Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup mandelate racemase

  ⌊ FunctionalDomain uncharacterized mandelate racemase subgroup sequence (ID 2133752)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Agrobacterium sp. UNC420CL41Cvi Taxon ID: 1340437 651232346 WP_026372456.1 (RefSeq)

Sequence

Length of Enzyme (full-length): 378 | Length of Functional Domain: 378

1       10        20        30        40        50        60

MKITAVRTHLLEHRLDTPFESASMRFDRRAHILVEIECDDGTIGWGECLGPARPNAAVVQ
AYAGWLIGQDPRQTEKIWAVLYNALRDQGQRGLSLTALSGIDIALWDIKGKHYGASISML
LGGRWRESVRAYATGSFKRDGVDRVSDNALEMAERRAEGFHACKIKIGFGIEEDLRVIAA
VREAIGPDMRLMIDANHGYTVTEAITLGNRAADYGIDWFEEPVVPEQLDAYARVRAGQPI
PVAGGETWHGRYGMWQALSAGAVDILQPDLCGCGGFSETQKIATLATLQGVRIVPHVWGT
GVQIAAALQFMAAMTPDPVRVNPIEPIMEFDRTHNPFRQAVLREPIEAVNGIVAIPNGPG
LGIEINRDALLEFRMPDP
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
194 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
220 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
246 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
194 Asp (D) side chain metal binding ligand metal ligand -- binding ICS
220 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
246 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
269 Asp (D) side chain controls pKa of catalytic His perturbates pKa -- spectator IDA
296 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
4HPN Crystal Structure Of A Proposed Galactarolactone Cycloisomerase From Agrobacterium Tumefaciens, Target Efi-500704, With Bound Ca, Ordered Loops Putative Uncharacterized Protein 12 1.6 Calcium Ion
(2 more ⇓) 		CSA • PDB • PDBSum
4GGB Crystal Structure Of A Proposed Galactarolactone Cycloisomerase From Agrobacterium Tumefaciens, Target Efi-500704, With Bound Ca, Disordered Loops Putative Uncharacterized Protein 12 2.0 Calcium Ion • Chloride 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, 2:51 a.m. update curation agent updateSuperfamily.py setDomainBoundaries.py
Sept. 14, 2015, 3:11 a.m. update domain end position 377 378
EC number assigned by UniProtKB accession ID.