Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

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

  ⌊ C1.5.5: Heptose Bisphosphate Phosphatase Like

  ⌊ FunctionalDomain C1.5.5: Heptose Bisphosphate Phosphatase Like (ID 127820)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Mesorhizobium loti Taxon ID: 381 122921333 URP

Uniprot

Protein NameAccessionEC Number Identifier
D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase Q98I56 3.1.3.82 GMHBB_RHILO (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 218 | Length of Functional Domain: 185

1       10        20        30        40        50        60

GXADKTGTPHPLTEPGVWIERIGGRVFPPHLPALFLDRDGTINVDTDYPSDPAEIVLRPQ
XLPAIATANRAGIPVVVVTNQSGIARGYFGWSAFAAVNGRVLELLREEGVFVDXVLACAY
HEAGVGPLAIPDHPXRKPNPGXLVEAGKRLALDLQRSLIVGDKLADXQAGKRAGLAQGWL
VDGEAAVQPGFAIRPLRDSSELGDLLAAIETLGRDNRS
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
37 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
39 Asp (D) side chain general acid, general base; Mg2+ ligand metal ligand -- binding,
proton relay -- reactant 		ICS PubMed:20050614
45 Asp (D) side chain Mg2+ ligand (via water) metal ligand -- binding ICS PubMed:20050614
79 Thr (T) side chain binds phosphate moiety of substrate substrate binding -- binding ICS PubMed:20050614
137 Lys (K) side chain binds phosphate moiety of substrate substrate binding -- binding ICS PubMed:20050614
162 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:20050614

Catalyzed Reaction

D-glycero-D-manno-heptose-1,7-bisphosphate 7-phosphatase

+ +
D-glycero-D-manno-heptose 1,7-bisphosphate
4188		 water
15377		 D-glycero-D-manno-heptose 1-phosphate
28137		 phosphoric acid
26078

EC: 3.1.3.- | IntEnz: 3.1.3.- | Kegg: 3.1.3.- | BioCyc: 3.1.3.- | BRENDA: 3.1.3.- |

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
2O2X Crystal Structure Of A Putative Had-Like Phosphatase (Mll2559) From Mesorhizobium Loti At 1.50 A Resolution Hypothetical Protein 2 1.5 Selenomethionine • Glycerol 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, 8:18 a.m. update curation agent sbrown setDomainBoundaries.py
update domain end position 209 213
update domain start position 30 29
EC number assigned by UniProtKB accession ID.