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 127796)

Superfamily Assignment Evidence Code(s) IEA
This entry was last updated onFeb. 13, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Bacteroides thetaiotaomicron VPI-5482 Taxon ID: 226186 29345887 NP_809390.1 (RefSeq) PRP URP
Bacteroides thetaiotaomicron Taxon ID: 818 499419823 WP_011107287.1 (RefSeq) URP
Bacteroides thetaiotaomicron VPI-5482 Taxon ID: 226186 29337780 AAO75584.1 (Genbank) PRP URP
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Uniprot

Protein NameAccessionEC Number Identifier
D-glycero-alpha-D-manno-heptose-1,7-bisphosphate 7-phosphatase Q8AAI7 3.1.3.83 GMHBA_BACTN (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 156 | Length of Functional Domain: 147

1       10        20        30        40        50        60

MRLQDIDVTGFETLLLDRDGVVNRLRPDDYVKKWEEFEFLPGVLEILKAWNTHFKYIFIV
TNQRGVGKEIMSEEDLKHIHERMISEVKNYGGRIDRIYYCTALTDSDINRKPGIGMFLQI
LRDYPDIDKAKCLMIGDSDSDIKFAKNCGIVGIKVI
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 5/6 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
17 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
19 Asp (D) side chain general acid, general base; Mg2+ ligand metal ligand -- binding,
proton relay -- reactant 		ICS PubMed:20050614
25 Leu (L) side chain MISMATCH: This residue does not match the specified amino acid type of D,E, and thus may not function in the same manner as other sequences in the subgroup
61 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
137 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.- |

Curation History
Time Change Annotation Old Value New Value
April 30, 2014, 8:18 a.m. update curation agent sbrown setDomainBoundaries.py
update domain start position 11 10
EC number assigned by UniProtKB accession ID.