Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

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

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

     ⌊ Family 2-deoxyglucose-6-phosphatase

  ⌊ FunctionalDomain 2-deoxyglucose-6-phosphatase (ID 1451)

Superfamily Assignment Evidence Code(s) ISS
Family Assignment Evidence Code CFM PubMed:8553694
This entry was last updated onNov. 22, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Saccharomyces cerevisiae S288c Taxon ID: 559292 6321834 NP_011910.1 (RefSeq) PRP URP
Saccharomyces cerevisiae YJM1355 Taxon ID: 1294353 768815992 AJV32577.1 (Genbank) URP
Saccharomyces cerevisiae YJM1342 Taxon ID: 1294352 768815733 AJV32319.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
2-deoxyglucose-6-phosphate phosphatase 1 P38774 3.1.3.68 DOG1_YEAST (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 246 | Length of Functional Domain: 246

1       10        20        30        40        50        60

MAEFSADLCLFDLDGTIVSTTVAAEKAWTKLCYEYGVDPSELFKHSHGARTQEVLRRFFP
KLDDTDNKGVLALEKDIAHSYLDTVSLIPGAENLLLSLDVDTETQKKLPERKWAIVTSGS
PYLAFSWFETILKNVGKPKVFITGFDVKNGKPDPEGYSRARDLLRQDLQLTGKQDLKYVV
FEDAPVGIKAGKAMGAITVGITSSYDKSVLFDAGADYVVCDLTQVSVVKNNENGIVIQVN
NPLTRA
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

Subgroup CAR This EFD conserves 2/2 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
12 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
151 Lys (K) side chain None -- ICS PubMed:10956028 PubMed:12081483
Family CAR This EFD conserves 4/4 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
12 Asp (D) side chain nucleophile: attacks phosphate moiety of substrate to form covalent intermediate covalent catalysis -- reactant ISS PubMed:9649311
14 Asp (D) side chain None -- ISS PubMed:9649311
151 Lys (K) side chain None -- ISS PubMed:9649311
183 Asp (D) side chain None -- ISS PubMed:9649311

Catalyzed Reaction

2-deoxyglucose-6-phosphatase

+ +
2-deoxy-D-glucose 6-phosphate(2-)
57615		 water
15377		 2-deoxy-D-glucose
15866		 hydrogenphosphate
43474

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

Curation History
Time Change Annotation Old Value New Value
Nov. 3, 2014, 9:22 a.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.