Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

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

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

  ⌊ FunctionalDomain C1.5.6: HAD, Beta-PGM, Phosphatase Like (ID 38303)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Saccharomyces cerevisiae Taxon ID: 4932 197253741 ACH54205.1 (Genbank)
Saccharomyces cerevisiae Taxon ID: 4932 197253739 ACH54204.1 (Genbank)
Saccharomyces cerevisiae Taxon ID: 4932 197253737 ACH54203.1 (Genbank)
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Uniprot

Protein NameAccessionEC Number Identifier
n/a B5LYQ9 B5LYQ9_YEASX (TrEMBL)

Sequence

Length of Enzyme (full-length): 171 | Length of Functional Domain: 171

1       10        20        30        40        50        60

YDAIAKFAPDFADEEYVNKLEGEIPEKYGEHSIEVPGAVKLCNALNALPKEKWAVATSGT
RDMAKKWFDILKIKRPEYFITANDVKQGKPHPEPYLKGRNGLGFPINEQDPSKSKVVVFE
DAPAGIAAGKAAGCKIVGIATTFDLDFLKEKGCDIIVKNHESIRVGEYNAE
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
57 Thr (T) side chain interacts with substrate/intermediate substrate binding -- binding ISS
Subgroup CAR This EFD conserves 1/2 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
89 Lys (K) side chain None -- ICS PubMed:10956028 PubMed:12081483

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.
EC number assigned by UniProtKB accession ID.