PHNX_VIBC3
ID PHNX_VIBC3 Reviewed; 271 AA.
AC A5F051; C3M5Y0;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
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};
GN OrderedLocusNames=VC0395_0548, VC395_A0709;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
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; CP000626; ABQ18775.1; -; Genomic_DNA.
DR EMBL; CP001236; ACP11543.1; -; Genomic_DNA.
DR RefSeq; WP_001889086.1; NZ_JAACZH010000032.1.
DR AlphaFoldDB; A5F051; -.
DR SMR; A5F051; -.
DR STRING; 345073.VC395_A0709; -.
DR EnsemblBacteria; ABQ18775; ABQ18775; VC0395_0548.
DR KEGG; vco:VC0395_0548; -.
DR KEGG; vcr:VC395_A0709; -.
DR PATRIC; fig|345073.21.peg.3443; -.
DR eggNOG; COG0637; Bacteria.
DR HOGENOM; CLU_045011_12_0_6; -.
DR OMA; GRPAPWM; -.
DR Proteomes; UP000000249; 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; 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; TIGR01509; HAD-SF-IA-v3; 1.
DR TIGRFAMs; TIGR01422; phosphonatase; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Metal-binding; Schiff base.
FT CHAIN 1..271
FT /note="Phosphonoacetaldehyde hydrolase"
FT /id="PRO_1000073458"
FT ACT_SITE 12
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
FT ACT_SITE 54
FT /note="Schiff-base intermediate with substrate"
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 14
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
FT BINDING 188
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
SQ SEQUENCE 271 AA; 29539 MW; F6CC95BBA074F81D CRC64;
MMNSPIQAVI FDWAGTIVDF GSFAPTSIFV EAFKQGFDFE ISLAEAREPM GLGKWQHIEA
VGKLPTVAQR WQKQFGRPMQ ASDIDAIYAA FMPLQIAKVA DHAAPIPHSL EVVEQIRSRG
IKIGSCSGYP RQVMDVLIAA AADYGYRPDY VVATDDLAQG GRPAPFMALK NVIELGVTDV
RACVKVDDAL PGIEEGHNAG MWTVGLLLSG NEAGLTLEEY QHADDQTLQA ARERAQAKLQ
QAKPHYLIDT VADLPAVLAQ IEQRLLAGER P