Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

    ⌊ Subgroup C1.4: 5'-Nucleotidase Like

  ⌊ FunctionalDomain C1.4: 5'-Nucleotidase Like (ID 35859)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Mus musculus Taxon ID: 10090 172072627 NP_080280.3 (RefSeq) PRP URP
Rattus norvegicus Taxon ID: 10116 564347000 XP_006236614.1 (RefSeq) PRP URP
Rattus norvegicus Taxon ID: 10116 149033246 EDL88047.1 (Genbank) PRP URP
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Uniprot

Protein NameAccessionEC Number Identifier
Cytosolic 5'-nucleotidase 3A {ECO:0000305|PubMed:16672222} Q9D020 5NT3A_MOUSE (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 331 | Length of Functional Domain: 292

1       10        20        30        40        50        60

MDRAAVARVGAVASASVCAVVAGVVLAQYIFTLKRKTGRKTKIIEMMPEFQKSSVRIKNP
TRVEEIICGLIKGGAAKLQIITDFDMTLSRFSYNGKRCPTCHNIIDNCKLVTDECRRKLL
QLKEQYYAIEVDPVLTVEEKFPYMVEWYTKSHGLLIEQGIPKAKLKEIVADSDVMLKEGY
ENFFGKLQQHGIPVFIFSAGIGDVLEEVIRQAGVYHSNVKVVSNFMDFDENGVLKGFKGE
LIHVFNKHDGALKNTDYFSQLKDNSNIILLGDSQGDLRMADGVANVEHILKIGYLNDRVD
ELLEKYMDSYDIVLVKEESLEVVNSILQKTL
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
83 Asp (D) side chain Mg2+ ligand; nucleophile covalent catalysis -- reactant,
metal ligand -- binding 		ICS PubMed:16672222
85 Asp (D) side chain Mg2+ ligand; general acid (donates proton); general base (activates nucleophile) metal ligand -- binding,
proton relay -- reactant 		ICS PubMed:16672222
87 Thr (T) side chain Stabilizes nucleophilic Asp electrostatic stabiliser -- spectator ICS PubMed:16672222
247 Lys (K) side chain Binds phosphate substrate binding -- binding ICS PubMed:16672222
272 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:16672222
276 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 46 40
EC number assigned by UniProtKB accession ID.