Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup glucarate dehydratase

  ⌊ FunctionalDomain uncharacterized glucarate dehydratase subgroup sequence, enolase superfamily (ID 8975)

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

References to Other Databases

Genbank: obsolete GI = 75176350

Sequence

Length of Enzyme (full-length): 335 | Length of Functional Domain: 334

1       10        20        30        40        50        60

MAALEAALLDLLGKALNVPVCELLGPGKQRETITVLGYLFYIGDRTKTDLPYLENTPGNH
EWYQLRHQKAMNSEAVVRLAEASQDRYGFKDFKLKGGVLPGEQEINTVRALKKRFPDARI
TVDPNGAWLLDEAISLCKGLNDVLTYAEDPCGAEQGFSGREVMAEFRRATGLPVATNMIA
TNWREMGHAVMLNAVDIPLADPHFWTLSGAVRVAQLCDDWGLTWGCHSNNHFDISLAMFT
HVGAAAPGNPTAIDTHWIWQEGDCRLTKNPLEIKNGKIAVPDAPGLGVELDWKQVQKAHE
AYKRLPGGARNDAGPMQYLIPGWTFDRKRPVFGRH
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
123 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
148 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
177 Asn (N) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
Subgroup CAR This EFD conserves 6/6 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
95 Lys (K) side chain abstracts alpha proton from l-stereochemistry substrates proton relay -- reactant ISS PubMed:10769114
123 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:10769114
148 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:10769114
177 Asn (N) side chain metal binding ligand metal ligand -- binding ICS PubMed:10769114
201 Asp (D) side chain controls pKa of catalytic His perturbates pKa -- spectator ISS PubMed:10769114
227 His (H) side chain abstracts alpha proton from d-stereochemistry substates proton relay -- reactant ISS PubMed:10769114

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
4IL0 Crystal Structure Of Glucdrp From E. Coli K-12 Mg1655 (Efi Target Efi-506058) Glucarate Dehydratase-Related Protein 409 2.8 Citric Acid • Glycerol 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
Nov. 3, 2014, 2:34 a.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.