Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

    ⌊ Subgroup C2.A: Pyridoxal Phosphate Phosphatase Like

  ⌊ FunctionalDomain C2.A: Pyridoxal Phosphate Phosphatase Like (ID 446853)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Saimiri boliviensis boliviensis Taxon ID: 39432 403283031 XP_003932931.1 (RefSeq)

Sequence

Length of Enzyme (full-length): 300 | Length of Functional Domain: 282

1       10        20        30        40        50        60

MARCERLRGAALRDVLGRAQGVLFDCDGVLWNGERAVPGAPELLERLARAGKAALFVSNN
SRRARPELALRFARLGFGGLRAEQLFSSALCAARLLRQRLPGPPDAPGAVFVLGGEGLRA
ELRAAGLRLAGDTGDDLGAGDGEAPRVRAVLVGYDEHFSFAKLSEACAHLRDPDCLLVAT
DRDPWHPLSDGSRTPGTGSLAAAVETASGRQALVVGKPSPYMFECITENFSMDPARTLMV
GDRLETDILFGHRCGMTTVLTLTGVSRLEEAQAYLAAGQQDLVPHYYVESIADLMEGLED
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
133 Thr (T) side chain interacts with substrate/intermediate substrate binding -- binding ISS
Subgroup CAR This EFD conserves 5/5 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
25 Asp (D) side chain Mg2+ ligand, nucleophile: attacks phosphate moiety of substrate to form covalent intermediate covalent catalysis -- reactant,
metal ligand -- binding 		ICS PubMed:16430214
58 Ser (S) side chain interacts with phosphate oxygen, facilitating hydrolysis activation -- spectator ICS PubMed:16430214
217 Lys (K) side chain Orients Asp nucleophile steric role -- spectator ICS PubMed:16430214
242 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:16430214
247 Asp (D) side chain Mg2+ ligand (via water) metal ligand -- binding ICS PubMed:16430214

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
2CFT Crystal Structure Of Human Pyridoxal 5'-Phosphate Phosphatase With Its Substrate Pyridoxal Phosphate Phosphatase 10 1.8 Calcium Ion • Pyridoxal-5'-Phosphate CSA • PDB • PDBSum
2CFS Crystal Structure Of Human Pyridoxal 5'-Phosphate Phosphatase Pyridoxal Phosphate Phosphatase 10 2.4 Magnesium Ion CSA • PDB • PDBSum
2P69 Crystal Structure Of Human Pyridoxal Phosphate Phosphatase With Plp Pyridoxal Phosphate Phosphatase 9 2.25 Selenomethionine
(2 more ⇓) 		CSA • PDB • PDBSum
2P27 Crystal Structure Of Human Pyridoxal Phosphate Phosphatase With Mg2+ At 1.9 A Resolution Pyridoxal Phosphate Phosphatase 9 1.9 Selenomethionine • Magnesium Ion CSA • PDB • PDBSum
2OYC Crystal Structure Of Human Pyridoxal Phosphate Phosphatase Pyridoxal Phosphate Phosphatase 9 1.72 Selenomethionine
(2 more ⇓) 		CSA • PDB • PDBSum
2CFR Crystal Structure Of Human Pyridoxal 5'-Phosphate Phosphatase Pyridoxal Phosphate Phosphatase 9 2.4 Selenomethionine • Magnesium Ion 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, 6:24 a.m. update curation agent sbrown setDomainBoundaries.py
update domain end position 300 299
update domain start position 19 18
EC number assigned by UniProtKB accession ID.