PHNX_PARXL
ID PHNX_PARXL Reviewed; 267 AA.
AC Q13YI8;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Phosphonoacetaldehyde hydrolase {ECO:0000255|HAMAP-Rule:MF_01375};
DE Short=Phosphonatase {ECO:0000255|HAMAP-Rule:MF_01375};
DE EC=3.11.1.1 {ECO:0000255|HAMAP-Rule:MF_01375};
DE AltName: Full=Phosphonoacetaldehyde phosphonohydrolase {ECO:0000255|HAMAP-Rule:MF_01375};
GN Name=phnX {ECO:0000255|HAMAP-Rule:MF_01375}; OrderedLocusNames=Bxeno_A2313;
GN ORFNames=Bxe_A2117;
OS Paraburkholderia xenovorans (strain LB400).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=266265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LB400;
RX PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT shaped for versatility.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC -!- FUNCTION: Involved in phosphonate degradation. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01375};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01375};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01375};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01375}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. PhnX family.
CC {ECO:0000255|HAMAP-Rule:MF_01375}.
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DR EMBL; CP000270; ABE30851.1; -; Genomic_DNA.
DR RefSeq; WP_011488465.1; NZ_CP008760.1.
DR AlphaFoldDB; Q13YI8; -.
DR SMR; Q13YI8; -.
DR STRING; 266265.Bxe_A2117; -.
DR EnsemblBacteria; ABE30851; ABE30851; Bxe_A2117.
DR KEGG; bxb:DR64_4272; -.
DR KEGG; bxe:Bxe_A2117; -.
DR PATRIC; fig|266265.5.peg.2421; -.
DR eggNOG; COG0637; Bacteria.
DR OMA; GRPAPWM; -.
DR OrthoDB; 1484726at2; -.
DR Proteomes; UP000001817; Chromosome 1.
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; 1.10.150.240; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR HAMAP; MF_01375; PhnX; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR InterPro; IPR006323; Phosphonoacetald_hydro.
DR Pfam; PF13419; HAD_2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01422; phosphonatase; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome; Schiff base.
FT CHAIN 1..267
FT /note="Phosphonoacetaldehyde hydrolase"
FT /id="PRO_0000284587"
FT ACT_SITE 10
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
FT ACT_SITE 51
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
FT BINDING 12
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
FT BINDING 184
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
SQ SEQUENCE 267 AA; 28358 MW; AB50CDAD236F0F83 CRC64;
MKHVKAVIFD WAGTVVDYGS LAPMGAFVET FGQFGVPITI DEARGPMGMA KRPHIAALMA
LPRVAQAWTD KYGHAPDDAD IDAVYDVFVP KNIAVAASYS SVIPGVADVA SALRGDDIRI
GTTTGYTREI MAEIVPGAAA QGFSPDSIVC TGDTAEGRPS PYMIYRTLPE LGVWRAKEAI
KVDDTEVGIE EGINGGTWTV GVSVSGNAFG MAEGDVKALA PDEFAWRRNA AIQKLQAAGA
HYVIDSVADL MPVVYDIEAR LARGERP