Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

    ⌊ Subgroup C1.4: 5'-Nucleotidase Like

  ⌊ FunctionalDomain C1.4: 5'-Nucleotidase Like (ID 35901)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
synthetic construct Taxon ID: 32630 649125457 AIC56422.1 (Genbank)
n/a 397148695 AFO15061.1 (Genbank)
n/a 314158346 ADR96969.1 (Genbank)
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Uniprot

Protein NameAccessionEC Number Identifier
Cytosolic 5'-nucleotidase 3A {ECO:0000305|PubMed:15968458, ECO:0000305|PubMed:24603684} Q9H0P0 5NT3A_HUMAN (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 286 | Length of Functional Domain: 286

1       10        20        30        40        50        60

MMPEFQKSSVRIKNPTRVEEIICGLIKGGAAKLQIITDFDMTLSRFSYKGKRCPTCHNII
DNCKLVTDECRKKLLQLKEKYYAIEVDPVLTVEEKYPYMVEWYTKSHGLLVQQALPKAKL
KEIVAESDVMLKEGYENFFDKLQQHSIPVFIFSAGIGDVLEEVIRQAGVYHPNVKVVSNF
MDFDETGVLKGFKGELIHVFNKHDGALRNTEYFNQLKDNSNIILLGDSQGDLRMADGVAN
VEHILKIGYLNDRVDELLEKYMDSYDIVLVQDESLEVANSILQKIL
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
184 Asp (D) side chain nucleophile: forms covalent intermediate covalent catalysis -- reactant ISS
Subgroup CAR This EFD conserves 6/6 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
38 Asp (D) side chain Mg2+ ligand; nucleophile covalent catalysis -- reactant,
metal ligand -- binding 		ICS PubMed:16672222
40 Asp (D) side chain Mg2+ ligand; general acid (donates proton); general base (activates nucleophile) metal ligand -- binding,
proton relay -- reactant 		ICS PubMed:16672222
42 Thr (T) side chain Stabilizes nucleophilic Asp electrostatic stabiliser -- spectator ICS PubMed:16672222
202 Lys (K) side chain Binds phosphate substrate binding -- binding ICS PubMed:16672222
227 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:16672222
231 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.