -.
DR PRO; PR:P16679; -.
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; IPI:ComplexPortal.
DR GO; GO:0061693; F:alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR012701; CP_lyase_PhnL.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02324; CP_lyasePhnL; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..226
FT /note="Alpha-D-ribose 1-methylphosphonate 5-triphosphate
FT synthase subunit PhnL"
FT /id="PRO_0000092745"
FT DOMAIN 2..226
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 41..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 226 AA; 24705 MW; 195EC8BB5A2D21D2 CRC64;
MINVQNVSKT FILHQQNGVR LPVLNRASLT VNAGECVVLH GHSGSGKSTL LRSLYANYLP
DEGQIQIKHG DEWVDLVTAP ARKVVEIRKT TVGWVSQFLR VIPRISALEV VMQPLLDTGV
PREACAAKAA RLLTRLNVPE RLWHLAPSTF SGGEQQRVNI ARGFIVDYPI LLLDEPTASL
DAKNSAAVVE LIREAKTRGA AIVGIFHDEA VRNDVADRLH PMGASS
