PHNM_ECOLI
ID PHNM_ECOLI Reviewed; 378 AA.
AC P16689; Q2M6K8;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase;
DE Short=RPnTP diphosphatase;
DE EC=3.6.1.63;
GN Name=phnM; OrderedLocusNames=b4095, JW4056;
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;
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).
CC -!- FUNCTION: Catalyzes the hydrolysis of alpha-D-ribose 1-
CC methylphosphonate triphosphate (RPnTP) to form alpha-D-ribose 1-
CC methylphosphonate phosphate (PRPn) and diphosphate.
CC {ECO:0000269|PubMed:22089136}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-ribose 1-methylphosphonate 5-triphosphate + H2O =
CC alpha-D-ribose 1-methylphosphonate 5-phosphate + diphosphate + H(+);
CC Xref=Rhea:RHEA:34683, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:68686, ChEBI:CHEBI:68823; EC=3.6.1.63;
CC Evidence={ECO:0000269|PubMed:22089136};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=56 uM for alpha-D-ribose 1-methylphosphonate 5-triphosphate
CC {ECO:0000269|PubMed:22089136};
CC KM=98 uM for D-ribose-5-triphosphate {ECO:0000269|PubMed:22089136};
CC KM=200 uM for D-ribose-5-diphosphate {ECO:0000269|PubMed:22089136};
CC -!- MISCELLANEOUS: The sequence shown is that of strain K12.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC {ECO:0000305}.
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DR EMBL; J05260; AAA24352.1; -; Genomic_DNA.
DR EMBL; D90227; BAA14273.1; -; Genomic_DNA.
DR EMBL; U14003; AAA96994.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77056.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78098.1; -; Genomic_DNA.
DR PIR; S56323; S56323.
DR RefSeq; NP_418519.1; NC_000913.3.
DR RefSeq; WP_000586325.1; NZ_SSZK01000016.1.
DR AlphaFoldDB; P16689; -.
DR SMR; P16689; -.
DR BioGRID; 4262021; 11.
DR STRING; 511145.b4095; -.
DR PaxDb; P16689; -.
DR PRIDE; P16689; -.
DR EnsemblBacteria; AAC77056; AAC77056; b4095.
DR EnsemblBacteria; BAE78098; BAE78098; BAE78098.
DR GeneID; 948613; -.
DR KEGG; ecj:JW4056; -.
DR KEGG; eco:b4095; -.
DR PATRIC; fig|1411691.4.peg.2605; -.
DR EchoBASE; EB0716; -.
DR eggNOG; COG3454; Bacteria.
DR HOGENOM; CLU_060303_1_0_6; -.
DR InParanoid; P16689; -.
DR OMA; MSLMDHT; -.
DR PhylomeDB; P16689; -.
DR BioCyc; EcoCyc:EG10722-MON; -.
DR BioCyc; MetaCyc:EG10722-MON; -.
DR SABIO-RK; P16689; -.
DR PRO; PR:P16689; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0019700; P:organic phosphonate catabolic process; IMP:EcoCyc.
DR CDD; cd01306; PhnM; 1.
DR InterPro; IPR013108; Amidohydro_3.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR012696; PhnM.
DR Pfam; PF07969; Amidohydro_3; 1.
DR PIRSF; PIRSF038971; PhnM; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR02318; phosphono_phnM; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Reference proteome.
FT CHAIN 1..378
FT /note="Alpha-D-ribose 1-methylphosphonate 5-triphosphate
FT diphosphatase"
FT /id="PRO_0000058399"
FT VARIANT 318
FT /note="Q -> E (in strain: B)"
SQ SEQUENCE 378 AA; 42010 MW; 28CC9C5C77EAD37D CRC64;
MIINNVKLVL ENEVVSGSLE VQNGEIRAFA ESQSRLPEAM DGEGGWLLPG LIELHTDNLD
KFFTPRPKVD WPAHSAMSSH DALMVASGIT TVLDAVAIGD VRDGGDRLEN LEKMINAIEE
TQKRGVNRAE HRLHLRCELP HHTTLPLFEK LVQREPVTLV SLMDHSPGQR QFANREKYRE
YYQGKYSLTD AQMQQYEEEQ LALAARWSQP NRESIAALCR ARKIALASHD DATHAHVAES
HQLGSVIAEF PTTFEAAEAS RKHGMNVLMG APNIVRGGSH SGNVAASELA QLGLLDILSS
DYYPASLLDA AFRVADDQSN RFTLPQAVKL VTKNPAQALN LQDRGVIGEG KRADLVLAHR
KDNHIHIDHV WRQGKRVF
