Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

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

  ⌊ C1.5.2: MDP Like

     ⌊ Family mdp-1

  ⌊ FunctionalDomain mdp-1 (ID 1448)

Superfamily Assignment Evidence Code(s) ISS
Family Assignment Evidence Code CFM PubMed:11601995
This entry was last updated onNov. 22, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Mus musculus Taxon ID: 10090 12963663 NP_075886.1 (RefSeq) PRP URP
Mus musculus Taxon ID: 10090 148704316 EDL36263.1 (Genbank) PRP URP
Mus musculus Taxon ID: 10090 28302279 AAH46613.1 (Genbank) PRP URP
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Uniprot

Protein NameAccessionEC Number Identifier
Magnesium-dependent phosphatase 1 Q9D967 3.1.3.- MGDP1_MOUSE (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 164 | Length of Functional Domain: 164

1       10        20        30        40        50        60

MTRLPKLAVFDLDYTLWPFWVDTHVDPPFHKSSDGTVRDRRGQNIQLYPEVPEVLGRLQS
LGVPVAAASRTSEIQGANQLLELFDLGKYFIQREIYPGSKVTHFERLHHKTGVPFSQMVF
FDDENRNIIDVGRLGVTCIHIRDGMSLQTLTQGLETFAKAQAGL
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
69 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
11 Asp (D) side chain Mg2+ ligand, nucleophile: attacks phosphate moiety of substrate to form covalent intermediate covalent catalysis -- reactant,
metal ligand -- binding 		ICS PubMed:15461449
13 Asp (D) side chain Mg2+ ligand, general acid: donates proton to leaving group metal ligand -- binding,
proton relay -- reactant 		ICS PubMed:15461449
69 Ser (S) side chain binds phosphate moiety of substrate substrate binding -- binding ICS PubMed:15461449
100 Lys (K) side chain binds phosphate moiety of substrate substrate binding -- binding ICS PubMed:15461449
123 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:15461449
Family CAR This EFD conserves 5/5 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
11 Asp (D) side chain Mg2+ ligand, nucleophile: attacks phosphate moiety of substrate to form covalent intermediate covalent catalysis -- reactant,
metal ligand -- binding 		ICS PubMed:15461449
13 Asp (D) side chain Mg2+ ligand, general acid: donates proton to leaving group metal ligand -- binding,
proton relay -- reactant 		ICS PubMed:15461449
69 Ser (S) side chain binds phosphate moiety of substrate substrate binding -- binding ICS PubMed:15461449
100 Lys (K) side chain binds phosphate moiety of substrate substrate binding -- binding ICS PubMed:15461449
123 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:15461449

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
1U7P X-Ray Crystal Structure Of The Hypothetical Phosphotyrosine Phosphatase Mdp-1 Of The Haloacid Dehalogenase Superfamily Magnesium-Dependent Phosphatase-1 1 1.9 Magnesium Ion • Tungstate(Vi)Ion CSA • PDB • PDBSum
1U7O Magnesium Dependent Phosphatase 1 (Mdp-1) Magnesium-Dependent Phosphatase-1 1 1.9 Acetate 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
Nov. 3, 2014, 9:22 a.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.