Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup mandelate racemase

  ⌊ FunctionalDomain uncharacterized mandelate racemase subgroup sequence (ID 2575089)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Streptomyces sp. MUSC135 Taxon ID: 1355015 759702054 WP_043417237.1 (RefSeq) URP
Streptomyces sp. MUSC135 Taxon ID: 1355015 745662923 KIE33077.1 (Genbank) URP

Sequence

Length of Enzyme (full-length): 324 | Length of Functional Domain: 311

1       10        20        30        40        50        60

RINDLWQTMYRAGFYRGGPILMSAVAGIDQALWDIKGKVLGVPVYELLGGLVRDKMRTYS
WVGGDRPADVIAGMKALQAVGFDHFKLNGCEEMGIIDTSRAVDAAVAKVAEIRSAFGNTV
EFGLDFHGRVSAPMAKVLIKELEPYRPLFIEEPVLAEQAETYARLAAHTHLPIAAGERMF
SRFDFKRVLEAGGVSILQPDLSHAGGITECVKIAAMAEAYDVALAPHCPLGPIALAACLH
VDFVSWNATLQEQSMGIHYNKGAELLDYVRNKADFALEGGYIRPPRLPGLGVDIDEALVI
ERSKEAPDWRNPVWRHADGSVAEW
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
125 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
151 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
177 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
125 Asp (D) side chain metal binding ligand metal ligand -- binding ICS
151 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
177 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
200 Asp (D) side chain controls pKa of catalytic His perturbates pKa -- spectator IDA
227 His (H) side chain proton abstraction (general base) proton relay -- reactant 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
May 8, 2015, 4:15 a.m. update curation agent updateSuperfamily.py setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.