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 105621)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Escherichia coli 908658 Taxon ID: 1269003 553686353 ESE02738.1 (Genbank) URP
Escherichia coli 908541 Taxon ID: 1268996 553654874 ESD73064.1 (Genbank) URP
Escherichia coli 908555 Taxon ID: 1268997 553649820 ESD68249.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
Alpha-D-glucose 1-phosphate phosphatase YihX P0A8Y3 YIHX_ECOLI (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 206 | Length of Functional Domain: 202

1       10        20        30        40        50        60

MARKEAKMLYIFDLGNVIVDIDFNRVLGAWSDLTRIPLASLKKSFHMGEAFHQHERGEIS
DEAFAEALCHEMALPLSYEQFSHGWQAVFVALRPEVIAIMHKLREQGHRVVVLSNTNRLH
TTFWPEEYPEIRDAADHIYLSQDLGMRKPEARIYQHVLQAEGFSPSDTVFFDDNADNIEG
ANQLGITSILVKDKTTIPDYFAKVLC
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
114 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
13 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
115 Asn (N) side chain binds phosphate moiety of substrate substrate binding -- binding ICS PubMed:15096040
148 Lys (K) side chain stabilizes negatively charged intermediate electrostatic stabiliser -- spectator ISS PubMed:12574508
172 Asp (D) side chain Mg2+ ligand (via water) metal ligand -- binding ICS PubMed:15096040
173 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:15096040

Catalyzed Reaction

glucose-1-phosphatase

+ +
alpha-D-glucose 1-phosphate
29042		 water
15377		 D-glucose
17634		 phosphoric acid
26078

EC: 3.1.3.10 | IntEnz: 3.1.3.10 | Kegg: 3.1.3.10 | BioCyc: 3.1.3.10 | BRENDA: 3.1.3.10

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
April 30, 2014, 7:15 a.m. update curation agent sbrown setDomainBoundaries.py
update domain start position 6 5
EC number assigned by UniProtKB accession ID.