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 onJune 3, 2017

References to Other Databases

Genbank

SpeciesGIAccessionModel
Bacillus cereus 10835408 MB URP
Bacillus cereus 10835407 MB URP
Bacillus cereus 10835406 MB URP
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. The Superfamily domain, when present, is shown using underlining. 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

Superfamily CAR This EFD conserves 2/2 Superfamily-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
8 Asp (D) side chain nucleophile: forms covalent intermediate covalent catalysis -- reactant ISS
122 Thr (T) side chain interacts with substrate/intermediate substrate binding -- binding ISS
Subgroup CAR This EFD conserves 2/2 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
8 Asp (D) side chain Mg2+ ligand, nucleophile: attacks phosphate moiety of intermediate to form covalent intermediate covalent catalysis -- reactant,
metal ligand -- binding
ICS
156 Arg (R) side chain None -- ICS
Family CAR This EFD conserves 8/8 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
8 Asp (D) side chain Mg2+ ligand, nucleophile: attacks phosphate moiety of schiff-base intermediate to form covalent intermediate covalent catalysis -- reactant,
metal ligand -- binding
IDA
12 Thr (T) side chain positions D29 steric role -- spectator ICS
45 Met (M) side chain involved in catalysis of schiff-base formation covalent catalysis -- reactant ICS
49 Lys (K) side chain forms schiff-base linkage to substrate covalent catalysis -- reactant IDA
52 His (H) side chain involved in catalysis of schiff-base formation covalent catalysis -- reactant ICS
122 Thr (T) side chain interacts with substrate substrate binding -- binding ICS
156 Arg (R) side chain forms salt bridge with D29 and interacts with substrate activation -- spectator ICS
182 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS

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.

Curation History

Time Change Annotation Old Value New Value
Nov. 3, 2014, 9:25 a.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.