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 126259)

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

References to Other Databases

Genbank: obsolete GI = 296200390

Uniprot

Protein NameAccessionEC Number Identifier
n/a F6PJD3 F6PJD3_CALJA (TrEMBL)

Sequence

Length of Enzyme (full-length): 248 | Length of Functional Domain: 238

1       10        20        30        40        50        60

MGLSRVRAVFFDLDNTLIDTAGASRRGMLEVIKLLQSKYHYKEEAEIICDKVQVKLSKEC
FHPYNTCITDLRTSHWEEAIQETKGGAANRKLAEECYFLWKSTRLQHMTLAEDVKAMLTE
LRKEVRLLLLTNGDKQTQREKIEACACQSYFDAVVVGGEQREEKPAPSIFYYCCSLLGVQ
PGDCVMVGDTLETDIQGGLNAGLKATVWINKNGVVPLKSSPVPHYIVSSVLELPALLQSI
DCKVSMSA
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 2/2 Superfamily-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
12 Asp (D) side chain nucleophile: forms covalent intermediate covalent catalysis -- reactant ISS
131 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
12 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
164 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
2W4M The Crystal Structure Of Human N-Acetylneuraminic Acid Phosphatase, Nanp N-Acylneuraminate-9-Phosphatase 7 2.6 Phosphate Ion
(2 more ⇓) 		CSA • PDB • PDBSum
4KNW The Crystal Structure Of Human Hdhd4 In Complex With Magnesium And The Phosphate Mimetic Vanadate N-Acylneuraminate-9-Phosphatase 7 2.7 Vanadate Ion • Magnesium Ion CSA • PDB • PDBSum
4KNV The Crystal Structure Of Apo Human Hdhd4 From Se-Mad N-Acylneuraminate-9-Phosphatase 6 1.99 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
Aug. 1, 2014, 4:14 p.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.