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 116721)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Rattus norvegicus Taxon ID: 10116 57863283 NP_001009409.1 (RefSeq) PRP URP
Rattus norvegicus Taxon ID: 10116 149031100 EDL86127.1 (Genbank) PRP URP
Rattus norvegicus Taxon ID: 10116 56541034 AAH87587.1 (Genbank) PRP URP
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Uniprot

Protein NameAccessionEC Number Identifier
N-acylneuraminate-9-phosphatase Q5M969 3.1.3.29 NANP_RAT (Swiss-Prot)

Sequence

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

1       10        20        30        40        50        60

MGLSRVRAVFFDLDNTLIDTAGASRRGMLEVIKLLQSKYHYKEEAEVICDKVQVKLSKEC
FHPYSTCITDVRTSHWEEAIQETKGGADNRKLAEECYFLWKSTRLQHMTLEEDVKAMLTE
LRKEVRLLLLTNGDRQTQREKIEACACQSYFDAIVVGGEQKEEKPAPSIFYHCCDLLGVQ
PGDCVMVGDTLETDIQGGLNAGLKATVWINKSGGVPLTSSPMPHYMVSSVLELPALLQSI
DCKVSMSV
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

Catalyzed Reaction

N-acylneuraminate-9-phosphatase

+ +
N-acylneuraminic acid 9-phosphate
15840		 water
15377		 N-acylneuraminate
60073		 phosphoric acid
26078

EC: 3.1.3.29 | IntEnz: 3.1.3.29 | Kegg: 3.1.3.29 | BioCyc: 3.1.3.29 | BRENDA: 3.1.3.29

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
2GFH Crystal Structure Of A N-Acetylneuraminic Acid Phosphatase (Nanp) From Mus Musculus At 1.90 A Resolution Haloacid Dehalogenase-Like Hydrolase Domain Containing 4 5 1.9 Sodium Ion
(3 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, 5:01 p.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.