Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

    ⌊ Subgroup C2.B: Phosphomannomutase and Phosphatase Like

  ⌊ C2.B.2: Mannosyl-3-phosphoglycerate Phosphatase Like

     ⌊ Family mannosyl-3-phosphoglycerate phosphatase

  ⌊ FunctionalDomain mannosyl-3-phosphoglycerate phosphatase (ID 37867)

Superfamily Assignment Evidence Code(s) ISS
Family Assignment Evidence Code ISS PubMed:21961705
This entry was last updated onNov. 22, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Thermus thermophilus Taxon ID: 274 499486394 WP_011173034.1 (RefSeq)
Thermus thermophilus HB27 Taxon ID: 262724 46196521 AAS80937.1 (Genbank) URP
Thermus thermophilus HB27 Taxon ID: 262724 28950685 AAO43098.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
n/a Q84B23 Q84B23_THETH (TrEMBL)
n/a Q72K29 Q72K29_THET2 (TrEMBL)

Sequence

Length of Enzyme (full-length): 259 | Length of Functional Domain: 251

1       10        20        30        40        50        60

MIVFTDLDGTLLDERGELGPAREALERLRALGVPVVPVTAKTRKEVEALGLEPPFIVENG
GGLYLPRDWPVRAGRPKGGYRVVSLAWPYRKVRARLREAEALAGRPILGYGDLTAEAVAR
LTGLSREAARRAKAREYDETLVLCPEEVEAVLEALEAVGLEWTHGGRFYHAAKGADKGRA
VARLRALWPDPEEARFAVGLGDSLNDLPLFRAVDLAVYVGRGDPPEGVLATPAPGPEGFR
YAVERYLLPRLSRRGGSGP
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
6 Asp (D) side chain nucleophile: forms covalent intermediate covalent catalysis -- reactant ISS
Subgroup CAR This EFD conserves 7/7 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
6 Asp (D) side chain Mg2+ ligand, nucleophile: attacks phosphate moiety of substrate to form covalent intermediate covalent catalysis -- reactant,
metal ligand -- binding 		ICS PubMed:21961705
8 Asp (D) side chain general acid proton relay -- reactant ICS PubMed:21961705
39 Thr (T) side chain None -- ISS PubMed:21961705
41 Lys (K) side chain Positions general acid/base Asp steric role -- spectator ICS PubMed:21961705
177 Lys (K) side chain None -- ISS PubMed:21961705
202 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:21961705
206 Asp (D) side chain None -- ISS PubMed:21961705
Family CAR This EFD conserves 14/14 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
6 Asp (D) side chain Mg2+ ligand; nucleophile: attacks phosphate moiety of substrate to form covalent intermediate covalent catalysis -- reactant,
metal ligand -- binding 		ICS PubMed:21961705
8 Asp (D) side chain general acid: donates proton to leaving group proton relay -- reactant ICS PubMed:21961705
39 Thr (T) side chain None -- ISS PubMed:21961705
41 Lys (K) side chain Positions Asp general acid steric role -- spectator ICS PubMed:21961705
45 Glu (E) side chain Binds substrate substrate binding -- binding ICS PubMed:21961705
110 Tyr (Y) side chain Assists in stereochemical discrimination of mannosyl group from other sugar compounds steric role -- spectator ICS PubMed:21961705
122 Thr (T) side chain Forms hydrogen bonding network that helps fix mannosyl moiety in active site substrate binding -- binding ICS PubMed:21961705
135 Arg (R) side chain Binds C3(OH) hydroxyl of mannosyl moiety substrate binding -- binding ICS PubMed:21961705
140 Thr (T) side chain Assists in stereochemical discrimination of mannosyl group from other sugar compounds steric role -- spectator ICS PubMed:21961705
165 Gly (G) side chain Mg2+ ligand (via water); Stabilizes conformational change of C23O13(H) group, allowing nucleophilic attack on phosphate by activated water electrostatic stabiliser -- spectator,
metal ligand -- binding 		ICS PubMed:21961705
167 Arg (R) side chain Helps close cap, fixing substrate in active site steric role -- spectator ICS PubMed:21961705
177 Lys (K) side chain None -- ISS PubMed:21961705
202 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:21961705
206 Asp (D) side chain None -- ISS PubMed:21961705

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.

Curation History
Time Change Annotation Old Value New Value
April 30, 2014, 6:09 a.m. update curation agent sbrown setDomainBoundaries.py
update domain end position 259 251
EC number assigned by UniProtKB accession ID.