PHNX_DESVM
ID PHNX_DESVM Reviewed; 280 AA.
AC B8DKP2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=DvMF_0514;
OS Desulfovibrio vulgaris (strain DSM 19637 / Miyazaki F).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=883;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19637 / Miyazaki F;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hazen T.C.,
RA Richardson P.;
RT "Complete sequence of Desulfovibrio vulgaris str. 'Miyazaki F'.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001197; ACL07471.1; -; Genomic_DNA.
DR RefSeq; WP_012611663.1; NC_011769.1.
DR AlphaFoldDB; B8DKP2; -.
DR SMR; B8DKP2; -.
DR STRING; 883.DvMF_0514; -.
DR EnsemblBacteria; ACL07471; ACL07471; DvMF_0514.
DR KEGG; dvm:DvMF_0514; -.
DR eggNOG; COG0637; Bacteria.
DR HOGENOM; CLU_045011_12_0_7; -.
DR OMA; GRPAPWM; -.
DR OrthoDB; 1484726at2; -.
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; IPR006439; HAD-SF_hydro_IA.
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; TIGR01549; HAD-SF-IA-v1; 1.
DR TIGRFAMs; TIGR01422; phosphonatase; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Metal-binding; Schiff base.
FT CHAIN 1..280
FT /note="Phosphonoacetaldehyde hydrolase"
FT /id="PRO_1000144832"
FT ACT_SITE 20
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
FT ACT_SITE 61
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
FT BINDING 20
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
FT BINDING 22
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
FT BINDING 194
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
SQ SEQUENCE 280 AA; 30244 MW; 102D065062AACB1E CRC64;
MKPFLRTRVY DGPVRAVVLD WAGTAVDHGC LGPAAVFVQA FALHGVEVAV SEAREPMGSE
KREHVRRMLA MDSVAARWRA VHGHVPHEAD VDAVYRDVEP LMLQTIAAHA VPVPGLAEFV
DRVRGRGMGL GSCTGYTGPM MEVLVPEAAR RGYSPDVVVH ASEVPAGRPY PWMCYLNAMR
LGVHPMESMV KIGDTVADMH EARNAGMWTV GVVRTGNDVG LSEVDAARMP PDQLAARMTV
AAARLREAGA HYVVDSIADC FSVIKAIEAR LARGDTPYPA