Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

    ⌊ Subgroup C1.5: HAD, Beta-PGM, Phosphatase Like

  C1.5.6: HAD, Beta-PGM, Phosphatase Like

     ⌊ Family phosphonoacetaldehyde hydrolase

  ⌊ FunctionalDomain phosphonoacetaldehyde hydrolase (ID 2216)

Superfamily Assignment Evidence Code(s) ISS
Family Assignment Evidence Code CFM
This entry was last updated onOct. 25, 2014

References to Other Databases

Genbank

SpeciesGIAccessionModel
Bacillus cereus P 10835408 MB
Bacillus cereus P 10835407 MB
Bacillus cereus P 10835406 MB
Show All

Uniprot

Protein NameAccessionEC Number IdentifierModel
Phosphonoacetaldehyde hydrolase O31156 3.11.1.1 PHNX_BACCE (Swiss-Prot) MB

Sequence

Length of Enzyme (full-length): 256 | Length of Functional Domain: 256

1       10        20        30        40        50        60

KIEAVIFDWAGTTVDYGCFAPLEVFMEIFHKRGVAITAEEARKPMGLLKIDHVRALTEMP
RIASEWNRVFRQLPTEADIQEMYEEFEEILFAILPRYASPINAVKEVIASLRERGIKIGS
TTGYTREMMDIVAKEAALQGYKPDFLVTPDDVPAGRPYPWMCYKNAMELGVYPMNHMIKV
GDTVSDMKEGRNAGMWTVGVILGSSELGLTEEEVENMDSVELREKIEVVRNRFVENGAHF
TIETMQELESVMEHIE

FASTA | BLAST | HMM

This shows the full-length sequence of the enzyme. The region of the functional domain is highlighted in black letters, while the residual residues are shown in grey. In many cases the functional domain is the full-length sequence. Conserved catalytic residues (as determined by automated alignment to family, subgroup, or superfamily HMMs) are shown with teal highlighting . Conserved catalytic residues which do not matched the Conserved Alignment Residue are shown with maroon highlighting . Information regarding their function can be found in the Conserved Residues section below.
FASTA formatted full-length sequence.
BLAST this sequence against SFLD.
Scan SFLD-HMMs with this sequence.

Conserved Residues

This EFD conserves 8/8 Family-specific CRs and 4/5 Subgroup-specific CRs.
Position Amino Acid Family/Subgroup CAR Function Evidence Code Reference
8 Asp (D) Both Mg2+ ligand, nucleophile: attacks phosphate moiety of intermediate to form covalent intermediate ICS
156 Arg (R) Both None ICS
182 Asp (D) Both Mg2+ ligand ICS
181 Gly (G) Subgroup Mg2+ ligand ICS
186 Asp (D) Subgroup Mg2+ ligand ICS
12 Thr (T) Family positions D29 ICS
45 Met (M) Family involved in catalysis of schiff-base formation ICS
49 Lys (K) Family forms schiff-base linkage to substrate IDA
52 His (H) Family involved in catalysis of schiff-base formation ICS
122 Thr (T) Family interacts with substrate ICS

Catalyzed Reaction(s)

hydrolysis of phosphonoacetaldehyde

Evidence Code: IDA

EC: 3.11.1.1 | IntEnz: 3.11.1.1 | Kegg: 3.11.1.1 | BioCyc: 3.11.1.1 | BRENDA: 3.11.1.1 | MACiE: M0181

Structures

PDB ID Title Molecule Name Number of
EFDs
Resolution (Å) Mutant? Het group Chimera Session Links
1RQN Phosphonoacetaldehyde Hydrolase Complexed With Magnesium Phosphonoacetaldehyde Hydrolase 33 2.8 Magnesium Ion CSA • PDB • PDBSum
1RQL Crystal Structure Of Phosponoacetaldehyde Hydrolase Complexed With Magnesium And The Inhibitor Vinyl Sulfonate Phosphonoacetaldehyde Hydrolase 33 2.4 Magnesium Ion • Vinylsulphonic Acid CSA • PDB • PDBSum
1FEZ The Crystal Structure Of Bacillus Cereus Phosphonoacetaldehyde Hydrolase Complexed With Tungstate, A Product Analog Phosphonoacetaldehyde Hydrolase 31 3.0 Tungstate(Vi)Ion • Magnesium Ion CSA • PDB • PDBSum
2IOF Crystal Structure Of Phosphonoacetaldehyde Hydrolase With Sodium Borohydride-Reduced Substrate Intermediate Phosphonoacetaldehyde Hydrolase • Phosphonoacetaldehyde Hydrolase 37 2.5 N~6~-Ethyl-L-Lysine
(2 more ⇓)
CSA • PDB • PDBSum
1RDF G50P Mutant Of Phosphonoacetaldehyde Hydrolase In Complex With Substrate Analogue Vinyl Sulfonate Phosphonoacetaldehyde Hydrolase 28 2.8 Yes Magnesium Ion • Ethanesulfonic Acid CSA • PDB • PDBSum
2IOH Crystal Structure Of Phosphonoacetaldehyde Hydrolase With A K53R Mutation Phosphonoacetaldehyde Hydrolase 33 2.9 Yes Phosphate Ion • Magnesium Ion CSA • PDB • PDBSum
1SWW Crystal Structure Of The Phosphonoacetaldehyde Hydrolase D12A Mutant Complexed With Magnesium And Substrate Phosphonoacetaldehyde Phosphonoacetaldehyde Hydrolase 33 2.3 Magnesium Ion • Phosphonoacetaldehyde CSA • PDB • PDBSum
1SWV Crystal Structure Of The D12A Mutant Of Phosphonoacetaldehyde Hydrolase Complexed With Magnesium Phosphonoacetaldehyde Hydrolase 33 2.3 Yes Magnesium Ion CSA • PDB • PDBSum
Percent identity and alignment length from the BLAST match of the Functional Domain sequence to the PDB sequence.
"Yes" indicates that a GI associated with this Functional Domain was mapped to the PDB ID via UniProtKB.
EC number assigned by UniProtKB accession ID.