PHNO_SALTY
ID PHNO_SALTY Reviewed; 154 AA.
AC Q8ZKE6;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Aminoalkylphosphonate N-acetyltransferase {ECO:0000303|PubMed:16503658};
DE EC=2.3.1.280 {ECO:0000269|PubMed:16503658};
GN Name=phnO {ECO:0000303|PubMed:16503658, ECO:0000312|EMBL:AAL23111.1};
GN OrderedLocusNames=STM4287 {ECO:0000312|EMBL:AAL23111.1};
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM, MASS SPECTROMETRY,
RP CLEAVAGE OF INITIATOR METHIONINE, AND SUBUNIT.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=16503658; DOI=10.1021/bi052297p;
RA Errey J.C., Blanchard J.S.;
RT "Functional annotation and kinetic characterization of PhnO from Salmonella
RT enterica.";
RL Biochemistry 45:3033-3039(2006).
CC -!- FUNCTION: Aminoalkylphosphonate N-acetyltransferase which is able to
CC acetylate a range of aminoalkylphosphonic acids, including (S)-1-
CC aminoethylphosphonate ((S)-1AEP) and 2-aminoethylphosphonate, using
CC acetyl-CoA as acetyl donor. Its physiological role in S.typhimurium is
CC unclear. However, by acetylating (S)-1AEP, PhnO would protect against
CC the deleterious effects of (S)-1AEP, a structural analog of D-alanine
CC that has antibacterial properties. {ECO:0000269|PubMed:16503658}.
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:16503658};
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:16503658};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:16503658};
CC Note=Requires a divalent metal ion for activity. In vitro, exhibits a
CC preference for Ni(2+) followed by Mn(2+) and very poor activity with
CC Mg(2+). However, it is unclear what the physiologically relevant metal
CC ion is. {ECO:0000269|PubMed:16503658};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.06 mM for acetyl-CoA (in the presence of Ni(2+))
CC {ECO:0000269|PubMed:16503658};
CC KM=0.07 mM for propionyl-CoA (in the presence of Ni(2+))
CC {ECO:0000269|PubMed:16503658};
CC KM=0.05 mM for malonyl-CoA (in the presence of Ni(2+))
CC {ECO:0000269|PubMed:16503658};
CC KM=1.7 mM for aminomethylphosphonate (in the presence of Ni(2+))
CC {ECO:0000269|PubMed:16503658};
CC KM=1.8 mM for 2-aminoethylphosphonate (in the presence of Ni(2+))
CC {ECO:0000269|PubMed:16503658};
CC KM=4.0 mM for 3-aminopropylphosphonate (in the presence of Ni(2+))
CC {ECO:0000269|PubMed:16503658};
CC KM=13.0 mM for 4-aminobutylphosphonate (in the presence of Ni(2+))
CC {ECO:0000269|PubMed:16503658};
CC KM=0.17 mM for (S)-1-aminoethylphosphonate (in the presence of
CC Ni(2+)) {ECO:0000269|PubMed:16503658};
CC KM=0.30 mM for (S)-1-aminoethylphosphonate (in the presence of
CC Mn(2+)) {ECO:0000269|PubMed:16503658};
CC KM=0.28 mM for (S)-1-aminoethylphosphonate (in the presence of
CC Co(2+)) {ECO:0000269|PubMed:16503658};
CC KM=2.00 mM for (S)-1-aminoethylphosphonate (in the presence of
CC Mg(2+)) {ECO:0000269|PubMed:16503658};
CC KM=4.1 mM for 1-aminopropylphosphonate (in the presence of Ni(2+))
CC {ECO:0000269|PubMed:16503658};
CC KM=12.5 mM for 1-aminobutylphosphonate (in the presence of Ni(2+))
CC {ECO:0000269|PubMed:16503658};
CC KM=18.9 mM for 2-aminoethanesulfonate (in the presence of Ni(2+))
CC {ECO:0000269|PubMed:16503658};
CC KM=16.4 mM for 2-aminoethanesulfinate (in the presence of Ni(2+))
CC {ECO:0000269|PubMed:16503658};
CC Note=kcat is 13.1 sec(-1) for the acetylation of (S)-1AEP. kcat is
CC 14.7 sec(-1) for the propionylation of (S)-1AEP. kcat is 0.4 sec(-1)
CC for the malonylation of (S)-1AEP. kcat is 7.0 sec(-1) for the
CC acetylation of aminomethylphosphonate. kcat is 9.0 sec(-1) for the
CC acetylation of 2-aminoethylphosphonate. kcat is 5.4 sec(-1) for the
CC acetylation of 3-aminopropylphosphonate. kcat is 0.5 sec(-1) for the
CC acetylation of 4-aminobutylphosphonate. kcat is 7.4 sec(-1) for the
CC acetylation of 1-aminopropylphosphonate. kcat is 1.0 sec(-1) for the
CC acetylation of 1-aminobutylphosphonate. kcat is 14.8 sec(-1) for the
CC acetylation of 2-aminoethanesulfonate. kcat is 20 sec(-1) for the
CC acetylation of 2-aminoethanesulfinate (in the presence of Ni(2+)).
CC {ECO:0000269|PubMed:16503658};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16503658}.
CC -!- MASS SPECTROMETRY: Mass=16499; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:16503658};
CC -!- MISCELLANEOUS: Reaction proceeds via an ordered, sequential kinetic
CC mechanism with AcCoA binding first followed by aminoalkylphosphonate.
CC {ECO:0000269|PubMed:16503658}.
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DR EMBL; AE006468; AAL23111.1; -; Genomic_DNA.
DR RefSeq; NP_463152.3; NC_003197.2.
DR RefSeq; WP_000602438.1; NC_003197.2.
DR AlphaFoldDB; Q8ZKE6; -.
DR SMR; Q8ZKE6; -.
DR STRING; 99287.STM4287; -.
DR PaxDb; Q8ZKE6; -.
DR EnsemblBacteria; AAL23111; AAL23111; STM4287.
DR GeneID; 1255813; -.
DR KEGG; stm:STM4287; -.
DR HOGENOM; CLU_013985_34_6_6; -.
DR OMA; ASHVGFK; -.
DR PhylomeDB; Q8ZKE6; -.
DR BioCyc; SENT99287:STM4287-MON; -.
DR BRENDA; 2.3.1.280; 5542.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:16503658"
FT CHAIN 2..154
FT /note="Aminoalkylphosphonate N-acetyltransferase"
FT /id="PRO_0000437189"
FT DOMAIN 14..154
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ SEQUENCE 154 AA; 17933 MW; F69DBA133D511744 CRC64;
MILMRRREDV MPVCELRHAT TEDTDSVYAL ICELLKNELD YQAFRDGFAA NLLDPNVHYR
LALRNGEVVG MISLHMQFHL HHANWIGEIQ ELVVLPPMRG QKIGSQLLAW AEEEARQAGA
ELTELSTNIK RRDAHRFYLR EGYKQSHFRF TKAL
