Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

    ⌊ Subgroup C2.B: Phosphomannomutase and Phosphatase Like

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

  ⌊ FunctionalDomain C2.B.2: Mannosyl-3-phosphoglycerate Phosphatase Like (ID 32785)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Pyrococcus horikoshii Taxon ID: 53953 222143030
Pyrococcus horikoshii Taxon ID: 53953 222143029

Uniprot

Protein NameAccessionEC Number Identifier
Mannosyl-3-phosphoglycerate phosphatase {ECO:0000255|HAMAP-Rule:MF_00617, ECO:0000303|PubMed:11562374, ECO:0000303|PubMed:19018103} O58690 MPGP_PYRHO (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 249 | Length of Functional Domain: 243

1       10        20        30        40        50        60

XIRLIFLDIDKTLIPGYEPDPAKPIIEELKDXGFEIIFNSSKTRAEQEYYRKELEVETPF
ISENGSAIFIPKGYFPFDVKGKEVGNYIVIELGIRVEKIREELKKLENIYGLKYYGNSTK
EEIEKFTGXPPELVPLAXEREYSETIFEWSRDGWEEVLVEGGFKVTXGSRFYTVHGNSDK
GKAAKILLDFYKRLGQIESYAVGDSYNDFPXFEVVDKVFIVGSLKHKKAQNVSSIIDVLE
VIKHHHHHH
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
40 Ser (S) side chain interacts with substrate/intermediate substrate binding -- binding ISS
Subgroup CAR This EFD conserves 7/7 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
8 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
10 Asp (D) side chain general acid proton relay -- reactant ICS PubMed:21961705
40 Ser (S) side chain None -- ISS PubMed:21961705
42 Lys (K) side chain Positions general acid/base Asp steric role -- spectator ICS PubMed:21961705
180 Lys (K) side chain None -- ISS PubMed:21961705
204 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:21961705
208 Asp (D) side chain None -- ISS PubMed:21961705

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
1WZC Crystal Structure Of Pyrococcus Horikoshii Mannosyl-3-Phosphoglycerate Phosphatase Complexed With Mg2+ And Phosphate Mannosyl-3-Phosphoglycerate Phosphatase 3 1.9 Yes Magnesium Ion • Phosphate Ion CSA • PDB • PDBSum
2ZOS Crystal Structure Of Mannosyl-3-Phosphoglycerate Phosphatase From Pyrococcus Horikoshii Mannosyl-3-Phosphoglycerate Phosphatase 3 1.7 Yes Selenomethionine 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
Nov. 3, 2014, 11:10 a.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.