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 22223)

Superfamily Assignment Evidence Code(s) IEA
Family Assignment Evidence Code IEA
This entry was last updated onNov. 22, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Bacillus anthracis str. Ames Taxon ID: 198094 30261426 NP_843803.1 (RefSeq) URP
Taxon ID: 86661 446610029 WP_000687375.1 (RefSeq)
Bacillus thuringiensis serovar konkukian str. 97-27 Taxon ID: 281309 49479773 YP_035550.1 (RefSeq) URP
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Uniprot

Protein NameAccessionEC Number Identifier
Phosphonoacetaldehyde hydrolase {ECO:0000255|HAMAP-Rule:MF_01375} Q81TE1 PHNX_BACAN (Swiss-Prot)
Phosphonoacetaldehyde hydrolase {ECO:0000255|HAMAP-Rule:MF_01375} Q6HLM1 PHNX_BACHK (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 264 | Length of Functional Domain: 264

1       10        20        30        40        50        60

MKIEAVIFDWAGTTVDYGCFAPLEVFMEIFHKRGVGITAEEARKPMGLLKIDHVRALTEM
PRIANEWNRIFGQLPTETDIQEMYEEFEEILFAILPRYASPIHGVKEVIASLRERGIKIG
STTGYTREMMDIVAKEAALQGYKPDFLVTPDDVPAGRPYPWMCYKNAMELGVYPMNHMIK
IGDTVSDMKEGRNAGMWTVGVILGSSELGLSEEEVENMDPAELREKIEVVRNRFVENGAH
FTIETMQELESVMERIEKQELIIS
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
9 Asp (D) side chain nucleophile: forms covalent intermediate covalent catalysis -- reactant ISS
123 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
9 Asp (D) side chain Mg2+ ligand, nucleophile: attacks phosphate moiety of intermediate to form covalent intermediate covalent catalysis -- reactant,
metal ligand -- binding 		ICS PubMed:12081483
157 Arg (R) side chain None -- ICS PubMed:10956028 PubMed:12081483
Family CAR This EFD conserves 8/8 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
9 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 PubMed:10956028
13 Thr (T) side chain positions D29 steric role -- spectator ICS PubMed:10956028
46 Met (M) side chain involved in catalysis of schiff-base formation covalent catalysis -- reactant ICS PubMed:14670958
50 Lys (K) side chain forms schiff-base linkage to substrate covalent catalysis -- reactant IDA PubMed:9649311
53 His (H) side chain involved in catalysis of schiff-base formation covalent catalysis -- reactant ICS PubMed:14670958
123 Thr (T) side chain interacts with substrate substrate binding -- binding ICS PubMed:10956028
157 Arg (R) side chain forms salt bridge with D29 and interacts with substrate activation -- spectator ICS PubMed:10956028
183 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:10956028

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
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
2IOH Crystal Structure Of Phosphonoacetaldehyde Hydrolase With A K53R Mutation Phosphonoacetaldehyde Hydrolase 33 2.9 Yes Phosphate Ion • Magnesium Ion CSA • PDB • PDBSum
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
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
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
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
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, 10:09 a.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.