ID R6DJU0_9BACE Unreviewed; 261 AA.
AC R6DJU0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=BN772_02959 {ECO:0000313|EMBL:CDA84541.1};
OS Bacteroides sp. CAG:754.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1262750 {ECO:0000313|EMBL:CDA84541.1, ECO:0000313|Proteomes:UP000017906};
RN [1] {ECO:0000313|EMBL:CDA84541.1, ECO:0000313|Proteomes:UP000017906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:754 {ECO:0000313|Proteomes:UP000017906};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:CDA84541.1}.
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DR EMBL; CBCP010000169; CDA84541.1; -; Genomic_DNA.
DR AlphaFoldDB; R6DJU0; -.
DR Proteomes; UP000017906; Unassembled WGS sequence.
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; IPR041492; HAD_2.
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; PF13419; HAD_2; 1.
DR SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 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:CDA84541.1};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01375};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01375};
KW Reference proteome {ECO:0000313|Proteomes:UP000017906};
KW Schiff base {ECO:0000256|HAMAP-Rule:MF_01375}.
FT ACT_SITE 10
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01375"
FT ACT_SITE 51
FT /note="Schiff-base intermediate with substrate"
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 12
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01375"
FT BINDING 184
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01375"
SQ SEQUENCE 261 AA; 28710 MW; 1AD84F4281400050 CRC64;
MKKIECIIMD WAGTAVDYGC FAPVAAFIEA FAEKGLTIDV VQTRKPMGLP KIQHIRELLS
MPEVNGQFIA RYQRAWTEED VVELNRLFEK HLFASLENYT DPIPGVIPTL EKLRADSLKI
GSTTGYTREM MDVVLPAAQA KGYRVDYCAT PNLFPAGRPA PYMIFENLIK LAVPSLDAVV
KVGDTIADIK EGVNAKVCSV GVILGSNEMA LTEEETRNMP ATELEARIAD VKERMLAAGA
SHVIRTIEEL PALIETLNAG K
//
