Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup glucarate dehydratase

  ⌊ FunctionalDomain uncharacterized glucarate dehydratase subgroup sequence, enolase superfamily (ID 286)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Escherichia coli O157:H7 str. SS52 Taxon ID: 1330457 734590553 AJA27754.1 (Genbank) URP
Escherichia coli O157:H7 EDL933 Taxon ID: 155864 667693512 AIG70121.1 (Genbank) URP
Escherichia coli O157:H7 str. SS17 Taxon ID: 1328859 666005449 AIF95306.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
n/a C3SX27 C3SX27_ECOLX (TrEMBL)
n/a L9HZW2 L9HZW2_ECOLX (TrEMBL)
n/a A0A0F6FBG4 A0A0F6FBG4_ECO57 (TrEMBL)
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Sequence

Length of Enzyme (full-length): 365 | Length of Functional Domain: 364

1       10        20        30        40        50        60

MVQQVHKGNQAADFDTFGKGAWTFELRVNAVAALEAALLDLLGKALNVPVCELLGPGKQR
DAITVLGYLFYIGDRTKTDLPYLENTPGNHEWYQLRHQKAMNSEAVVRLAEASQDRYGFK
DFKLKGGVLPGEQEIDTVRALKKRFPDARITVDPNGAWLLDEAISLCKGLNDVLTYAEDP
CGAEQGFSGREVMAEFRRATGLPVATNMIATNWREMGHAVMLNAVDIPLADPHFWTLSGA
VRVAQLCDDWGLTWGCHSNNHFDISLAMFTHVGAAAPGNPTAIDTHWIWQEGDCRLTQNP
LEIKNGKIAVPDAPGLGVELDWEQVQKAHEAYKRLPGGARNDAGPMQYLIPGWTFDRKRP
VFGRH
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
153 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
178 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
207 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
125 Lys (K) side chain abstracts alpha proton from l-stereochemistry substrates proton relay -- reactant ISS PubMed:10769114
153 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:10769114
178 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:10769114
207 Asn (N) side chain metal binding ligand metal ligand -- binding ICS PubMed:10769114
231 Asp (D) side chain controls pKa of catalytic His perturbates pKa -- spectator ISS PubMed:10769114
257 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.

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 ece:Z4103 Escherichia coli O157:H7 EDL933 ygcY; putative glucarate dehydratase [EC:4.2.1.40] [KO:K01706] BTC Feb. 17, 2006
TrEMBL Q8X6T9_ECO57 Escherichia coli O157:H7 Putative glucarate dehydratase BTC 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.