Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

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

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

  ⌊ FunctionalDomain C1.5.6: HAD, Beta-PGM, Phosphatase Like (ID 33979)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Shigella dysenteriae Taxon ID: 622 446029005 WP_000106860.1 (RefSeq)
Shigella dysenteriae 155-74 Taxon ID: 766142 332085915 EGI91079.1 (Genbank) URP
Shigella dysenteriae 1012 Taxon ID: 358708 194418230 EDX34321.1 (Genbank) URP

Uniprot

Protein NameAccessionEC Number Identifier
n/a F3VBG1 F3VBG1_SHIDY (TrEMBL)
n/a A0A1S9JZ94 A0A1S9JZ94_SHIDY (TrEMBL)
n/a B3X2E6 B3X2E6_9ENTR (TrEMBL)

Sequence

Length of Enzyme (full-length): 222 | Length of Functional Domain: 216

1       10        20        30        40        50        60

MSTPRQILAAIFDMDGLLIDSEPLWDRAELDVMASLGVNISRRNELPDTLGLRIDMVVDL
WYARQPWNGPSRQEVVERVIARAISLVEETRPLLPGVREAVALCKEQGLLVGLASASPLH
MLEKVLTMFDLRDSFDALASAEKLPYSKPHPQVYLDCAAKLGVDPLTCVALEDSVNGMIA
SKAARMRSIVVPAPEAQNDPRFVLANVKLSSLTELTAKDLLG
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
115 Ser (S) 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
148 Lys (K) side chain None -- ICS PubMed:10956028 PubMed:12081483

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
1TE2 Putative Phosphatase Ynic From Escherichia Coli K12 2-Deoxyglucose-6-P Phosphatase 39 1.76 Selenomethionine
(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
April 30, 2014, 6 a.m. update curation agent sbrown setDomainBoundaries.py
update domain end position 221 220
update domain start position 6 5
EC number assigned by UniProtKB accession ID.