PHNJ_ECOLI
ID PHNJ_ECOLI Reviewed; 281 AA.
AC P16688; Q2M6K5;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Alpha-D-ribose 1-methylphosphonate 5-phosphate C-P lyase;
DE Short=PRPn C-P lyase;
DE EC=4.7.1.1 {ECO:0000269|PubMed:22089136};
GN Name=phnJ; OrderedLocusNames=b4098, JW4059;
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 COFACTOR.
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: Catalyzes the breakage of the C-P bond in alpha-D-ribose 1-
CC methylphosphonate 5-phosphate (PRPn) forming alpha-D-ribose 1,2-cyclic
CC phosphate 5-phosphate (PRcP). {ECO:0000269|PubMed:22089136}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + alpha-D-ribose 1-methylphosphonate 5-phosphate + S-
CC adenosyl-L-methionine = 5'-deoxyadenosine + A + alpha-D-ribose 1,2-
CC cyclic phosphate 5-phosphate + H(+) + L-methionine + methane;
CC Xref=Rhea:RHEA:34707, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16183, ChEBI:CHEBI:17319, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:68686,
CC ChEBI:CHEBI:68687; EC=4.7.1.1;
CC Evidence={ECO:0000269|PubMed:22089136};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:22089136};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000269|PubMed:22089136};
CC -!- SUBUNIT: Forms a complex with PhnG, PhnH, PhnI and PhnK with the
CC suggested composition PhnG(4)H(2)I(2)J(2)K.
CC {ECO:0000269|PubMed:21705661}.
CC -!- MISCELLANEOUS: The sequence shown is that of strain K12.
CC -!- SIMILARITY: Belongs to the PhnJ family. {ECO:0000305}.
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DR EMBL; J05260; AAA24348.1; -; Genomic_DNA.
DR EMBL; D90227; BAA14270.1; -; Genomic_DNA.
DR EMBL; U14003; AAA96997.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77059.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78101.1; -; Genomic_DNA.
DR PIR; A65219; A65219.
DR RefSeq; NP_418522.1; NC_000913.3.
DR RefSeq; WP_000002303.1; NZ_SSZK01000016.1.
DR PDB; 4XB6; X-ray; 1.70 A; D/H=1-281.
DR PDBsum; 4XB6; -.
DR AlphaFoldDB; P16688; -.
DR SMR; P16688; -.
DR BioGRID; 4263382; 9.
DR ComplexPortal; CPX-1929; PhnGHIJKL complex.
DR DIP; DIP-10489N; -.
DR IntAct; P16688; 4.
DR STRING; 511145.b4098; -.
DR PaxDb; P16688; -.
DR PRIDE; P16688; -.
DR EnsemblBacteria; AAC77059; AAC77059; b4098.
DR EnsemblBacteria; BAE78101; BAE78101; BAE78101.
DR GeneID; 948606; -.
DR KEGG; ecj:JW4059; -.
DR KEGG; eco:b4098; -.
DR PATRIC; fig|1411691.4.peg.2602; -.
DR EchoBASE; EB0713; -.
DR eggNOG; COG3627; Bacteria.
DR HOGENOM; CLU_063386_0_0_6; -.
DR InParanoid; P16688; -.
DR OMA; MVYQVPI; -.
DR PhylomeDB; P16688; -.
DR BioCyc; EcoCyc:EG10719-MON; -.
DR BioCyc; MetaCyc:EG10719-MON; -.
DR BRENDA; 4.7.1.1; 2026.
DR PRO; PR:P16688; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0061694; C:alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase complex; IPI:ComplexPortal.
DR GO; GO:1904176; C:carbon phosphorus lyase complex; IDA:EcoCyc.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0098848; F:alpha-D-ribose 1-methylphosphonate 5-phosphate C-P-lyase activity; IDA:EcoCyc.
DR GO; GO:0016829; F:lyase activity; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion 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 InterPro; IPR010306; PhnJ.
DR Pfam; PF06007; PhnJ; 1.
DR PIRSF; PIRSF011468; PhnJ; 1.
DR SFLD; SFLDF00379; Phosphonate_metabolism_(PhnJ); 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding;
KW Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..281
FT /note="Alpha-D-ribose 1-methylphosphonate 5-phosphate C-P
FT lyase"
FT /id="PRO_0000058397"
FT VARIANT 103
FT /note="V -> L (in strain: B)"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:4XB6"
FT HELIX 14..29
FT /evidence="ECO:0007829|PDB:4XB6"
FT HELIX 50..59
FT /evidence="ECO:0007829|PDB:4XB6"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:4XB6"
FT HELIX 77..90
FT /evidence="ECO:0007829|PDB:4XB6"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:4XB6"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:4XB6"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:4XB6"
FT TURN 130..134
FT /evidence="ECO:0007829|PDB:4XB6"
FT HELIX 138..147
FT /evidence="ECO:0007829|PDB:4XB6"
FT HELIX 151..164
FT /evidence="ECO:0007829|PDB:4XB6"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:4XB6"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:4XB6"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:4XB6"
FT HELIX 190..196
FT /evidence="ECO:0007829|PDB:4XB6"
FT STRAND 200..207
FT /evidence="ECO:0007829|PDB:4XB6"
FT TURN 208..211
FT /evidence="ECO:0007829|PDB:4XB6"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:4XB6"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:4XB6"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:4XB6"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:4XB6"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:4XB6"
FT STRAND 251..255
FT /evidence="ECO:0007829|PDB:4XB6"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:4XB6"
FT STRAND 262..268
FT /evidence="ECO:0007829|PDB:4XB6"
FT HELIX 269..277
FT /evidence="ECO:0007829|PDB:4XB6"
SQ SEQUENCE 281 AA; 31845 MW; 241F6AF140995468 CRC64;
MANLSGYNFA YLDEQTKRMI RRAILKAVAI PGYQVPFGGR EMPMPYGWGT GGIQLTASVI
GESDVLKVID QGADDTTNAV SIRNFFKRVT GVNTTERTDD ATVIQTRHRI PETPLTEDQI
IIFQVPIPEP LRFIEPRETE TRTMHALEEY GVMQVKLYED IARFGHIATT YAYPVKVNGR
YVMDPSPIPK FDNPKMDMMP ALQLFGAGRE KRIYAVPPFT RVESLDFDDH PFTVQQWDEP
CAICGSTHSY LDEVVLDDAG NRMFVCSDTD YCRQQSEAKN Q
