Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

    ⌊ Subgroup C1.4: 5'-Nucleotidase Like

  ⌊ FunctionalDomain C1.4: 5'-Nucleotidase Like (ID 35869)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Rattus norvegicus Taxon ID: 10116 157823103 NP_001101332.1 (RefSeq) PRP URP
Rattus norvegicus Taxon ID: 10116 564346996 XP_006236612.1 (RefSeq) PRP URP
Rattus norvegicus Taxon ID: 10116 183986025 AAI66444.1 (Genbank) PRP URP
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Uniprot

Protein NameAccessionEC Number Identifier
n/a B2GUX5 B2GUX5_RAT (TrEMBL)

Sequence

Length of Enzyme (full-length): 297 | Length of Functional Domain: 292

1       10        20        30        40        50        60

MTNQESAVRLEMMPEFQKSSVRIKNPTRVEEIICGLIKGGAAKLQIITDFDMTLSRFSYN
GKRCPTCHNIIDNCKLVTDECRRKLLQLKEQYYAIEVDPVLTVEEKFPYMVEWYTKSHGL
LIEQGIPKAKLKEIVADSDVMLKEGYENFFGKLQQHGIPVFIFSAGIGDVLEEVIRQAGV
YHSNVKVVSNFMDFDENGVLKGFKGELIHVFNKHDGALKNTDYFSQLKDNSNIILLGDSQ
GDLRMADGVANVEHILKIGYLNDRVDELLEKYMDSYDIVLVKEESLEVVNSILQKTL
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
49 Asp (D) side chain Mg2+ ligand; nucleophile covalent catalysis -- reactant,
metal ligand -- binding 		ICS PubMed:16672222
51 Asp (D) side chain Mg2+ ligand; general acid (donates proton); general base (activates nucleophile) metal ligand -- binding,
proton relay -- reactant 		ICS PubMed:16672222
53 Thr (T) side chain Stabilizes nucleophilic Asp electrostatic stabiliser -- spectator ICS PubMed:16672222
213 Lys (K) side chain Binds phosphate substrate binding -- binding ICS PubMed:16672222
238 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:16672222
242 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
2G0A X-Ray Structure Of Mouse Pyrimidine 5'-Nucleotidase Type 1 With Lead(Ii) Bound In Active Site Cytosolic 5'-Nucleotidase Iii 8 2.35 Selenomethionine
(2 more ⇓) 		CSA • PDB • PDBSum
2Q4T Ensemble Refinement Of The Protein Crystal Structure Of A Cytosolic 5'-Nucleotidase Iii From Mus Musculus Mm.158936 Cytosolic 5'-Nucleotidase Iii 8 2.35 Selenomethionine • 4-(2-Hydroxyethyl)-1-Piperazine Ethanesulfonic Acid CSA • PDB • PDBSum
2G09 X-Ray Structure Of Mouse Pyrimidine 5'-Nucleotidase Type 1, Product Complex Cytosolic 5'-Nucleotidase Iii 8 2.1 Selenomethionine
(3 more ⇓) 		CSA • PDB • PDBSum
2G08 X-Ray Structure Of Mouse Pyrimidine 5'-Nucleotidase Type 1, Product-Transition Complex Analog With Aluminum Fluoride Cytosolic 5'-Nucleotidase Iii 8 2.35 Selenomethionine
(2 more ⇓) 		CSA • PDB • PDBSum
2BDU X-Ray Structure Of A Cytosolic 5'-Nucleotidase Iii From Mus Musculus Mm.158936 Cytosolic 5'-Nucleotidase Iii 8 2.35 Selenomethionine • 4-(2-Hydroxyethyl)-1-Piperazine Ethanesulfonic Acid CSA • PDB • PDBSum
2G06 X-Ray Structure Of Mouse Pyrimidine 5'-Nucleotidase Type 1, With Bound Magnesium(Ii) Cytosolic 5'-Nucleotidase Iii 8 2.25 Selenomethionine
(2 more ⇓) 		CSA • PDB • PDBSum
2G07 X-Ray Structure Of Mouse Pyrimidine 5'-Nucleotidase Type 1, Phospho-Enzyme Intermediate Analog With Beryllium Fluoride Cytosolic 5'-Nucleotidase Iii 8 2.3 Selenomethionine
(2 more ⇓) 		CSA • PDB • PDBSum
4FE3 Structure Of Murine Cytosolic 5'-Nucleotidase Iii Complexed With Uridinine Monophosphate Cytosolic 5'-Nucleotidase 3 9 1.74 Yes Beta-Mercaptoethanol
(3 more ⇓) 		CSA • PDB • PDBSum
4KX5 Cytosolic 5'-Nucleotidase Iii Complexed With Cytidine 5'-Monophosphate Cytosolic 5'-Nucleotidase 3 9 1.9 Yes Cytidine-5'-Monophosphate
(4 more ⇓) 		CSA • PDB • PDBSum
4KX3 Structure Of Murine Cytosolic 5'-Nucleotidase Iii Complexed With Thymidine Monophosphate Cytosolic 5'-Nucleotidase 3 9 2.1 Yes Thymidine-5'-Monophosphate
(4 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, 6:04 a.m. update curation agent sbrown setDomainBoundaries.py
update domain start position 12 6
EC number assigned by UniProtKB accession ID.