ID   PHNHY_PSEFL             Reviewed;         407 AA.
AC   Q51782; Q50HR7; Q9R4G3;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Phosphonoacetate hydrolase {ECO:0000312|EMBL:AAC15507.1};
DE            EC=3.11.1.2;
GN   Name=phnA {ECO:0000312|EMBL:AAC15507.1};
OS   Pseudomonas fluorescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=294;
RN   [1] {ECO:0000312|EMBL:AAC15507.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RC   STRAIN=23F {ECO:0000312|EMBL:AAC15507.1};
RX   PubMed=9300819; DOI=10.1016/s0378-1119(97)00151-0;
RA   Kulakova A.N., Kulakov L.A., Quinn J.P.;
RT   "Cloning of the phosphonoacetate hydrolase gene from Pseudomonas
RT   fluorescens 23F encoding a new type of carbon-phosphorus bond cleaving
RT   enzyme and its expression in Escherichia coli and Pseudomonas putida.";
RL   Gene 195:49-53(1997).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:CAI93864.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=R3e {ECO:0000312|EMBL:CAI93864.1};
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).
RN   [3] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 2-20, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY
RP   REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=23F {ECO:0000269|PubMed:8529644};
RX   PubMed=8529644; DOI=10.1111/j.1432-1033.1995.225_c.x;
RA   McGrath J.W., Wisdom G.B., McMullan G., Larkin M.J., Quinn J.P.;
RT   "The purification and properties of phosphonoacetate hydrolase, a novel
RT   carbon-phosphorus bond-cleavage enzyme from Pseudomonas fluorescens 23F.";
RL   Eur. J. Biochem. 234:225-230(1995).
RN   [4] {ECO:0000305}
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND INDUCTION.
RC   STRAIN=23F {ECO:0000269|PubMed:8288524};
RX   PubMed=8288524; DOI=10.1128/jb.176.2.320-324.1994;
RA   McMullan G., Quinn J.P.;
RT   "In vitro characterization of a phosphate starvation-independent carbon-
RT   phosphorus bond cleavage activity in Pseudomonas fluorescens 23F.";
RL   J. Bacteriol. 176:320-324(1994).
RN   [5] {ECO:0000305}
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 4-407, AND ZINC-BINDING.
RC   STRAIN=23F {ECO:0000269|Ref.5};
RA   Holden H.M., Benning M.M., Dunaway-Mariano D., Kim A.D.;
RT   "Crystal structure of phosphonoacetate hydrolase complexed with
RT   phosphonoformate.";
RL   Submitted (FEB-2000) to the PDB data bank.
CC   -!- FUNCTION: Specifically hydrolyzes phosphonoacetate. Does not have
CC       activity on other organophosphonates or acetates.
CC       {ECO:0000269|PubMed:8288524}.
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:0000269|PubMed:8288524, ECO:0000269|PubMed:8529644,
CC         ECO:0000269|PubMed:9300819};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:8529644, ECO:0000269|Ref.5};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:8529644,
CC       ECO:0000269|Ref.5};
CC   -!- ACTIVITY REGULATION: Completely inhibited by EDTA and 1,10-
CC       phenanthroline. Moderately inhibited by the phosphonocarboxylic acids
CC       phosphonoformate and 3-phosphonopropionate and the phosphonate
CC       herbicide glyphosate. Partially inhibited by the reducing agents sodium
CC       sulfide and dithiotheitol and the chelating agent iminodiacetate.
CC       Nonphosphonate analogs of phosphonoacetate, such as arsonoacetate,
CC       sulfonoacetate and malonate are poor inhibitors. Inorganic phosphate,
CC       acetate and the known phosphonotase inhibitor phosphite have little
CC       effect on activity. Not inhibited by the alkylphosphonic acids
CC       methylphosphonate and ethylphosphonate, or the aminoalkylphosphonates
CC       2-aminoethylphosphonate, 3-aminopropylphosphonate and 4-
CC       aminobutylphosphonate. Fe(3+), Ca(2+), Mg(2+) and Cs(+) have no effect
CC       on activity. Activity is slightly increased by the
CC       aminoalkylphosphonates 1-aminoethylphosphonate, 1-
CC       aminobutylphosphonate, 2-amino-4-butylphosphonate. Activity is
CC       increased by Zn(2+), Mn(2+) and Co(2+), these 3 metal ions also allow
CC       recovery of activity after EDTA treatment. {ECO:0000269|PubMed:8288524,
CC       ECO:0000269|PubMed:8529644}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.25 mM for phosphonoacetate {ECO:0000269|PubMed:8529644};
CC         Vmax=1.25 umol/min/mg enzyme {ECO:0000269|PubMed:8529644};
CC       pH dependence:
CC         Optimum pH is approximately 7.8. {ECO:0000269|PubMed:8529644};
CC       Temperature dependence:
CC         Optimum temperature is 37 degrees Celsius. Activity is rapidly lost
CC         after incubation for 30 minutes above 40 degrees Celsius.
