Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup mandelate racemase

     ⌊ Family gluconate dehydratase

  ⌊ FunctionalDomain gluconate dehydratase (ID 51)

Superfamily Assignment Evidence Code(s) ISS
Family Assignment Evidence Code IES PubMed:15474024
This entry was last updated onNov. 21, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Sulfolobus solfataricus Taxon ID: 2287 497677502 WP_009991686.1 (RefSeq) URP
Sulfolobus solfataricus Taxon ID: 2287 800906528 AKA78709.1 (Genbank) URP
Sulfolobus solfataricus Taxon ID: 2287 800903834 AKA76016.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
D-gluconate/D-galactonate dehydratase {ECO:0000303|PubMed:15474024} Q97U27 GAD_SULSO (Swiss-Prot)
n/a A0A0E3MGU8 A0A0E3MGU8_SULSF (TrEMBL)
n/a D0KR11 D0KR11_SULS9 (TrEMBL)

Sequence

Length of Enzyme (full-length): 395 | Length of Functional Domain: 393

1       10        20        30        40        50        60

MRIREIEPIVLTSKEKGSATWASIMIVTRVITENGEVGYGEAVPTLRVISVYNAIKQVSK
AYIGKEVEEVEKNYHEWYKQDFYLARSFESATAVSAIDIASWDIIGKELGAPIHKLLGGK
TRDRVPVYANGWYQDCVTPEEFAEKAKDVVKMGYKALKFDPFGPYYDWIDERGLREAEER
VKAVREAVGDNVDILIEHHGRFNANSAIMIAKRLEKYNPGFMEEPVHHEDVIGLRKYKAS
THLRVALGERLISEKETAFYVEEGLVNILQPDLTNIGGVTVGRSVIKIAEANDVEVAFHN
AFGSIQNAVEIQLSAVTQNLYLLENFYDWFPQWKRDLVYNETPVEGGHVKVPYKPGLGVS
INEKIIEQLRAEPIPLDVIEEPVWVVKGTWKNYGV
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 3/3 Superfamily-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
197 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
223 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
249 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
Subgroup CAR This EFD conserves 5/5 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
197 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
223 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
249 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
272 Asp (D) side chain controls pKa of catalytic His perturbates pKa -- spectator IDA
299 His (H) side chain proton abstraction (general base) proton relay -- reactant IDA
Family CAR This EFD conserves 7/7 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
197 Glu (E) side chain metal binding ligand metal ligand -- binding ISS
199 His (H) side chain general acid proton relay -- reactant ISS
223 Glu (E) side chain metal binding ligand metal ligand -- binding ISS
249 Glu (E) side chain metal binding ligand metal ligand -- binding ISS
272 Asp (D) side chain proton abstraction proton relay -- reactant ISS
299 His (H) side chain proton abstraction (general base) proton relay -- reactant ISS
324 Glu (E) side chain stabilizes transition state electrostatic stabiliser -- spectator ISS

Catalyzed Reaction

gluconate dehydratase

+
D-gluconate
18391		 2-dehydro-3-deoxy-D-gluconate
57990		 water
15377

EC: 4.2.1.39 | IntEnz: 4.2.1.39 | Kegg: 4.2.1.39 | BioCyc: 4.2.1.39 | BRENDA: 4.2.1.39

Curation History
Time Change Annotation Old Value New Value
Nov. 3, 2014, 2:33 a.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.