ID A0A0S2K0V6_9GAMM Unreviewed; 269 AA.
AC A0A0S2K0V6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=PP2015_1426 {ECO:0000313|EMBL:ALO41931.1};
OS Pseudoalteromonas phenolica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=161398 {ECO:0000313|EMBL:ALO41931.1, ECO:0000313|Proteomes:UP000061457};
RN [1] {ECO:0000313|EMBL:ALO41931.1, ECO:0000313|Proteomes:UP000061457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 12086 {ECO:0000313|EMBL:ALO41931.1,
RC ECO:0000313|Proteomes:UP000061457};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) 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}.
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DR EMBL; CP013187; ALO41931.1; -; Genomic_DNA.
DR RefSeq; WP_058029627.1; NZ_CP013187.1.
DR AlphaFoldDB; A0A0S2K0V6; -.
DR STRING; 161398.PP2015_1426; -.
DR KEGG; pphe:PP2015_1426; -.
DR PATRIC; fig|161398.10.peg.1451; -.
DR OrthoDB; 9758757at2; -.
DR Proteomes; UP000061457; Chromosome I.
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; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR InterPro; IPR006323; Phosphonoacetald_hydro.
DR NCBIfam; TIGR01509; HAD-SF-IA-v3; 1.
DR NCBIfam; TIGR01422; phosphonatase; 1.
DR PANTHER; PTHR43434; PHOSPHOGLYCOLATE PHOSPHATASE; 1.
DR PANTHER; PTHR43434:SF26; PHOSPHONOACETALDEHYDE HYDROLASE; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01375, ECO:0000313|EMBL:ALO41931.1};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01375};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01375};
KW Reference proteome {ECO:0000313|Proteomes:UP000061457};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP-
KW Rule:MF_01375}.
FT ACT_SITE 10
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01375"
FT ACT_SITE 52
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01375"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01375"
FT BINDING 12
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01375"
FT BINDING 186
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01375"
SQ SEQUENCE 269 AA; 29198 MW; 7EC47124BFFC7B9C CRC64;
MKHIEALILD WAGTVVDYGS IAPTSIFVEA FKQGFDFEIS LEEARGPMGM GKWDHIHALL
NTGSIQVRWQ NQFGRLPNQE DVDQIYNTFM PLQQAKVADR AAPIEGVLPV IHRLQSDNVK
IGSCSGYPKP VMDVLVPAAT EYGYKPDCVV ASDECEAGSR PGPWMALENV QKLGISRVSA
CVKVDDSVHG ISEGLNAGMW TVGIAITGNA IGLSEQEWAD ESEASQVALT RKAYAQLASA
GAHYVIDSLA DIEPILHVIE ARIARGERP
//
