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 2477)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Shigella flexneri 2a str. 301 Taxon ID: 198214 24111636 NP_706146.1 (RefSeq)
Escherichia coli str. K-12 substr. MG1655 Taxon ID: 511145 16128193 NP_414742.1 (RefSeq) URP
Escherichia coli O157:H7 str. Sakai Taxon ID: 386585 15829456 NP_308229.1 (RefSeq)
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Uniprot

Protein NameAccessionEC Number Identifier
D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase P63229 3.1.3.82 GMHBB_ECO57 (Swiss-Prot)
D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase P63228 GMHBB_ECOLI (Swiss-Prot)
D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase P63230 3.1.3.82 GMHBB_SHIFL (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 191 | Length of Functional Domain: 185

1       10        20        30        40        50        60

MAKSVPAIFLDRDGTINVDHGYVHEIDNFEFIDGVIDAMRELKKMGFALVVVTNQSGIAR
GKFTEAQFETLTEWMDWSLADRDVDLDGIYYCPHHPQGSVEEFRQVCDCRKPHPGMLLSA
RDYLHIDMAASYMVGDKLEDMQAAVAANVGTKVLVRTGKPITPEAENAADWVLNSLADLP
QAIKKQQKPAQ
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
53 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
11 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
13 Asp (D) side chain general acid, general base; Mg2+ ligand metal ligand -- binding,
proton relay -- reactant 		ICS PubMed:20050614
19 Asp (D) side chain Mg2+ ligand (via water) metal ligand -- binding ICS PubMed:20050614
53 Thr (T) side chain binds phosphate moiety of substrate substrate binding -- binding ICS PubMed:20050614
111 Lys (K) side chain binds phosphate moiety of substrate substrate binding -- binding ICS PubMed:20050614
136 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
3ESQ Crystal Structure Of Calcium-Bound D,D-Heptose 1.7-Bisphosphate Phosphatase From E. Coli D,D-Heptose 1,7-Bisphosphate Phosphatase 37 1.7 Zinc Ion • Calcium Ion CSA • PDB • PDBSum
2GMW Crystal Structure Of D,D-Heptose 1.7-Bisphosphate Phosphatase From E. Coli. D,D-Heptose 1,7-Bisphosphate Phosphatase 37 1.5 Zinc Ion CSA • PDB • PDBSum
3ESR Crystal Structure Of D,D-Heptose1.7-Bisphosphate Phosphatase From E. Coli In Complex With Calcium And Phosphate D,D-Heptose 1,7-Bisphosphate Phosphatase 37 1.95 Zinc Ion
(2 more ⇓) 		CSA • PDB • PDBSum
3L1U Crystal Structure Of Calcium-Bound Gmhb From E. Coli. D,D-Heptose 1,7-Bisphosphate Phosphatase 37 1.95 Zinc Ion • Calcium Ion CSA • PDB • PDBSum
3L1V Crystal Structure Of Gmhb From E. Coli In Complex With Calcium And Phosphate. D,D-Heptose 1,7-Bisphosphate Phosphatase 37 1.95 Zinc Ion
(2 more ⇓) 		CSA • PDB • PDBSum
3L8E Crystal Structure Of Apo Form Of D,D-Heptose 1.7-Bisphosphate Phosphatase From E. Coli D,D-Heptose 1,7-Bisphosphate Phosphatase 37 1.64 Zinc Ion • Acetic Acid CSA • PDB • PDBSum
3L8G Crystal Structure Of D,D-Heptose 1.7-Bisphosphate Phosphatase From E. Coli Complexed With D-Glycero-D-Manno-Heptose 1 ,7-Bisphosphate D,D-Heptose 1,7-Bisphosphate Phosphatase 25 2.18 Selenomethionine
(4 more ⇓) 		CSA • PDB • PDBSum
3L8F Crystal Structure Of D,D-Heptose 1.7-Bisphosphate Phosphatase From E. Coli Complexed With Magnesium And Phosphate D,D-Heptose 1,7-Bisphosphate Phosphatase 25 1.79 Selenomethionine
(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
April 30, 2014, 5:15 a.m. update curation agent sbrown setDomainBoundaries.py
update domain end position 191 187
update domain start position 1 3
EC number assigned by UniProtKB accession ID.