Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

    ⌊ Subgroup C2.B: Phosphomannomutase and Phosphatase Like

  ⌊ C2.B.3: Phosphomannomutase Like

  ⌊ FunctionalDomain C2.B.3: Phosphomannomutase Like (ID 270002)

Superfamily Assignment Evidence Code(s) IEA
This entry was last updated onFeb. 13, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Mus musculus Taxon ID: 10090 12851309 PRP URP

Uniprot

Protein NameAccessionEC Number Identifier
n/a Q9D6D9 Q9D6D9_MOUSE (TrEMBL)

Sequence

Length of Enzyme (full-length): 165 | Length of Functional Domain: 154

1       10        20        30        40        50        60

MAVAVEGARRKERILCLFDVDGTLTPARQKIDPEVSAFLQKLRSRVQIGVVGGSDYSKIA
EQLGEGDEVIEKFDYVFAENGTVQYKHGRLLSKQTIQNHLGEELLQDLINFCLSYMALLR
LPKKRGTFIEFRNGMLNVSPIGRSCTLEERIEFSELDKVPFAGQL
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 0/2 Superfamily-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
52 Gly (G) side chain MISMATCH: This residue does not match the specified amino acid type of S,T, and thus may not function in the same manner as other sequences in the superfamily
Subgroup CAR This EFD conserves 3/8 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
19 Asp (D) side chain Mg2+ ligand, nucleophile: attacks phosphate moiety of substrate to form covalent intermediate covalent catalysis -- reactant,
metal ligand -- binding 		ICS PubMed:16540464
21 Asp (D) side chain Mg2+ ligand, acid/base metal ligand -- binding,
proton relay -- reactant 		ICS PubMed:16540464
62 Gln (Q) side chain Positions acid/base Asp steric role -- spectator ICS PubMed:16540464

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
2FUC Human Alpha-Phosphomannomutase 1 With Mg2+ Cofactor Bound Phosphomannomutase 1 10 2.1 Selenomethionine • Magnesium Ion CSA • PDB • PDBSum
2FUE Human Alpha-Phosphomannomutase 1 With D-Mannose 1-Phosphate And Mg2+ Cofactor Bound Phosphomannomutase 1 10 1.75 Selenomethionine
(2 more ⇓) 		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, 5:19 a.m. update curation agent sbrown setDomainBoundaries.py
update domain end position 153 161
update domain start position 12 8
EC number assigned by UniProtKB accession ID.