Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

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

  ⌊ C1.5.1: Epoxide Hydrolase Phosphatase Like

  ⌊ FunctionalDomain C1.5.1: Epoxide Hydrolase Phosphatase Like (ID 124877)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Escherichia fergusonii Taxon ID: 564 446888435 WP_000965691.1 (RefSeq) URP
Escherichia fergusonii Taxon ID: 564 803343836 KKA84452.1 (Genbank) URP
Escherichia fergusonii B253 Taxon ID: 550694 324111500 EGC05481.1 (Genbank) URP

Sequence

Length of Enzyme (full-length): 199 | Length of Functional Domain: 199

1       10        20        30        40        50        60

MLYIFDLGNVIVDIDFNRVLGTWSDLTRVPLASLKKSFHMGEAFHQHERGEISDEAFAEA
LCHEMALPLSYEQFSHGWQAVFVALRPEVIAIMHKLREQGHRVVVLSNTNRLHTTFWPEE
YPEIRAAADHIYLSQDLGMRKPEARIYQHVLQAEGFSASDTVFFDDNADNIEGANQLGIT
SILVKDKTTIPDYFAKLLC
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 1/2 Superfamily-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
107 Ser (S) side chain interacts with substrate/intermediate substrate binding -- binding ISS
Subgroup CAR This EFD conserves 5/5 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
6 Asp (D) side chain nucleophile: attacks phosphate moiety of substrate to form covalent intermediate; Mg2+ ligand covalent catalysis -- reactant,
metal ligand -- binding 		IDA PubMed:12574508
108 Asn (N) side chain binds phosphate moiety of substrate substrate binding -- binding ICS PubMed:15096040
141 Lys (K) side chain stabilizes negatively charged intermediate electrostatic stabiliser -- spectator ISS PubMed:12574508
165 Asp (D) side chain Mg2+ ligand (via water) metal ligand -- binding ICS PubMed:15096040
166 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:15096040

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
2B0C The Crystal Structure Of The Putative Phosphatase From Escherichia Coli Putative Phosphatase 29 2.0 Alpha-D-Glucose-1-Phosphate • 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
Aug. 1, 2014, 5:31 p.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.