Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

    ⌊ Subgroup C1.6: Phosphoserine Phosphatase Like

  ⌊ C1.6.1: Phosphoserine Phosphatase Like

     ⌊ Family phosphoserine phosphatase

  ⌊ FunctionalDomain phosphoserine phosphatase (ID 31954)

Superfamily Assignment Evidence Code(s) IEA
Family Assignment Evidence Code IEA
This entry was last updated onFeb. 13, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Methanocaldococcus jannaschii Taxon ID: 2190 15826096
Methanocaldococcus jannaschii Taxon ID: 2190 15826095

Uniprot

Protein NameAccessionEC Number Identifier
Phosphoserine phosphatase Q58989 SERB_METJA (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 211 | Length of Functional Domain: 209

1       10        20        30        40        50        60

MEKKKKLILFXFDSTLVNNETIDEIAREAGVEEEVKKITKEAMEGKLNFEQSLRKRVSLL
KDLPIEKVEKAIKRITPTEGAEETIKELKNRGYVVAVVSGGFDIAVNKIKEKLGLDYAFA
NRLIVKDGKLTGDVEGEVLKENAKGEILEKIAKIEGINLEDTVAVGDGANDISMFKKAGL
KIAFCAKPILKEKADICIEKRDLREILKYIK
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
11 (X) side chain MISMATCH: This residue does not match the specified amino acid type of D, and thus may not function in the same manner as other sequences in the superfamily
99 Ser (S) side chain interacts with substrate/intermediate substrate binding -- binding ISS
Subgroup CAR This EFD conserves 5/6 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
11 (X) side chain MISMATCH: This residue does not match the specified amino acid type of D, and thus may not function in the same manner as other sequences in the subgroup
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
20 Glu (E) side chain activates water (indirectly) activation -- spectator ICS PubMed:12051918
99 Ser (S) side chain interacts with phosphate oxygen, facilitating hydrolysis activation -- spectator ICS PubMed:12051918
144 Lys (K) side chain forms cationic cavity that facilitates hydrolysis of phosphate electrostatic stabiliser -- spectator ICS PubMed:12051918
167 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:12051918
Family CAR This EFD conserves 5/6 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
11 (X) side chain MISMATCH: This residue does not match the specified amino acid type of D, and thus may not function in the same manner as other sequences in the family
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
20 Glu (E) side chain activates water (indirectly) activation -- spectator ICS PubMed:12051918
99 Ser (S) side chain interacts with phosphate oxygen, facilitating hydrolysis activation -- spectator ICS PubMed:11342136
144 Lys (K) side chain forms cationic cavity that facilitates hydrolysis of phosphate electrostatic stabiliser -- spectator ICS PubMed:12051918
167 Asp (D) side chain Mg2+ ligand metal ligand -- binding IDA PubMed:10567362

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
1J97 Phospho-Aspartyl Intermediate Analogue Of Phosphoserine Phosphatase Phosphoserine Phosphatase 4 1.5 Aspartate Beryllium Trifluoride
(2 more ⇓) 		CSA • PDB • PDBSum
1F5S Crystal Structure Of Phosphoserine Phosphatase From Methanococcus Jannaschii Phosphoserine Phosphatase (Psp) 5 1.8 Phosphate Ion • Magnesium Ion CSA • PDB • PDBSum
1L7P Substrate Bound Phosphoserine Phosphatase Complex Structure Phosphoserine Phosphatase 4 1.9 Yes Selenomethionine
(2 more ⇓) 		CSA • PDB • PDBSum
1L7O Crystal Structure Of Phosphoserine Phosphatase In Apo Form Phosphoserine Phosphatase 4 2.2 Yes Selenomethionine
(2 more ⇓) 		CSA • PDB • PDBSum
1L7N Transition State Analogue Of Phosphoserine Phosphatase (Aluminum Fluoride Complex) Phosphoserine Phosphatase 4 1.8 Selenomethionine
(4 more ⇓) 		CSA • PDB • PDBSum
1L7M High Resolution Liganded Structure Of Phosphoserine Phosphatase (Pi Complex) Phosphoserine Phosphatase 4 1.48 Selenomethionine
(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
April 30, 2014, 5:55 a.m. update curation agent sbrown setDomainBoundaries.py
update domain start position 1 3
EC number assigned by UniProtKB accession ID.