PHNX_PSEP1
ID PHNX_PSEP1 Reviewed; 275 AA.
AC A5W696;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=Pput_3530;
OS Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=351746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT "Complete sequence of Pseudomonas putida F1.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in phosphonate degradation. {ECO:0000255|HAMAP-
CC Rule:MF_01375}.
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 -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01375}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. PhnX family.
CC {ECO:0000255|HAMAP-Rule:MF_01375}.
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DR EMBL; CP000712; ABQ79656.1; -; Genomic_DNA.
DR RefSeq; WP_003250077.1; NC_009512.1.
DR AlphaFoldDB; A5W696; -.
DR SMR; A5W696; -.
DR STRING; 351746.Pput_3530; -.
DR EnsemblBacteria; ABQ79656; ABQ79656; Pput_3530.
DR KEGG; ppf:Pput_3530; -.
DR eggNOG; COG0637; Bacteria.
DR HOGENOM; CLU_045011_12_0_6; -.
DR OMA; GRPAPWM; -.
DR OrthoDB; 1484726at2; -.
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; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR InterPro; IPR006323; Phosphonoacetald_hydro.
DR Pfam; PF13419; HAD_2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
DR TIGRFAMs; TIGR01422; phosphonatase; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Metal-binding; Schiff base.
FT CHAIN 1..275
FT /note="Phosphonoacetaldehyde hydrolase"
FT /id="PRO_1000068240"
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"
SQ SEQUENCE 275 AA; 30051 MW; 3E17780EDD2DDEB9 CRC64;
MNYNNPTQLQ AAILDWAGTV VDFGSFAPTQ IFVEAFAEFD VQVSIEEARG PMGMGKWDHI
RTLCDVPEIA ERYRKVFGRT PTDDDVTAIY NRFMPLQIEK IAVHSALIPG ALDTLTGLRQ
DGLKIGSCSG YPKVVMDKVV ELAAQNGYVA DHVVATDETP NGRPWPAQAL ANVIALGIDD
VAACVKVDDT VPGILEGRRA GMWTVALVCS GNALGLTWEG FRALSAEKLE SERQRIHALF
AGSRPHYLID TINDLPEVIA DINRRLAKGE MPQAF