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 2207)

Superfamily Assignment Evidence Code(s) FSM PubMed:9649311
Family Assignment Evidence Code CFM PubMed:8662716
This entry was last updated onNov. 22, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Saccharomyces cerevisiae S288c Taxon ID: 559292 86558907 NP_012211.2 (RefSeq) PRP URP
Saccharomyces cerevisiae YJM1592 Taxon ID: 1294387 766282274 AJR53688.1 (Genbank) URP
Saccharomyces cerevisiae YJM1573 Taxon ID: 1294385 766281890 AJR53306.1 (Genbank) URP
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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): 250 | Length of Functional Domain: 250

1       10        20        30        40        50        60

MPLTTKPLSLKINAALFDVDGTIIISQPAIAAFWRDFGKDKPYFDAEHVIHISHGWRTYD
AIAKFAPDFADEEYVNKLEGEIPEKYGEHSIEVPGAVKLCNALNALPKEKWAVATSGTRD
MAKKWFDILKIKRPEYFITANDVKQGKPHPEPYLKGRNGLGFPINEQDPSKSKVVVFEDA
PAGIAAGKAAGCKIVGIATTFDLDFLKEKGCDIIVKNHESIRVGEYNAETDEVELIFDDY
LYAKDDLLKW
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
115 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
18 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
147 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
18 Asp (D) side chain nucleophile: attacks phosphate moiety of substrate to form covalent intermediate covalent catalysis -- reactant ISS
20 Asp (D) side chain None -- ISS
147 Lys (K) side chain None -- ISS
179 Asp (D) side chain None -- ISS

Catalyzed Reaction

glycerol-1-phosphatase

+ +
glycerol 1-phosphate(2-)
231935		 water
15377		 glycerol
17754		 hydrogenphosphate
43474

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

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.