(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 104.
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};
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   SMR; Q7ZAP3; -.
DR   PaxDb; Q7ZAP3; -.
DR   PRIDE; Q7ZAP3; -.
DR   EnsemblBacteria; AAL19386; AAL19386; STM0432.
DR   GeneID; 1251951; -.
DR   KEGG; stm:STM0432; -.
DR   PATRIC; fig|99287.12.peg.461; -.
DR   eggNOG; ENOG4108KAZ; Bacteria.
DR   eggNOG; COG0637; LUCA.
DR   HOGENOM; HOG000217971; -.
DR   KO; K05306; -.
DR   OMA; GRPAPWM; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050194; F:phosphonoacetaldehyde hydrolase activity; IBA:GO_Central.
DR   GO; GO:0019700; P:organic phosphonate catabolic process; IBA:GO_Central.
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;
DR   PRODOM; Q7ZAP3.
DR   SWISS-2DPAGE; Q7ZAP3.
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   METAL           10
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250"
FT   METAL           12
FT                   /note="Magnesium; via carbonyl oxygen"
FT                   /evidence="ECO:0000250"
FT   METAL           186
FT                   /note="Magnesium"
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
//

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