Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

    ⌊ Subgroup C1.6: Phosphoserine Phosphatase Like

  ⌊ FunctionalDomain uncharacterized C1.6: Phosphoserine Phosphatase Like subgroup sequence (ID 466832)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Bacillus subtilis Taxon ID: 1423 505196405 WP_015383507.1 (RefSeq) URP
Bacillus subtilis Taxon ID: 1423 825064089 AKI91813.1 (Genbank) URP
Bacillus subtilis HJ5 Taxon ID: 1453990 808339906 AKD34764.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
n/a M4KR13 M4KR13_BACIU (TrEMBL)

Sequence

Length of Enzyme (full-length): 235 | Length of Functional Domain: 223

1       10        20        30        40        50        60

MTTRKPFIICDFDGTITMNDNIINIMKTFAPPEWVALKDGVLSKTLSIKEGVGQMFGLLP
SRLKEEITSFVLEDAKIREGFREFVAFINEHEIPFYVISGGMDFFVYPLLEGIVEKDRIY
CNHASFDNDYIHIDWPHSCKGTCSNQCGCCKPSVIHELSEPNQYIIMIGDSVTDVEAAKL
SDLCFARDYLLNECREQNLNHLPYQDFYEIRKEIENVKEVQEWLQNKNAGESSLK
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
11 Asp (D) side chain Mg2+ ligand, nucleophile: attacks phosphate moiety of substrate to form covalent intermediate covalent catalysis -- reactant,
metal ligand -- binding 		ICS PubMed:12051918
13 Asp (D) side chain Mg2+ ligand, general acid (donates proton to leaving group), general base (activates water) metal ligand -- binding,
proton relay -- reactant 		ICS PubMed:12051918
99 Ser (S) side chain interacts with phosphate oxygen, facilitating hydrolysis activation -- spectator ICS PubMed:12051918
151 Lys (K) side chain forms cationic cavity that facilitates hydrolysis of phosphate electrostatic stabiliser -- spectator ICS PubMed:12051918
170 Asp (D) side chain Mg2+ ligand metal ligand -- binding ISS PubMed:11835514
174 Asp (D) side chain Positions Lys steric role -- spectator ICS PubMed:11835514

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
2FEA Crystal Structure Of Mtnx Phosphatase From Bacillus Subtilis At 2.00 A Resolution 2-Hydroxy-3-Keto-5-Methylthiopentenyl-1-Phosphatephosphatase 5 2.0 Selenomethionine
(3 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, 2:43 p.m. update curation agent updateSuperfamily.py setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.