Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup mandelate racemase

  ⌊ FunctionalDomain uncharacterized mandelate racemase subgroup sequence, enolase superfamily (ID 17)

Superfamily Assignment Evidence Code(s) ISS
This entry was last updated onJune 3, 2017

References to Other Databases

Genbank

SpeciesGIAccessionModel
Archaeoglobus fulgidus DSM 4304 2648434 AAB89156.1 (Genbank) MB URP

Uniprot

Protein NameAccessionEC Number IdentifierModel
n/a O28181 O28181_ARCFU (TrEMBL) MB

Sequence

Length of Enzyme (full-length): 375 | Length of Functional Domain: 370

1       10        20        30        40        50        60

MLRKRSMKLGDLKVHTLAIPLREPIQFSWEPFPHPVYVFSIVEVEAGGFKGYSAIEFGAA
YKHFLETTVKLTIQGLDIEIEDVDARLLEVGSWAIQRLGALEVAIWDLIAKREGLPLYRL
LGGGRRKVKVYASTGRLLSAEETVKMVEKYAELGIDVVKLRFRRERINEDLEVLKAVARE
FSDVKISVDANQAWSYTPPYWSRKKAMKVAKELENFEVLWLEEPLWKDDVEGYRWLRENT
SIEISGGELEHGIQRFRMLIEGGAFDIVQADAVYSNGIQECRKVAALAEAFNLKFMPHAW
DPGLGWLANLHLAASLPEKLCPYIETPLDPLWWNEVMFGVLNGEVELEKGYAKLPEQPGL
GFEPDEEKMKKFRIA

FASTA | BLAST | HMM

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 2/3 Superfamily-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
189 Asp (D) side chain metal binding ligand metal ligand -- binding ISS
222 Glu (E) side chain metal binding ligand metal ligand -- binding ISS
247 Gly (G) side chain MISMATCH: This residue does not match the specified amino acid type of E,D,N,Q, and thus may not function in the same manner as other sequences in the superfamily
Subgroup CAR This EFD conserves 5/5 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
189 Asp (D) side chain metal binding ligand metal ligand -- binding ICS
222 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
248 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
271 Asp (D) side chain controls pKa of catalytic His perturbates pKa -- spectator IDA
298 His (H) side chain proton abstraction (general base) proton relay -- reactant IDA

Identical Sequences with Suspect Annotations in Other Databases (Schnoes et.al. 2009)

Genbank

Source DB Accession Species Source Annotation Misannot. Evid. Code Source Date
KEGG afu:AF2099 Archaeoglobus fulgidus DSM 4304 clcB; muconate cycloisomerase II (ClcB) [EC:5.5.1.7] [KO:K01860] SFA Feb. 17, 2006
NR 2648434 Archaeoglobus fulgidus DSM 4304 muconate cycloisomerase II (clcB) SFA Feb. 17, 2006
NR 11499682 Archaeoglobus fulgidus DSM 4304 muconate cycloisomerase II (clcB) SFA Feb. 17, 2006
TrEMBL O28181_ARCFU Archaeoglobus fulgidus Muconate cycloisomerase II (ClcB) SFA Feb. 17, 2006

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.