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Database: UniProt
Entry: A0A090SY22_9VIBR
LinkDB: A0A090SY22_9VIBR
Original site: A0A090SY22_9VIBR 
ID   A0A090SY22_9VIBR        Unreviewed;       169 AA.
AC   A0A090SY22;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Phosphonoacetaldehyde hydrolase {ECO:0000256|HAMAP-Rule:MF_01375};
DE            Short=Phosphonatase {ECO:0000256|HAMAP-Rule:MF_01375};
DE            EC=3.11.1.1 {ECO:0000256|HAMAP-Rule:MF_01375};
DE   AltName: Full=Phosphonoacetaldehyde phosphonohydrolase {ECO:0000256|HAMAP-Rule:MF_01375};
GN   Name=phnX {ECO:0000256|HAMAP-Rule:MF_01375};
GN   ORFNames=JCM19240_5249 {ECO:0000313|EMBL:GAL31818.1};
OS   Vibrio maritimus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=990268 {ECO:0000313|EMBL:GAL31818.1, ECO:0000313|Proteomes:UP000029224};
RN   [1] {ECO:0000313|EMBL:GAL31818.1, ECO:0000313|Proteomes:UP000029224}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 19240 {ECO:0000313|EMBL:GAL31818.1,
RC   ECO:0000313|Proteomes:UP000029224};
RA   Sawabe T., Meirelles P., Nakanishi M., Sayaka M., Hattori M., Ohkuma M.;
RT   "Vibrio maritimus JCM 19240. (C210) whole genome shotgun sequence.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GAL31818.1, ECO:0000313|Proteomes:UP000029224}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 19240 {ECO:0000313|EMBL:GAL31818.1,
RC   ECO:0000313|Proteomes:UP000029224};
RG   NBRP consortium;
RA   Sawabe T., Meirelles P., Nakanishi M., Sayaka M., Hattori M., Ohkuma M.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in phosphonate degradation. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01375};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01375};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01375};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01375}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. PhnX family.
CC       {ECO:0000256|HAMAP-Rule:MF_01375}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01375}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAL31818.1}.
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DR   EMBL; BBMT01000001; GAL31818.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A090SY22; -.
DR   Proteomes; UP000029224; Unassembled WGS sequence.
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   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   HAMAP; MF_01375; PhnX; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR023198; PGP-like_dom2.
DR   InterPro; IPR006323; Phosphonoacetald_hydro.
DR   PANTHER; PTHR43434; PHOSPHOGLYCOLATE PHOSPHATASE; 1.
DR   PANTHER; PTHR43434:SF26; PHOSPHONOACETALDEHYDE HYDROLASE; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01375, ECO:0000313|EMBL:GAL31818.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01375};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01375};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029224};
KW   Schiff base {ECO:0000256|HAMAP-Rule:MF_01375}.
FT   ACT_SITE        13
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01375"
FT   ACT_SITE        55
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01375"
FT   BINDING         13
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01375"
FT   BINDING         15
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01375"
SQ   SEQUENCE   169 AA;  18897 MW;  8F50286BD2F9334C CRC64;
     MSHSSPIQAV IFDWAGTIVD FGSFAPTSIF VEAFKQGFDF EISLDEAREP MGIGKWDHIK
     AVGQIPAVNA RWTAQFGQEM QDSDVDAIYA AFMPLQKAKV ADHAKPILNA VEVVNDLKHK
     GIKIGSCSGY PRQVMDVLIQ WRQITAINQT MSSQRMTCHK VAAQRHLWH
//
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