PHNH_ECOLI
ID PHNH_ECOLI Reviewed; 194 AA.
AC P16686; Q2M6K3;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnH;
DE Short=RPnTP synthase subunit PhnH;
DE EC=2.7.8.37;
GN Name=phnH; OrderedLocusNames=b4100, JW4061;
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, AND CATALYTIC ACTIVITY.
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).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), SUBUNIT, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=K12;
RX PubMed=17993513; DOI=10.1128/jb.01274-07;
RA Adams M.A., Luo Y., Hove-Jensen B., He S.M., van Staalduinen L.M.,
RA Zechel D.L., Jia Z.;
RT "Crystal structure of PhnH: an essential component of carbon-phosphorus
RT lyase in Escherichia coli.";
RL J. Bacteriol. 190:1072-1083(2008).
CC -!- FUNCTION: Together with PhnG, PhnI and PhnL 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 -!- SUBUNIT: Homodimer. Forms a complex with PhnG, PhnI, PhnJ and PhnK with
CC the suggested composition PhnG(4)H(2)I(2)J(2)K.
CC {ECO:0000269|PubMed:17993513, ECO:0000269|PubMed:21705661}.
CC -!- INTERACTION:
CC P16686; P16686: phnH; NbExp=5; IntAct=EBI-6401276, EBI-6401276;
CC -!- MISCELLANEOUS: The sequence shown is that of strains K12 and B.
CC -!- SIMILARITY: Belongs to the PhnH family. {ECO:0000305}.
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DR EMBL; J05260; AAA24345.1; -; Genomic_DNA.
DR EMBL; D90227; BAA14268.1; -; Genomic_DNA.
DR EMBL; U14003; AAA96999.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77061.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78103.1; -; Genomic_DNA.
DR PIR; I35718; I35718.
DR RefSeq; NP_418524.1; NC_000913.3.
DR RefSeq; WP_000171628.1; NZ_SSZK01000016.1.
DR PDB; 2FSU; X-ray; 1.70 A; A=1-194.
DR PDB; 4XB6; X-ray; 1.70 A; B/F=1-194.
DR PDBsum; 2FSU; -.
DR PDBsum; 4XB6; -.
DR AlphaFoldDB; P16686; -.
DR SMR; P16686; -.
DR BioGRID; 4262694; 8.
DR ComplexPortal; CPX-1929; PhnGHIJKL complex.
DR DIP; DIP-10487N; -.
DR IntAct; P16686; 2.
DR STRING; 511145.b4100; -.
DR PaxDb; P16686; -.
DR PRIDE; P16686; -.
DR EnsemblBacteria; AAC77061; AAC77061; b4100.
DR EnsemblBacteria; BAE78103; BAE78103; BAE78103.
DR GeneID; 948619; -.
DR KEGG; ecj:JW4061; -.
DR KEGG; eco:b4100; -.
DR PATRIC; fig|1411691.4.peg.2600; -.
DR EchoBASE; EB0711; -.
DR eggNOG; COG3625; Bacteria.
DR HOGENOM; CLU_115317_1_0_6; -.
DR InParanoid; P16686; -.
DR OMA; HDTPVWL; -.
DR PhylomeDB; P16686; -.
DR BioCyc; EcoCyc:EG10717-MON; -.
DR BioCyc; MetaCyc:EG10717-MON; -.
DR EvolutionaryTrace; P16686; -.
DR PRO; PR:P16686; -.
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; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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; 3.40.50.11310; -; 1.
DR InterPro; IPR038058; PhnH-like_sp.
DR InterPro; IPR008772; Phosphonate_metab_PhnH.
DR Pfam; PF05845; PhnH; 1.
DR PIRSF; PIRSF020680; PhnH; 1.
DR SUPFAM; SSF159709; SSF159709; 1.
DR TIGRFAMs; TIGR03292; PhnH_redo; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Transferase.
FT CHAIN 1..194
FT /note="Alpha-D-ribose 1-methylphosphonate 5-triphosphate
FT synthase subunit PhnH"
FT /id="PRO_0000058393"
FT HELIX 14..26
FT /evidence="ECO:0007829|PDB:2FSU"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:2FSU"
FT HELIX 46..55
FT /evidence="ECO:0007829|PDB:2FSU"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:2FSU"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:2FSU"
FT HELIX 71..81
FT /evidence="ECO:0007829|PDB:2FSU"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:2FSU"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:2FSU"
FT HELIX 103..108
FT /evidence="ECO:0007829|PDB:2FSU"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:2FSU"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:2FSU"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:2FSU"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:2FSU"
FT HELIX 155..163
FT /evidence="ECO:0007829|PDB:2FSU"
FT TURN 167..170
FT /evidence="ECO:0007829|PDB:2FSU"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:2FSU"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:2FSU"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:2FSU"
SQ SEQUENCE 194 AA; 21027 MW; 69F068F78EF44EF3 CRC64;
MTLETAFMLP VQDAQHSFRR LLKAMSEPGV IVALHQLKRG WQPLNIATTS VLLTLADNDT
PVWLSTPLNN DIVNQSLRFH TNAPLVSQPE QATFAVTDEA ISSEQLNALS TGTAVAPEAG
ATLILQVASL SGGRMLRLTG AGIAEERMIA PQLPECILHE LTERPHPFPL GIDLILTCGE
RLLAIPRTTH VEVC
