Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

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

  ⌊ C1.5.5: Heptose Bisphosphate Phosphatase Like

  ⌊ FunctionalDomain uncharacterized C1.5.5: Heptose Bisphosphate Phosphatase Like subgroup sequence (ID 472576)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Bordetella bronchiseptica Taxon ID: 518 504877880 WP_015064982.1 (RefSeq) URP
Bordetella bronchiseptica 253 Taxon ID: 568707 412341591 YP_006970346.1 (RefSeq) URP
Bordetella bronchiseptica Taxon ID: 518 673485559 KFJ52024.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
n/a A0A1M8SEI2 A0A1M8SEI2_9MYCO (TrEMBL)
n/a A0A0C6P9H1 A0A0C6P9H1_BORBO (TrEMBL)

Sequence

Length of Enzyme (full-length): 179 | Length of Functional Domain: 179

1       10        20        30        40        50        60

MKLIILDRDGVVNQDSDAFVKSPDEWIALPGSLQAIARLTQADWTVVLATNQSGLARGLF
DTATLNAIHDKMHRALAQMGGVVDAIFMCPHGPEDGCACRKPLPGMYRDIARRYDIDLAG
VPAVGDSLRDLQAAAQAGCAPWLVQTGNGRKTLAQGGLPEGTRVCEDLAAMVEQLLQEA
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
50 Thr (T) side chain interacts with substrate/intermediate substrate binding -- binding ISS
Subgroup CAR This EFD conserves 6/6 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
7 Asp (D) side chain nucleophile: attacks phosphate moiety of substrate to form covalent intermediate; Mg2+ ligand covalent catalysis -- reactant,
metal ligand -- binding 		ICS PubMed:20050614
9 Asp (D) side chain general acid, general base; Mg2+ ligand metal ligand -- binding,
proton relay -- reactant 		ICS PubMed:20050614
15 Asp (D) side chain Mg2+ ligand (via water) metal ligand -- binding ICS PubMed:20050614
50 Thr (T) side chain binds phosphate moiety of substrate substrate binding -- binding ICS PubMed:20050614
101 Lys (K) side chain binds phosphate moiety of substrate substrate binding -- binding ICS PubMed:20050614
126 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:20050614

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
3L8H Crystal Structure Of D,D-Heptose 1.7-Bisphosphate Phosphatase From B. Bronchiseptica Complexed With Magnesium And Phosphate Putative Haloacid Dehalogenase-Like Hydrolase 4 1.68 Selenomethionine
(6 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, 3:11 p.m. update curation agent updateSuperfamily.py setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.