Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

    ⌊ Subgroup C2.B: Phosphomannomutase and Phosphatase Like

  ⌊ C2.B.1: Sucrose Phosphatase Like

  ⌊ FunctionalDomain C2.B.1: Sucrose Phosphatase Like (ID 105187)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Bacillus subtilis subsp. subtilis str. 168 Taxon ID: 224308 237640626 PRP URP
Bacillus subtilis subsp. subtilis str. 168 Taxon ID: 224308 237640625 PRP URP
Bacillus subtilis subsp. subtilis str. 168 Taxon ID: 224308 237640624 PRP URP
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Uniprot

Protein NameAccessionEC Number Identifier
Kanosamine-6-phosphate phosphatase O07565 3.1.3.92 NTDB_BACSU (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 289 | Length of Functional Domain: 263

1       10        20        30        40        50        60

SNAXLLSKKSEYKTLSTVEHPQYIVFCDFDETYFPHTIDEQKQQDIYELEDYLEQKSKDG
ELIIGWVTGSSIESILDKXGRGKFRYFPHFIASDLGTEITYFSEHNFGQQDNKWNSRINE
GFSKEKVEKLVKQLHENHNILLNPQTQLGKSRYKHNFYYQEQDEINDKKNLLAIEKICEE
YGVSVNINRCNPLAGDPEDSYDVDFIPIGTGKNEIVTFXLEKYNLNTERAIAFGDSGNDV
RXLQTVGNGYLLKNATQEAKNLHNLITDSEYSKGITNTLKKLIGFXRRK
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

Subgroup CAR This EFD conserves 6/6 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
28 Asp (D) side chain Mg2+ ligand, nucleophile: attacks phosphate moiety of substrate to form covalent intermediate covalent catalysis -- reactant,
metal ligand -- binding 		ICS PubMed:15937230
30 Asp (D) side chain Mg2+ ligand, binds and orients phosphate group metal ligand -- binding,
steric role -- spectator 		ICS PubMed:15937230
68 Thr (T) side chain Binds and orients phosphate group steric role -- spectator ICS PubMed:15937230
212 Lys (K) side chain Orients Asp nucleophile, Binds and orients phosphate group steric role -- spectator ICS PubMed:15937230
235 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:15937230
239 Asp (D) side chain Mg2+ ligand when metal in noncatalytic position metal ligand -- binding ICS PubMed:15937230

Catalyzed Reaction

kanosamine-6-phosphate phosphatase

+ +
3-amino-3-deoxy-6-O-phosphono-D-glucopyranose
31748		 water
15377		 3-amino-3-deoxy-D-glucopyranose
72725		 phosphoric acid
26078

EC: 3.1.3.92 | IntEnz: 3.1.3.92 | Kegg: 3.1.3.92 | BioCyc: 3.1.3.92 | BRENDA: 3.1.3.92

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
3GYG Crystal Structure Of Yhjk (Haloacid Dehalogenase-Like Hydrolase Protein) From Bacillus Subtilis Ntd Biosynthesis Operon Putative Hydrolase Ntdb 7 2.45 Selenomethionine • Magnesium Ion 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
April 30, 2014, 7:14 a.m. update curation agent sbrown setDomainBoundaries.py
update domain end position 285 283
EC number assigned by UniProtKB accession ID.