Top Level Name

  ⌊ FunctionalDomain uncharacterized sequence (ID 268260)

This sequence has not been fully curated yet.
This entry was last updated onJuly 22, 2015

References to Other Databases

Sequence

Length of Enzyme (full-length): 258 | Length of Functional Domain: 258

1       10        20        30        40        50        60

IVFTDLDGTLLDERGELGPAREALERLRALGVPVVPVTAKTRKEVEALGLEPPFIVENGG
GLYLPRDWPVRAGRPKGGYRVVSLAWPYRKVRARLREAEALAGRPILGYGDLTAEAVARL
TGLSPEAARRAKAREYDETLVLCPEEVEAVLEALEAVGLEWTHGGRFYHAAKGADKGRAA
ARLRALWPDPEEARFAVGLGDSLNDLPLFRAVDLAVYVGRRDPPEGVLATPAPGPEGFRY
AVERYLLPRLSRRGGSGP
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.

Structures

PDB ID Title Molecule Name Number of
EFDs
Resolution (Å) Mutant? Het group Links
3ZUP The 3-Dimensional Structure Of Mpgp From Thermus Thermophilus Hb27, In Complex With The Alpha-Mannosylglycerate And Orthophosphate Reaction Products. Mannosyl-3-Phosphoglycerate Phosphatase 3 1.8 Magnesium Ion
(2 more ⇓)
CSA • PDB • PDBSum
3ZX5 The 3-Dimensional Structure Of Mpgp From Thermus Thermophilus Hb27, Covalently Bound To Vanadate And In Complex With Alpha-Mannosylglycerate And Magnesium Mannosyl-3-Phosphoglycerate Phosphatase 3 1.81 Magnesium Ion
(2 more ⇓)
CSA • PDB • PDBSum
3ZX4 The 3-Dimensional Structure Of Mpgp From Thermus Thermophilus Hb27, In Complex With The Alpha-Mannosylglycerate,Orthophosphate And Magnesium Mannosyl-3-Phosphoglycerate Phosphatase 3 1.74 Magnesium Ion
(2 more ⇓)
CSA • PDB • PDBSum
3ZTW The 3-Dimensional Structure Of Apo-Mpgp, The Mannosyl-3-Phosphoglycerate Phosphatase From Thermus Thermophilus Hb27 In Its Apo-Form Mannosyl-3-Phosphoglycerate Phosphatase 3 1.9 Phosphate Ion CSA • PDB • PDBSum
3ZU6 The 3-Dimensional Structure Of Mpgp From Thermus Thermophilus Hb27, In Complex With The Alpha-Mannosylglycerate And Orthophosphate Reaction Products. Mannosyl-3-Phosphoglycerate Phosphatase 3 1.9 Magnesium Ion
(2 more ⇓)
CSA • PDB • PDBSum
3ZW7 The 3-Dimensional Structure Of Mpgp From Thermus Thermophilus Hb27, In Complex With The Alpha-Mannosylglycerate And Metaphosphate. Mannosyl-3-Phosphoglycerate Phosphatase 3 1.9 Magnesium Ion
(4 more ⇓)
CSA • PDB • PDBSum
3ZTY The 3-Dimensional Structure Of The Gadolinium Derivative Of Mpgp, The Mannosyl-3-Phosphoglycerate Phosphatase From Thermus Thermophilus Hb27 Mannosyl-3-Phosphoglycerate Phosphatase 3 2.5 Gadolinium Atom • Chloride Ion CSA • PDB • PDBSum
3ZWK The 3-Dimensional Structure Of Mpgp From Thermus Thermophilus Hb27, In Complex With The Metavanadate Mannosyl-3-Phosphoglycerate Phosphatase 3 2.1 Magnesium Ion • Vanadate Ion CSA • PDB • PDBSum
3ZWD The 3-Dimensional Structure Of Mpgp From Thermus Thermophilus Hb27, In Complex With The Alpha-Mannosylglycerate. Mannosyl-3-Phosphoglycerate Phosphatase 3 1.92 2-O-Alpha-Mannosyl-D-Glycerate • 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.
EC number assigned by UniProtKB accession ID.