Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup mandelate racemase

     ⌊ Family galactarate dehydratase 3

  ⌊ FunctionalDomain galactarate dehydratase 3 (ID 2578827)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Agrobacterium rhizogenes Taxon ID: 359 736488918 WP_034506795.1 (RefSeq) URP

Sequence

Length of Enzyme (full-length): 395 | Length of Functional Domain: 395

1       10        20        30        40        50        60

MKIDRMRVFMTRDKDRPRVIVALDTDDGLTGWGECYNHGPDKALPPLLDYLYGFIAGQDP
TRIDYLVNLLIQQSRFPPGALGLAAISALDHCLWDLSAKAVNVPVYKLLGGAVRDRIKVY
AGVYTAPDAPAAREEFDRLNAEWGFTAFKLSPWRIDMHAHRWGNVVKASADYFRSLRETV
RDDYEIAFDAHAKIFEPVAARQLGNALAPYDPLFYEEPLRPENIEMWGELKQGLNCVLAT
GESLYNRNEFLRLLQVKGADLIQPDICVVGGISEMRRIATLAEAHFVGVAPHNPMGPLAT
AVNVHFSAATQNFRILEYRLPKGQAYVYGGNDIEKRQGETRYVVDPYLPKDGYLELRPDR
PGWGVEMDEKAMEEEGYIHWQRRVPKRPDGSYAFA
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
189 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
216 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
242 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
189 Asp (D) side chain metal binding ligand metal ligand -- binding ICS
216 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
242 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
265 Asp (D) side chain controls pKa of catalytic His perturbates pKa -- spectator IDA
292 His (H) side chain proton abstraction (general base) proton relay -- reactant IDA
Family CAR This EFD conserves 7/7 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
189 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:24926996
191 His (H) side chain general acid proton relay -- reactant IME PubMed:24926996
216 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:24926996
242 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:24926996
265 Asp (D) side chain controls pKa of His that functions as general base activation -- spectator ICS PubMed:24926996
292 His (H) side chain general base proton relay -- reactant IME PubMed:24926996
317 Glu (E) side chain None -- ISS PubMed:24926996

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
4JN8 Crystal Structure Of An Enolase (Putative Galactarate Dehydratase, Target Efi-500740) From Agrobacterium Radiobacter, Bound Sulfate, No Metal Ion, Ordered Active Site Enolase 8 1.4 Sulfate Ion
(2 more ⇓) 		CSA • PDB • PDBSum
4JN7 Crystal Structure Of An Enolase (Putative Galactarate Dehydratase, Target Efi-500740) From Agrobacterium Radiobacter, Bound Na And L-Malate, Ordered Active Site Enolase 8 1.15 Sodium Ion
(4 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
May 8, 2015, 4:25 a.m. update curation agent updateSuperfamily.py setDomainBoundaries.py
July 9, 2015, 3:34 a.m. update curation agent setDomainBoundaries.py sbrown
update curation agent sbrown setDomainBoundaries.py
update domain end position 380 395
update name uncharacterized mandelate racemase subgroup sequence galactarate dehydratase 3
EC number assigned by UniProtKB accession ID.