PHNX_SALTY
ID PHNX_SALTY Reviewed; 269 AA.
AC Q7ZAP3; P96059;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Phosphonoacetaldehyde hydrolase;
DE Short=Phosphonatase;
DE EC=3.11.1.1;
DE AltName: Full=Phosphonoacetaldehyde phosphonohydrolase;
GN Name=phnX; OrderedLocusNames=STM0432;
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 [GENOMIC DNA], PROTEIN SEQUENCE OF 1-9, BIOPHYSICAL
RP CHARACTERIZATION, REACTION MECHANISM, SCHIFF BASE, AND MUTAGENESIS OF
RP LYS-52.
RC STRAIN=LT2;
RX PubMed=9649311; DOI=10.1021/bi972677d;
RA Baker A.S., Ciocci M.J., Metcalf W.W., Kim J., Babbitt P.C., Wanner B.L.,
RA Martin B.M., Dunaway-Mariano D.;
RT "Insights into the mechanism of catalysis by the P-C bond-cleaving enzyme
RT phosphonoacetaldehyde hydrolase derived from gene sequence analysis and
RT mutagenesis.";
RL Biochemistry 37:9305-9315(1998).
RN [2]
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 [3]
RP CHARACTERIZATION, CLONING, AND INDUCTION.
RC STRAIN=LT2;
RX PubMed=7592415; DOI=10.1128/jb.177.22.6411-6421.1995;
RA Jiang W., Metcalf W.W., Lee K.-S., Wanner B.L.;
RT "Molecular cloning, mapping, and regulation of Pho regulon genes for
RT phosphonate breakdown by the phosphonatase pathway of Salmonella
RT typhimurium LT2.";
RL J. Bacteriol. 177:6411-6421(1995).
CC -!- FUNCTION: Involved in phosphonate degradation.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + phosphonoacetaldehyde = acetaldehyde + H(+) + phosphate;
CC Xref=Rhea:RHEA:18905, ChEBI:CHEBI:15343, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58383; EC=3.11.1.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=40 uM for phosphonoacetaldehyde (at pH 7.0, 25 degrees Celsius);
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- INDUCTION: Induced when inorganic phosphate is limiting; this is
CC controlled by PhoB. {ECO:0000269|PubMed:7592415}.
CC -!- MISCELLANEOUS: Maps to a phosphate-starvation-inducible locus
CC previously known as psiC.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. PhnX family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB39641.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAL19386.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U69493; AAB39641.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE006468; AAL19386.1; ALT_INIT; Genomic_DNA.
DR PIR; T46946; T46946.
DR RefSeq; NP_459427.1; NC_003197.2.
DR AlphaFoldDB; Q7ZAP3; -.
DR SMR; Q7ZAP3; -.
DR STRING; 99287.STM0432; -.
DR PaxDb; Q7ZAP3; -.
DR EnsemblBacteria; AAL19386; AAL19386; STM0432.
DR GeneID; 1251951; -.
DR KEGG; stm:STM0432; -.
DR PATRIC; fig|99287.12.peg.461; -.
DR HOGENOM; CLU_045011_12_0_6; -.
DR OMA; GRPAPWM; -.
DR PhylomeDB; Q7ZAP3; -.
DR BRENDA; 3.11.1.1; 5542.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050194; F:phosphonoacetaldehyde hydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019700; P:organic phosphonate catabolic process; IEA:InterPro.
DR CDD; cd02586; HAD_PHN; 1.
DR Gene3D; 1.10.150.240; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR HAMAP; MF_01375; PhnX; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR InterPro; IPR006323; Phosphonoacetald_hydro.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
DR TIGRFAMs; TIGR01422; phosphonatase; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome; Schiff base.
FT CHAIN 1..269
FT /note="Phosphonoacetaldehyde hydrolase"
FT /id="PRO_0000284601"
FT ACT_SITE 10
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 52
FT /note="Schiff-base intermediate with substrate"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MUTAGEN 52
FT /note="K->R: Complete loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:9649311"
FT CONFLICT 242..265
FT /note="AHYVVDSLADLPGVIAHINARLAQ -> RITWWIHWRIYL (in Ref. 1;
FT AAB39641)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 269 AA; 28574 MW; 0359B0E1124A3AF3 CRC64;
MNRIHAVILD WAGTTVDFGS FAPTQIFVEA FRQAFDVEIT LAEARVPMGL GKWQHIEALG
KLPAVDARWQ AKFGRSMSAA DIDAIYAAFM PLQIAKVVDF SSPIAGVIDT IAALRAEGIK
IGSCSGYPRA VMERLVPAAA GHGYRPDHWV ATDDLAAGGR PGPWMALQNV IALGIDAVAH
CVKVDDAAPG ISEGLNAGMW TVGLAVSGNE FGATWDAYQT MSKEDVAVRR EHAASKLYAA
GAHYVVDSLA DLPGVIAHIN ARLAQGERP
