ID H6N8Y6_9BACL Unreviewed; 265 AA.
AC H6N8Y6;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
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=PM3016_778 {ECO:0000313|EMBL:AFC27732.1};
OS Paenibacillus mucilaginosus 3016.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1116391 {ECO:0000313|EMBL:AFC27732.1, ECO:0000313|Proteomes:UP000007523};
RN [1] {ECO:0000313|EMBL:AFC27732.1, ECO:0000313|Proteomes:UP000007523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3016 {ECO:0000313|EMBL:AFC27732.1,
RC ECO:0000313|Proteomes:UP000007523};
RX PubMed=22535950; DOI=10.1128/JB.00323-12;
RA Ma M., Wang Z., Li L., Jiang X., Guan D., Cao F., Chen H., Wang X.,
RA Shen D., Du B., Li J.;
RT "Complete Genome Sequence of Paenibacillus mucilaginosus 3016, a Bacterium
RT Functional as Microbial Fertilizer.";
RL J. Bacteriol. 194:2777-2778(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}.
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DR EMBL; CP003235; AFC27732.1; -; Genomic_DNA.
DR RefSeq; WP_013914637.1; NC_016935.1.
DR AlphaFoldDB; H6N8Y6; -.
DR STRING; 1116391.PM3016_778; -.
DR KEGG; pmq:PM3016_778; -.
DR HOGENOM; CLU_045011_12_0_9; -.
DR Proteomes; UP000007523; 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; IPR023214; HAD_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR InterPro; IPR006323; Phosphonoacetald_hydro.
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; 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:AFC27732.1};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01375};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01375};
KW Reference proteome {ECO:0000313|Proteomes:UP000007523};
KW Schiff base {ECO:0000256|HAMAP-Rule:MF_01375}.
FT ACT_SITE 8
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01375"
FT ACT_SITE 49
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01375"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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 182
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01375"
SQ SEQUENCE 265 AA; 28824 MW; B4FA514ADAA871B2 CRC64;
MVQAVILDWA GTTVDYGSFA PVKAFMDTFA EEGVEVTAEE VRKPMGRLKI DHLRAICALD
RVAARWREVH GAEPGEADVQ RMYAAFEERL LGILPQYAEP VPGAVALAER LRERGIRIGS
TTGYTAEMMD IVAPEAQKRG YAPDVLVTPS EVAAGRPAPW MIYRNAEKLG VQEMHGMVKC
GDTFSDIEEG RRAGVWTAAV LLGSSELGLT QPEVLAEDPA ALAGRMERLA EAYREAGAHY
VIDTIGDLDA VVTDISARLA RGERP
//
