PHNX_PSEAE
ID PHNX_PSEAE Reviewed; 275 AA.
AC Q9I433; Q51386;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Phosphonoacetaldehyde hydrolase {ECO:0000255|HAMAP-Rule:MF_01375};
DE Short=Phosphonatase {ECO:0000255|HAMAP-Rule:MF_01375};
DE EC=3.11.1.1 {ECO:0000255|HAMAP-Rule:MF_01375};
DE AltName: Full=Phosphonoacetaldehyde phosphonohydrolase {ECO:0000255|HAMAP-Rule:MF_01375};
GN Name=phnX {ECO:0000255|HAMAP-Rule:MF_01375}; OrderedLocusNames=PA1311;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-20, AND
RP CHARACTERIZATION.
RC STRAIN=A237;
RX PubMed=9332393; DOI=10.1016/s0378-1119(97)00185-6;
RA Dumora C., Marche M., Doignon F., Aigle M., Cassaigne A., Crouzet M.;
RT "First characterization of the phosphonoacetaldehyde hydrolase gene of
RT Pseudomonas aeruginosa.";
RL Gene 197:405-412(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP INDUCTION, CHARACTERIZATION, ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=A237;
RX PubMed=2504289; DOI=10.1016/0167-4838(89)90186-6;
RA Dumora C., Lacoste A.-M., Cassaigne A.;
RT "Phosphonoacetaldehyde hydrolase from Pseudomonas aeruginosa: purification
RT properties and comparison with Bacillus cereus enzyme.";
RL Biochim. Biophys. Acta 997:193-198(1989).
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 Evidence={ECO:0000255|HAMAP-Rule:MF_01375};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01375};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01375};
CC -!- ACTIVITY REGULATION: Inhibited by phosphite, moderately inhibited by
CC phosphonic acids, the corresponding aminophosphonic acids activate the
CC enzyme. {ECO:0000269|PubMed:2504289}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=210 uM for 2-phosphonoacetaldehyde {ECO:0000269|PubMed:2504289,
CC ECO:0000269|PubMed:9332393};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01375,
CC ECO:0000269|PubMed:2504289}.
CC -!- INDUCTION: By 2-aminoethylphosphonic acid.
CC {ECO:0000269|PubMed:2504289}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. PhnX family.
CC {ECO:0000255|HAMAP-Rule:MF_01375}.
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DR EMBL; U45309; AAC45742.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG04700.1; -; Genomic_DNA.
DR PIR; C83482; C83482.
DR RefSeq; NP_250002.1; NC_002516.2.
DR RefSeq; WP_003112369.1; NZ_QZGE01000005.1.
DR AlphaFoldDB; Q9I433; -.
DR SMR; Q9I433; -.
DR STRING; 287.DR97_483; -.
DR PaxDb; Q9I433; -.
DR PRIDE; Q9I433; -.
DR DNASU; 881484; -.
DR EnsemblBacteria; AAG04700; AAG04700; PA1311.
DR GeneID; 881484; -.
DR KEGG; pae:PA1311; -.
DR PATRIC; fig|208964.12.peg.1362; -.
DR PseudoCAP; PA1311; -.
DR HOGENOM; CLU_045011_12_0_6; -.
DR InParanoid; Q9I433; -.
DR OMA; TWPGILE; -.
DR PhylomeDB; Q9I433; -.
DR BioCyc; MetaCyc:PHNXPSEUDO-MON; -.
DR BioCyc; PAER208964:G1FZ6-1336-MON; -.
DR BRENDA; 3.11.1.1; 5087.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050194; F:phosphonoacetaldehyde hydrolase activity; IDA:PseudoCAP.
DR GO; GO:0019700; P:organic phosphonate catabolic process; IDA:PseudoCAP.
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..275
FT /note="Phosphonoacetaldehyde hydrolase"
FT /id="PRO_0000284591"
FT ACT_SITE 15
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
FT ACT_SITE 56
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
FT BINDING 15
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
FT BINDING 17
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
FT BINDING 189
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
FT CONFLICT 222
FT /note="Q -> K (in Ref. 1; AAC45742)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 275 AA; 29929 MW; CA886B7B7760257A CRC64;
MNYNQPATLQ AAILDWAGTV VDFGSFAPTQ IFVEAFAEFG VQVSLEEARG PMGMGKWDHI
RTLCDIPAIA ERYRAVFGRL PSDDDVTAIY ERFMPLQIEK IAEHSALIPG ALQAIAELRG
MGLKIGSCSG YPAVVMEKVV ALAETNGYVA DHVVATDEVP NGRPWPAQAL ANVIALGIDD
VAACVKVDDT WPGILEGRRA GMWTVALTCS GNALGLTYEQ YQALPAAELE RERTRIEQMF
EGSRPHYLIE TIAELPAVVR DINARLARGE MPQGN
