ID   PHNHY_PSEPU             Reviewed;         407 AA.
AC   Q50HR6;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Phosphonoacetate hydrolase {ECO:0000312|EMBL:CAI93865.1};
DE            EC=3.11.1.2;
GN   Name=phnA {ECO:0000312|EMBL:CAI93865.1};
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAI93865.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=3b {ECO:0000312|EMBL:CAI93865.1};
RX   PubMed=16623750; DOI=10.1111/j.1462-2920.2005.00974.x;
RA   Panas P., Ternan N.G., Dooley J.S., McMullan G.;
RT   "Detection of phosphonoacetate degradation and phnA genes in soil bacteria
RT   from distinct geographical origins suggest its possible biogenic origin.";
RL   Environ. Microbiol. 8:939-945(2006).
CC   -!- FUNCTION: Specifically hydrolyzes phosphonoacetate. Does not have
CC       activity on other organophosphonates or acetates (By similarity).
CC       {ECO:0000250|UniProtKB:Q51782}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + phosphonoacetate = acetate + H(+) + phosphate;
CC         Xref=Rhea:RHEA:16749, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30089, ChEBI:CHEBI:43474, ChEBI:CHEBI:57488; EC=3.11.1.2;
CC         Evidence={ECO:0000250|UniProtKB:Q51782};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q51782};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q51782};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q51782}.
CC   -!- SIMILARITY: Belongs to the alkaline phosphatase family. PhnA subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AJ969112; CAI93865.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q50HR6; -.
DR   SMR; Q50HR6; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0047400; F:phosphonoacetate hydrolase activity; ISS:UniProtKB.
DR   GO; GO:0019636; P:phosphonoacetate metabolic process; ISS:UniProtKB.
DR   Gene3D; 3.30.1360.110; -; 1.
DR   Gene3D; 3.40.720.10; -; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR002591; Phosphodiest/P_Trfase.
DR   InterPro; IPR012710; Phosphonoacetate_hydro.
DR   InterPro; IPR023116; Phosphonoacetate_hydro_insert.
DR   Pfam; PF01663; Phosphodiest; 1.
DR   SUPFAM; SSF53649; SSF53649; 1.
DR   TIGRFAMs; TIGR02335; hydr_PhnA; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q51782"
FT   CHAIN           2..407
FT                   /note="Phosphonoacetate hydrolase"
FT                   /evidence="ECO:0000250|UniProtKB:Q51782"
FT                   /id="PRO_0000402580"
FT   BINDING         25
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q51782"
FT   BINDING         64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q51782"
FT   BINDING         64
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q51782"
FT   BINDING         202
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q51782"
FT   BINDING         202
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q51782"
FT   BINDING         206
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q51782"
FT   BINDING         241
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q51782"
FT   BINDING         242
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q51782"
FT   BINDING         242
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q51782"
FT   BINDING         368
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q51782"
FT   BINDING         368
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q51782"
SQ   SEQUENCE   407 AA;  44418 MW;  28FC71FA32667346 CRC64;
     MTQLINVNSR SYRLSSAPTI VICVDGCEQE YINQAIQAGQ APFLAELTDF GTVLTGDCVV
     PSFTNPNNLS IVTGAPPSVH GICGNFFFDQ ETQEEVLMND AKYLRAPTIL AEMAKAGQLV
     AVVTAKDKLR NLLGHQLKGI CFSAEKADQV SLEEHGVENI LARVGMPVPS VYSADLSEFV
     FAAGLSLLIN ERPDFMYLST TDYVQHKHAP GTPEANAFYA MMDSYFKRYH EQGAIVAITA
     DHGMNAKTDA IGRPNILFLQ DLLDAQYGAQ RTRVLLPITD PYVVHHGALG SYATVYLRDA
     VPQRDAIDFL AGIAGVEAVL TRSQACQRFE LPEDRIGDLV VLGERLTVLG SAADKHDLSG
     LTVPLRSHGG VSEQKVPLIF NRKLVGLDSF DRLRNFDIID LALNHLA