Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

    ⌊ Subgroup C1.5: HAD, Beta-PGM, Phosphatase Like

  ⌊ C1.5.6: HAD, Beta-PGM, Phosphatase Like

     ⌊ Family glycerol-3-phosphate phosphatase

  ⌊ FunctionalDomain glycerol-3-phosphate phosphatase (ID 2206)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
n/a 756901444 AJN19855.1 (Genbank)
n/a 756729181 AJM56120.1 (Genbank)
n/a 756334110 AJL10509.1 (Genbank)
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Uniprot

Protein NameAccessionEC Number Identifier
Glycerol-1-phosphate phosphohydrolase 1 {ECO:0000305} P41277 GPP1_YEAST (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 271 | Length of Functional Domain: 271

1       10        20        30        40        50        60

MKRFNVLKYIRTTKANIQTIAMPLTTKPLSLKINAALFDVDGTIIISQPAIAAFWRDFGK
DKPYFDAEHVIHISHGWRTYDAIAKFAPDFADEEYVNKLEGEIPEKYGEHSIEVPGAVKL
CNALNALPKEKWAVATSGTRDMAKKWFDILKIKRPEYFITANDVKQGKPHPEPYLKGRNG
LGFPINEQDPSKSKVVVFEDAPAGIAAGKAAGCKIVGIATTFDLDFLKEKGCDIIVKNHE
SIRVGEYNAETDEVELIFDDYLYAKDDLLKW
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
136 Thr (T) side chain interacts with substrate/intermediate substrate binding -- binding ISS
Subgroup CAR This EFD conserves 2/2 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
39 Asp (D) side chain Mg2+ ligand, nucleophile: attacks phosphate moiety of intermediate to form covalent intermediate covalent catalysis -- reactant,
metal ligand -- binding 		ICS PubMed:12081483
168 Lys (K) side chain None -- ICS PubMed:10956028 PubMed:12081483
Family CAR This EFD conserves 4/4 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
39 Asp (D) side chain nucleophile: attacks phosphate moiety of substrate to form covalent intermediate covalent catalysis -- reactant ISS
41 Asp (D) side chain None -- ISS
168 Lys (K) side chain None -- ISS
200 Asp (D) side chain None -- ISS

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
2QLT Crystal Structure Of An Isoform Of Dl-Glycerol-3-Phosphatase, Rhr2P, From Saccharomyces Cerevisiae (Dl)-Glycerol-3-Phosphatase 1 10 1.6 Mercury (Ii) Ion
(4 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
Nov. 3, 2014, 9:25 a.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.