Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

    ⌊ Subgroup C1.6: Phosphoserine Phosphatase Like

  ⌊ FunctionalDomain C1.6: Phosphoserine Phosphatase Like (ID 274546)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Bacillus subtilis subsp. subtilis str. 168 Taxon ID: 224308 16078424 NP_389243.1 (RefSeq) PRP URP
Bacillus subtilis Taxon ID: 1423 489338546 WP_003245748.1 (RefSeq) URP
Bacillus subtilis Taxon ID: 1423 846136035 AKN13482.1 (Genbank) URP
Show All

Uniprot

Protein NameAccessionEC Number Identifier
2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase O31667 3.1.3.87 MTNX_BACSU (Swiss-Prot)

Sequence

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

1       10        20        30        40        50        60

MTTRKPFIICDFDGTITMNDNIINIMKTFAPPEWMALKDGVLSKTLSIKEGVGRMFGLLP
SSLKEEITSFVLEDAKIREGFREFVAFINEHEIPFYVISGGMDFFVYPLLEGIVEKDRIY
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

Catalyzed Reaction

2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase

+ +
2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-enyl phosphate
50605		 water
15377		 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one
49252		 phosphoric acid
26078

EC: 3.1.3.87 | IntEnz: 3.1.3.87 | Kegg: 3.1.3.87 | BioCyc: 3.1.3.87 | BRENDA: 3.1.3.87

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
April 30, 2014, 5:28 a.m. update curation agent sbrown setDomainBoundaries.py
update domain end position 215 224
update domain start position 4 2
EC number assigned by UniProtKB accession ID.