Top Level Name

  ⌊ Superfamily (core) Enolase

  ⌊ FunctionalDomain uncharacterized Enolase superfamily sequence (ID 3794613)

Superfamily Assignment Evidence Code(s) IEA
This entry was last updated onDec. 10, 2016

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Escherichia coli Taxon ID: 562 798931027 WP_045907256.1 (RefSeq) URP
Escherichia coli Taxon ID: 562 788906058 KJW56151.1 (Genbank) URP

Sequence

Length of Enzyme (full-length): 446 | Length of Functional Domain: 446

1       10        20        30        40        50        60

MSSQFTTPVVTEMQVIPVAGHDSMLMNLSGAHAPFFTRNIVIIKDNSGHTGVGEIPGGEK
IRKTLEDAIPLVVGKTLGKYKNVLTLVRNTFADRDAGGRGLQTFDLRTTIHVVTGIEAAM
LDLLGQHLGVNVASLLGDGQQRSEVEMLGYLFFVGDRKATPLPYQSQPDDSCDWYRLRHE
EAMTPDAVVRLAEAAYEKYGFNDFKLKGGVLAGEEEAESIVALAQRFPQARITLAPNGAW
SLNEAIKIGKYLKGSLAYAEDPCGAEQGFSGREVMAEFRRATGLPTATNMIATDWRQMGH
TLSLQSVDIPLADPHFWTMQGSVRVAQMCHEFGLTWGSHSNNHFDISLAMFTHVAAAAPG
KITAIDTHWIWQEGNQRLTKEPFEIKGGLVQVPEKPGLGVEIDMDQVMKAHELYQKHGLG
ARDDAMGMQYLIPGWTFDNKRPCMVR
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
235 Ala (A) side chain MISMATCH: This residue does not match the specified amino acid type of D,E, and thus may not function in the same manner as other sequences in the superfamily
260 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
289 Asn (N) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982

Structures

PDB ID Title Molecule Name Number of
EFDs
Resolution (Å) Mutant? Het group Links
4GYP Crystal Structure Of The Heterotetrameric Complex Of Glucd And Glucdrp From E. Coli K-12 Mg1655 Glucarate Dehydratase • Glucarate Dehydratase-Related Protein 791 2.1 Magnesium Ion
(5 more ⇓)
CSA • PDB • PDBSum
1ECQ E. Coli Glucarate Dehydratase Bound To 4-Deoxyglucarate Glucarate Dehydratase 365 2.0 4-Deoxyglucarate
(2 more ⇓)
CSA • PDB • PDBSum
1EC9 E. Coli Glucarate Dehydratase Bound To Xylarohydroxamate Glucarate Dehydratase 365 2.0 Magnesium Ion
(2 more ⇓)
CSA • PDB • PDBSum
1EC8 E. Coli Glucarate Dehydratase Bound To Product 2,3-Dihydroxy-5-Oxo-Hexanedioate Glucarate Dehydratase 365 1.9 Magnesium Ion
(2 more ⇓)
CSA • PDB • PDBSum
1EC7 E. Coli Glucarate Dehydratase Native Enzyme Glucarate Dehydratase 365 1.9 Magnesium Ion • Isopropyl Alcohol CSA • PDB • PDBSum
1JDF Glucarate Dehydratase From E.Coli N341D Mutant Glucarate Dehydratase 363 2.0 Yes Magnesium Ion
(2 more ⇓)
CSA • PDB • PDBSum
3PWI Crystal Structure Of The Mutant P34A Of D-Glucarate Dehydratase From Escherichia Coli Complexed With Product 5-Keto-4-Deoxy-D-Glucarate Glucarate Dehydratase 363 2.23 Yes Magnesium Ion
(2 more ⇓)
CSA • PDB • PDBSum
1JCT Glucarate Dehydratase, N341L Mutant Orthorhombic Form Glucarate Dehydratase 363 2.75 Yes Magnesium Ion
(2 more ⇓)
CSA • PDB • PDBSum
3PWG Crystal Structure Of The Mutant S29G.P34A Of D-Glucarate Dehydratase From Escherichia Coli Complexed With Product 5-Keto-4-Deoxy-D-Glucarate Glucarate Dehydratase 359 2.0 Yes Magnesium Ion
(2 more ⇓)
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.
EC number assigned by UniProtKB accession ID.