Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

    ⌊ Subgroup C1.4: 5'-Nucleotidase Like

  ⌊ FunctionalDomain C1.4: 5'-Nucleotidase Like (ID 35870)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Macaca nemestrina Taxon ID: 9545 795615411 XP_011729700.1 (RefSeq)
Mandrillus leucophaeus Taxon ID: 9568 795293309 XP_011821735.1 (RefSeq)
Cercocebus torquatus atys Taxon ID: 9531 795207358 XP_011938993.1 (RefSeq)

Sequence

Length of Enzyme (full-length): 285 | Length of Functional Domain: 285

1       10        20        30        40        50        60

MPEFQKSSVRIKNPTRVEEIICGLIKGGAAKLQIITDFDMTLSRFSYKGKRCPTCHNIID
NCKLVTDECRKKLLQLKEKYYAIEVDPVLTVEEKYPYMVEWYTKSHGLLVEQALPKAKLK
EIVAESDVMLKEGYENFFDKLQQHSIPVFIFSAGIGDVLEEVIRQAGVYHPNVKVVSNFM
DFDETGVLKGFKGELIHVFNKHDGALRNTEYFNQLKDNSNIILLGDSQGDLRMADGVANV
EHILKIGYLNDRVDELLEKYMNSYDIVLVQDESLEVANSILQKIL
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

Subgroup CAR This EFD conserves 6/6 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
37 Asp (D) side chain Mg2+ ligand; nucleophile covalent catalysis -- reactant,
metal ligand -- binding 		ICS PubMed:16672222
39 Asp (D) side chain Mg2+ ligand; general acid (donates proton); general base (activates nucleophile) metal ligand -- binding,
proton relay -- reactant 		ICS PubMed:16672222
41 Thr (T) side chain Stabilizes nucleophilic Asp electrostatic stabiliser -- spectator ICS PubMed:16672222
201 Lys (K) side chain Binds phosphate substrate binding -- binding ICS PubMed:16672222
226 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:16672222
230 Asp (D) side chain Stabilizes nucleophilic Asp electrostatic stabiliser -- spectator ICS PubMed:16672222

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
2VKQ Crystal Structure Of Human Cytosolic 5'-Nucleotidase Iii ( Cn-Iii, Nt5C3) In Complex With Beryllium Trifluoride Cytosolic 5'-Nucleotidase Iii 9 2.5 Beryllium Trifluoride Ion • Magnesium Ion CSA • PDB • PDBSum
2CN1 Crystal Structure Of Human Cytosolic 5'-Nucleotidase Iii ( Nt5C3)(Casp Target) Cytosolic 5'-Nucleotidase Iii 9 2.67 CSA • PDB • PDBSum
2JGA Crystal Structure Of Human Cytosolic 5'-Nucleotidase Iii In Complex With Phosphate And Magnesium Cytosolic 5'-Nucleotidase Iii 9 3.01 Phosphate Ion • 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
Feb. 11, 2017, 2:44 a.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.