ID C3GFZ9_BACTU Unreviewed; 267 AA.
AC C3GFZ9;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
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=bthur0010_11730 {ECO:0000313|EMBL:EEM78843.1};
OS Bacillus thuringiensis serovar pondicheriensis BGSC 4BA1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=527029 {ECO:0000313|EMBL:EEM78843.1};
RN [1] {ECO:0000313|EMBL:EEM78843.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGSC 4BA1 {ECO:0000313|EMBL:EEM78843.1};
RX PubMed=22645259; DOI=10.1101/gr.134437.111;
RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A.,
RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K.,
RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.;
RT "Genomic characterization of the Bacillus cereus sensu lato species:
RT Backdrop to the evolution of Bacillus anthracis.";
RL Genome Res. 22:1512-1524(2012).
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: 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:EEM78843.1}.
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; ACNH01000028; EEM78843.1; -; Genomic_DNA.
DR AlphaFoldDB; C3GFZ9; -.
DR HOGENOM; CLU_045011_12_0_9; -.
DR Proteomes; UP000006660; Chromosome.
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; 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; TIGR01549; HAD-SF-IA-v1; 1.
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; SFLDG01135; C1.5.6:_HAD__Beta-PGM__Phospha; 1.
DR SFLD; SFLDF00038; phosphonoacetaldehyde_hydrolas; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01375};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01375};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01375};
KW Pyruvate {ECO:0000313|EMBL:EEM78843.1};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP-
KW Rule:MF_01375}.
FT ACT_SITE 12
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01375"
FT ACT_SITE 53
FT /note="Schiff-base intermediate with substrate"
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 14
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 267 AA; 30381 MW; E6ABD86D0515C47B CRC64;
MDCMKIEAVI FDWAGTTVDY GCFAPLEVFM EIFHKRGVGI TAEEARKPMG LLKIDHVRAL
TEMPRIANEW NRIFGQLPTE TDIQEMYEEF EEILFAILPR YASPIHGVKE VIASLRERGI
KIGSTTGYTR EMMDIVAKEA ALQGYKPDFL VTPDDVPAGR PYPWMCYKNA MELGVYPMNH
MIKIGDTVSD MKEGRNAGMW TVGVILGSSE LGLSEEEVEN MDSAELREKI EVVRNRFVEN
GAHFTIETMQ ELESVMERIE KQELIIS
//
