Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup mandelate racemase

     ⌊ Family D-galactonate dehydratase

  ⌊ FunctionalDomain D-galactonate dehydratase (ID 1395029)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Ralstonia pickettii Taxon ID: 329 490770648 WP_004632875.1 (RefSeq) URP
Ralstonia pickettii OR214 Taxon ID: 1264675 480893223 ENZ76399.1 (Genbank) URP

Uniprot

Protein NameAccessionEC Number Identifier
n/a R0E2M5 R0E2M5_RALPI (TrEMBL)

Sequence

Length of Enzyme (full-length): 382 | Length of Functional Domain: 369

1       10        20        30        40        50        60

MKITRLTTYRLPPRWMFLKVETDEGVTGWGEPVIEGRARTVEAAVHELSDYLIGQDPSRI
NDLWQTMYRAGFYRGGPILMSAIAGIDQALWDIKGKVLGVPVYELLGGLVRDKMRTYSWV
GGDRPADVIAGMKALQAGGFDHFKLNGCEEMGIIDTSRAVDAAVAKVAEIRSAFGNTIEF
GLDFHGRVSAPMAKVLIKELEPYRPLFIEEPVLAEQAETYARLAAHTHLPIAAGERMFSR
FDFKRVLEAGGVSILQPDLSHAGGITECVKIAAMAEAYDVALAPHCPLGPIALAACLHVD
FVSWNATLQEQSMGIHYNKGAELLDYVRNKADFALEGGYIRPPRLPGLGVDIDEALVIER
SKEAPDWRNPVWRHADGSVAEW
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
183 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
209 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
235 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
183 Asp (D) side chain metal binding ligand metal ligand -- binding ICS
209 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
235 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
258 Asp (D) side chain controls pKa of catalytic His perturbates pKa -- spectator IDA
285 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
183 Asp (D) side chain metal binding ligand metal ligand -- binding ICS
185 His (H) side chain general acid proton relay -- reactant IDA
209 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
235 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
258 Asp (D) side chain controls pKa of H287 perturbates pKa -- spectator ISS
285 His (H) side chain abstracts alpha proton (base) proton relay -- reactant IDA
310 Glu (E) side chain stabilizes transition state electrostatic stabiliser -- spectator IDA

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
3RRA Crystal Structure Of Enolase Prk14017 (Target Efi-500653) From Ralstonia Pickettii 12J With Magnesium Bound Putative D-Galactonate Dehydratase 12 2.3 Chloride Ion • Magnesium Ion CSA • PDB • PDBSum
3RR1 Crystal Structure Of Enolase Prk14017 (Target Efi-500653) From Ralstonia Pickettii 12J Putative D-Galactonate Dehydratase 12 1.95 Chloride Ion • Malate Ion 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, 2:59 a.m. update curation agent updateSuperfamily.py setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.