Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

    ⌊ Subgroup C2.B: Phosphomannomutase and Phosphatase Like

  ⌊ FunctionalDomain uncharacterized C2.B: Phosphomannomutase and Phosphatase Like subgroup sequence (ID 466632)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Bacillus subtilis Taxon ID: 1423 505196181 WP_015383283.1 (RefSeq) URP
Bacillus subtilis HJ5 Taxon ID: 1453990 808339586 AKD34444.1 (Genbank) URP
Bacillus subtilis subsp. subtilis str. BAB-1 Taxon ID: 1302650 472253793 AGI28324.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
n/a M4KTL5 M4KTL5_BACIU (TrEMBL)

Sequence

Length of Enzyme (full-length): 282 | Length of Functional Domain: 263

1       10        20        30        40        50        60

MLLSKKSEYKTLSTVEHPQYIVFCDFDETYFPHTIDEQKQKDIYELENYLEQKSKDGELI
IGWVTGSSIESILDKMGRGKFRYFPHFIASDLGTEITYFSEHNFGQQDNKWNSRINEGFS
KEKVEKLVKQLHENHNILLNPQTQLGKSRYKHNFYYQEQDEINDKKNLLAIEKICEEYGV
SVNINRCNPLAGDPEDSYDVDFIPIGTGKNEIVTFMLEKYNLNTERAIAFGDSGNDVRML
QAVGNGYLLKNATQEAKNLHHLITDSEYSKGITNTLKKLIGS
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
25 Asp (D) side chain Mg2+ ligand, nucleophile: attacks phosphate moiety of substrate to form covalent intermediate covalent catalysis -- reactant,
metal ligand -- binding 		ICS PubMed:21961705
27 Asp (D) side chain general acid, sometimes general base, Mg2+ ligand metal ligand -- binding,
proton relay -- reactant 		ICS PubMed:16540464
65 Thr (T) side chain Helps position phosphoryl group steric role -- spectator ICS PubMed:16540464
209 Lys (K) side chain None -- ISS PubMed:21961705
232 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:21961705
236 Asp (D) side chain None -- ISS PubMed:21961705

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
Aug. 1, 2014, 2:42 p.m. update curation agent updateSuperfamily.py setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.