CC         {ECO:0000269|PubMed:8529644};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8529644}.
CC   -!- INDUCTION: By phosphonoacetate. {ECO:0000269|PubMed:8288524}.
CC   -!- SIMILARITY: Belongs to the alkaline phosphatase family. PhnA subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L49465; AAC15507.1; -; Genomic_DNA.
DR   EMBL; AJ969111; CAI93864.1; -; Genomic_DNA.
DR   PIR; S63510; S63510.
DR   PDB; 1EI6; X-ray; 2.10 A; A/B/C/D=2-407.
DR   PDBsum; 1EI6; -.
DR   AlphaFoldDB; Q51782; -.
DR   SMR; Q51782; -.
DR   DrugBank; DB01694; D-tartaric acid.
DR   KEGG; ag:AAC15507; -.
DR   BioCyc; MetaCyc:MON-202; -.
DR   BRENDA; 3.11.1.2; 5121.
DR   EvolutionaryTrace; Q51782; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0047400; F:phosphonoacetate hydrolase activity; IDA:UniProtKB.
DR   GO; GO:0019636; P:phosphonoacetate metabolic process; IDA: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   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Hydrolase; Metal-binding; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8529644"
FT   CHAIN           2..407
FT                   /note="Phosphonoacetate hydrolase"
FT                   /evidence="ECO:0000269|PubMed:8529644"
FT                   /id="PRO_0000402579"
FT   BINDING         25
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|Ref.5"
FT   BINDING         64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|Ref.5"
FT   BINDING         64
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|Ref.5"
FT   BINDING         202
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|Ref.5"
FT   BINDING         202
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|Ref.5"
FT   BINDING         206
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|Ref.5"
FT   BINDING         241
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|Ref.5"
FT   BINDING         242
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|Ref.5"
FT   BINDING         242
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|Ref.5"
FT   BINDING         368
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|Ref.5"
FT   BINDING         368
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|Ref.5"
FT   CONFLICT        6
FT                   /note="S -> N (in Ref. 2; CAI93864)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        265
FT                   /note="A -> T (in Ref. 2; CAI93864)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        380
FT                   /note="F -> V (in Ref. 2; CAI93864)"
FT                   /evidence="ECO:0000305"
FT   STRAND          4..7
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   STRAND          10..13
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   STRAND          19..23
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   HELIX           29..37
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   HELIX           42..46
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   HELIX           47..49
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   STRAND          51..57
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   HELIX           64..73
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   HELIX           77..80
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   STRAND          84..89
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   TURN            90..93
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   STRAND          94..97
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   HELIX           101..103
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   HELIX           109..115
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   STRAND          120..126
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   HELIX           127..133
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   TURN            134..136
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   STRAND          139..144
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   HELIX           152..155
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   HELIX           160..164
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   STRAND          171..173
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   HELIX           175..189
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   STRAND          194..199
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   HELIX           203..207
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   HELIX           213..231
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   STRAND          235..239
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   STRAND          256..258
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   HELIX           259..267
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   STRAND          271..275
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   HELIX           286..288
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   STRAND          290..297
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   HELIX           303..311
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   STRAND          316..321
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   HELIX           322..329
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   HELIX           333..335
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   STRAND          338..343
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   STRAND          348..351
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   TURN            353..355
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   HELIX           358..360
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   HELIX           371..373
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   STRAND          375..382
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   HELIX           395..397
FT                   /evidence="ECO:0007829|PDB:1EI6"
FT   HELIX           398..404
FT                   /evidence="ECO:0007829|PDB:1EI6"
SQ   SEQUENCE   407 AA;  44239 MW;  B706D4A07C42C795 CRC64;
     MTQLISVNSR SYRLSSAPTI VICVDGCEQE YINQAIQAGQ APFLAELTGF GTVLTGDCVV
     PSFTNPNNLS IVTGAPPSVH GICGNFFFDQ ETQEEVLMND AKYLRAPTIL AEMAKAGQLV
     AVVTAKDKLR NLLGHQLKGI CFSAEKADQV NLEEHGVENI LARVGMPVPS VYSADLSEFV
     FAAGLSLLTN ERPDFMYLST TDYVQHKHAP GTPEANAFYA MMDSYFKRYH EQGAIVAITA
     DHGMNAKTDA IGRPNILFLQ DLLDAQYGAQ RTRVLLPITD PYVVHHGALG SYATVYLRDA
     VPQRDAIDFL AGIAGVEAVL TRSQACQRFE LPEDRIGDLV VLGERLTVLG SAADKHDLSG
     LTVPLRSHGG VSEQKVPLIF NRKLVGLDSP GRLRNFDIID LALNHLA