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 117105)

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 thuringiensis serovar pulsiensis BGSC 4CC1 Taxon ID: 527028 228845600 EEM90629.1 (Genbank) URP

Uniprot

Protein NameAccessionEC Number Identifier
n/a C3HFM5 C3HFM5_BACTU (TrEMBL)

Sequence

Length of Enzyme (full-length): 268 | Length of Functional Domain: 268

1       10        20        30        40        50        60

MMDCMKIEAVIFDWAGTTVDYGCFAPLEVFMEIFHKRGVGITAEEARKPMGLLKIDHVRA
LTEMPRIANEWNRIFGQLPTETDIQEMYEEFEEILFAILPRYASPIHGVKEVIASLRERG
IKIGSTTGYTREMMNIVAKEAALQGYKPDFLVTPDDVPAGRPYPWMCYKNAMELGVYPMN
HMIKIGDTVSDMKEGRNAGMWTVGVILGSSELGLSEEEVENMDSAELREKIEVVRNRFVE
NGAHFTIETMQELESVMERIKKQELIIS
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
13 Asp (D) side chain nucleophile: forms covalent intermediate covalent catalysis -- reactant ISS
127 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
13 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
161 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
13 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
17 Thr (T) side chain positions D29 steric role -- spectator ICS PubMed:10956028
50 Met (M) side chain involved in catalysis of schiff-base formation covalent catalysis -- reactant ICS PubMed:14670958
54 Lys (K) side chain forms schiff-base linkage to substrate covalent catalysis -- reactant IDA PubMed:9649311
57 His (H) side chain involved in catalysis of schiff-base formation covalent catalysis -- reactant ICS PubMed:14670958
127 Thr (T) side chain interacts with substrate substrate binding -- binding ICS PubMed:10956028
161 Arg (R) side chain forms salt bridge with D29 and interacts with substrate activation -- spectator ICS PubMed:10956028
187 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
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
Aug. 1, 2014, 5:02 p.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.