Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup glucarate dehydratase

     ⌊ Family glucarate dehydratase

  ⌊ FunctionalDomain glucarate dehydratase (ID 1398139)

Superfamily Assignment Evidence Code(s) IEA
Family Assignment Evidence Code IEA
This entry was last updated onNov. 21, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Escherichia coli O157:H7 str. EC4042 Taxon ID: 444449 365812948 URP
Escherichia coli O157:H7 str. EC4042 Taxon ID: 444449 365812947 URP
Escherichia coli O157:H7 str. EC4042 Taxon ID: 444449 365812946 URP
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Uniprot

Protein NameAccessionEC Number Identifier
Glucarate dehydratase P0AES2 4.2.1.40 GUDD_ECOLI (Swiss-Prot)

Sequence

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

1       10        20        30        40        50        60

MSSQFTTPVVTEMQVIPVAGHDSMLMNLGGAHAAFFTRNIVIIKDNSGHTGVGEIPGGEK
IRKTLEDAIPLVVGKTLGEYKNVLTLVRNTFADRDAGGRGLQTFDLRTTIHVVTGIEAAM
LDLLGQHLGVNVASLLGDGQQRSEVEMLGYLFFVGNRKATPLPYQSQPDDSCDWYRLRHE
EAMTPDAVVRLAEAAYEKYGFNDFKLKGGVLAGEEEAESIVALAQRFPQARITLDPNGAW
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 3/3 Superfamily-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
235 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
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
Subgroup CAR This EFD conserves 6/6 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
207 Lys (K) side chain abstracts alpha proton from l-stereochemistry substrates proton relay -- reactant ISS PubMed:10769114
235 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:10769114
260 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:10769114
289 Asn (N) side chain metal binding ligand metal ligand -- binding ICS PubMed:10769114
313 Asp (D) side chain controls pKa of catalytic His perturbates pKa -- spectator ISS PubMed:10769114
339 His (H) side chain abstracts alpha proton from d-stereochemistry substates proton relay -- reactant ISS PubMed:10769114
Family CAR This EFD conserves 7/7 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
207 Lys (K) side chain abstracts alpha proton from l-idarate proton relay -- reactant IDA PubMed:11513584
235 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:10769114
260 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:10769114
289 Asn (N) side chain metal binding ligand metal ligand -- binding ICS PubMed:10769114
313 Asp (D) side chain controls pKa of H385 perturbates pKa -- spectator ICS PubMed:10769114
339 His (H) side chain abstracts alpha proton from d-glucarate proton relay -- reactant IDA PubMed:11513584
341 Asn (N) side chain general acid (facilitates departure of 4-OH and stereospecific tautomerization) OR positions H339 to act as general acid proton relay -- reactant IDA PubMed:11513584

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
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
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
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
1JCT Glucarate Dehydratase, N341L Mutant Orthorhombic Form Glucarate Dehydratase 363 2.75 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.

Curation History
Time Change Annotation Old Value New Value
Aug. 1, 2014, 3:09 a.m. update curation agent updateSuperfamily.py setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.