PHNO_ECOLI
ID PHNO_ECOLI Reviewed; 144 AA.
AC P16691; Q2M6L0;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Aminoalkylphosphonate N-acetyltransferase {ECO:0000303|PubMed:23056305};
DE EC=2.3.1.280 {ECO:0000269|PubMed:23056305};
DE AltName: Full=KAT {ECO:0000303|PubMed:30352934};
DE AltName: Full=Peptidyl-lysine N-acetyltransferase {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:30352934};
GN Name=phnO {ECO:0000303|PubMed:2155230}; OrderedLocusNames=b4093, JW4054;
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 DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=23056305; DOI=10.1371/journal.pone.0046416;
RA Hove-Jensen B., McSorley F.R., Zechel D.L.;
RT "Catabolism and detoxification of 1-aminoalkylphosphonic acids: N-
RT acetylation by the phnO gene product.";
RL PLoS ONE 7:E46416-E46416(2012).
RN [7]
RP FUNCTION AS A LYSINE ACETYLTRANSFERASE, AND CATALYTIC ACTIVITY.
RC STRAIN=K12;
RX PubMed=30352934; DOI=10.1128/mbio.01905-18;
RA Christensen D.G., Meyer J.G., Baumgartner J.T., D'Souza A.K., Nelson W.C.,
RA Payne S.H., Kuhn M.L., Schilling B., Wolfe A.J.;
RT "Identification of novel protein lysine acetyltransferases in Escherichia
RT coli.";
RL MBio 9:E01905-E01905(2018).
RN [8]
RP ERRATUM OF PUBMED:30352934.
RX PubMed=30967468; DOI=10.1128/mbio.00592-19;
RA Christensen D.G., Meyer J.G., Baumgartner J.T., D'Souza A.K., Nelson W.C.,
RA Payne S.H., Kuhn M.L., Schilling B., Wolfe A.J.;
RT "Correction for Christensen et al., 'Identification of novel protein lysine
RT acetyltransferases in Escherichia coli'.";
RL MBio 10:0-0(2019).
CC -!- FUNCTION: Aminoalkylphosphonate N-acetyltransferase which is able to
CC acetylate a range of aminoalkylphosphonic acids, including
CC aminomethylphosphonate, (S)-1-aminoethylphosphonate and 2-
CC aminoethyl- and 3-aminopropylphosphonate, using acetyl-CoA as acetyl
CC donor. Is required for the utilization of aminomethylphosphonate and
CC (S)-1-aminoethylphosphonate as a phosphate source via the C-P lyase
CC pathway. Is also essential for the detoxification of (S)-1-
CC aminoethylphosphonate, a structural analog of D-alanine that has
CC bacteriocidal properties due to inhibition of cell wall synthesis
CC (PubMed:23056305). Also acts as a N-epsilon-lysine acetyltransferase
CC that catalyzes acetylation of several proteins (PubMed:30352934).
CC {ECO:0000269|PubMed:23056305, ECO:0000269|PubMed:30352934}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + aminomethylphosphonate = 2-N-
CC acetamidomethylphosphonate + CoA; Xref=Rhea:RHEA:51428,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133674,
CC ChEBI:CHEBI:134093; EC=2.3.1.280;
CC Evidence={ECO:0000269|PubMed:23056305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-1-aminoethylphosphonate + acetyl-CoA = [(1S)-1-
CC acetamidoethyl]phosphonate + CoA; Xref=Rhea:RHEA:51432,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:134098,
CC ChEBI:CHEBI:134099; Evidence={ECO:0000269|PubMed:23056305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930;
CC Evidence={ECO:0000269|PubMed:30352934};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:Q8ZKE6};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8ZKE6}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene have lost the ability to
CC utilize aminomethylphosphonate or (S)-1-aminoethylphosphonate as the
CC sole source of phosphate for growth, but are still able to utilize the
CC other aminoalkylphosphonates 2-aminoethyl- and 3-
CC aminopropylphosphonate, and alkylphosphonates. They are also much more
CC susceptible to the bacteriocidal effect of (S)-1-aminoethylphosphonate,
CC even with phosphate or D-alanine present.
CC {ECO:0000269|PubMed:23056305}.
CC -!- MISCELLANEOUS: The sequence shown is that of strains K12 and B.
CC {ECO:0000305}.
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DR EMBL; J05260; AAA24354.1; -; Genomic_DNA.
DR EMBL; D90227; BAA14275.1; -; Genomic_DNA.
DR EMBL; U14003; AAA96992.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77054.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78096.1; -; Genomic_DNA.
DR PIR; G35719; G35719.
DR RefSeq; NP_418517.1; NC_000913.3.
DR RefSeq; WP_001110490.1; NZ_STEB01000014.1.
DR AlphaFoldDB; P16691; -.
DR SMR; P16691; -.
DR BioGRID; 4262023; 11.
DR BioGRID; 852893; 1.
DR IntAct; P16691; 1.
DR STRING; 511145.b4093; -.
DR jPOST; P16691; -.
DR PaxDb; P16691; -.
DR PRIDE; P16691; -.
DR EnsemblBacteria; AAC77054; AAC77054; b4093.
DR EnsemblBacteria; BAE78096; BAE78096; BAE78096.
DR GeneID; 66671996; -.
DR GeneID; 948599; -.
DR KEGG; ecj:JW4054; -.
DR KEGG; eco:b4093; -.
DR PATRIC; fig|1411691.4.peg.2607; -.
DR EchoBASE; EB0718; -.
DR eggNOG; COG0456; Bacteria.
DR HOGENOM; CLU_013985_34_6_6; -.
DR InParanoid; P16691; -.
DR OMA; ASHVGFK; -.
DR PhylomeDB; P16691; -.
DR BioCyc; EcoCyc:EG10724-MON; -.
DR BioCyc; MetaCyc:EG10724-MON; -.
DR BRENDA; 2.3.1.280; 2026.
DR BRENDA; 2.3.1.286; 2026.
DR PRO; PR:P16691; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0008080; F:N-acetyltransferase activity; IDA:EcoCyc.
DR GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; IDA:EcoCyc.
DR GO; GO:0033051; P:aminophosphonate metabolic process; IMP:EcoCyc.
DR GO; GO:0018393; P:internal peptidyl-lysine acetylation; IMP:EcoCyc.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..144
FT /note="Aminoalkylphosphonate N-acetyltransferase"
FT /id="PRO_0000058401"
FT DOMAIN 4..144
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ SEQUENCE 144 AA; 16570 MW; B4BCBD253788737B CRC64;
MPACELRPAT QYDTDAVYAL ICELKQAEFD HHAFRVGFNA NLRDPNMRYH LALLDGEVVG
MIGLHLQFHL HHVNWIGEIQ ELVVMPQARG LNVGSKLLAW AEEEARQAGA EMTELSTNVK
RHDAHRFYLR EGYEQSHFRF TKAL
