Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

    ⌊ Subgroup C1.8: polynucleotide 5'-hydroxyl-kinase c-terminal phosphatase like

  ⌊ FunctionalDomain uncharacterized C1.8: polynucleotide 5'-hydroxyl-kinase c-terminal phosphatase like subgroup sequence (ID 471646)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Escherichia phage ECML-134 Taxon ID: 1204522 712915055 YP_009102692.1 (RefSeq) URP
Escherichia phage ECML-134 Taxon ID: 1204522 397134236 AFO10743.1 (Genbank) URP

Uniprot

Protein NameAccessionEC Number Identifier
n/a I6ZYF5 I6ZYF5_9CAUD (TrEMBL)

Sequence

Length of Enzyme (full-length): 302 | Length of Functional Domain: 149

1       10        20        30        40        50        60

MMKKIILTIGCPGSGKSTWAREFIAKNPGFYNINRDDYRQSIMAHEERDEYKYTKKKEGI
VTGMQFDTAKSILYGGDSVKGVIISDTNLNPERRLAWETFAKEYGWKVEHKVFDVPWTEL
VKRNSKRGTKAVPIDVLRSMYKSMREYLGLPLYKGTPGKPKAVIFDVDGTLAKMNGRGPY
DLEKCDTDIINPMVVELSKMYALMGYQIVVVSGRESGTEEDPTKYYRMTRKWVEDIADVP
LVMQCQREQGDTRKDDVVKEEIFWKYIAPHFDVKLAIDDRTQVVEMWRRIGVECWQVASG
DF
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
166 Asp (D) side chain nucleophile: forms covalent intermediate covalent catalysis -- reactant ISS
Subgroup CAR This EFD conserves 7/7 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
166 Asp (D) side chain Mg2+ ligand, nucleophile: attacks phosphate moiety of substrate to form covalent intermediate covalent catalysis -- reactant,
metal ligand -- binding 		IDA PubMed:12220496
168 Asp (D) side chain Mg2+ ligand, binds phosphate moiety of substrate electrostatic stabiliser -- spectator,
metal ligand -- binding 		ICS PubMed:12220496
212 Ser (S) side chain binds phosphate moiety of substrate substrate binding -- binding ICS PubMed:12220496
214 Arg (R) side chain positions D15 steric role -- spectator IDA PubMed:12220496
255 Asp (D) side chain None -- IDA PubMed:12220496
259 Lys (K) side chain binds phosphate moiety of substrate substrate binding -- binding ICS PubMed:12220496
279 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:12220496

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
2IA5 T4 Polynucleotide Kinase/Phosphatase With Bound Sulfate And Magnesium. Polynucleotide Kinase 6 2.9 Magnesium Ion
(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
Aug. 1, 2014, 3:06 p.m. update curation agent updateSuperfamily.py setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.