Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup mandelate racemase

     ⌊ Family rhamnonate dehydratase

  ⌊ FunctionalDomain rhamnonate dehydratase (ID 278307)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Shigella boydii Taxon ID: 621 491132296 WP_004990723.1 (RefSeq) URP
Shigella boydii 5216-82 Taxon ID: 766141 332093849 EGI98903.1 (Genbank) URP

Uniprot

Protein NameAccessionEC Number Identifier
n/a F3WFM8 F3WFM8_9ENTR (TrEMBL)

Sequence

Length of Enzyme (full-length): 401 | Length of Functional Domain: 401

1       10        20        30        40        50        60

MTLPKIKQVRAWFTGGATAEKGAGGGDYHDQGANHWIDDHIATPMSKYRDYEQSRQSFGI
NVLGTLVVEVEAENGQTGFAVSTAGEMGCFIVEKHLNRFIEGKCVSDIKLIHDQMLNATL
YYSGSGGLVMNTISCVDLALWDLFGKVVGLPVYKLLGGAVRDEIQFYATGARPDLAKEMG
FIGGKMPTHWGPHDGDAGIRKDAAMVADMREKCGEDFWLMLDCWMSQDVNYATKLAHACA
PYNLKWIEECLPPQQYEGYRELKRNAPVGMMVTSGEHHGTLQSFRTLSETGIDIMQPDVG
WCGGLTTLVEIAAIAKSRGQLVVPYGSSVYSHHAVITFTNTPFSEFLMTSPDCSTMRPQF
DPILLNEPVPVNGRIHKSVLDKPGFGVELNRDCNLKRPYSH
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
222 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
248 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
276 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
Subgroup CAR This EFD conserves 4/5 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
222 Asp (D) side chain metal binding ligand metal ligand -- binding ICS
248 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
276 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
298 Asp (D) side chain controls pKa of catalytic His perturbates pKa -- spectator IDA
325 Tyr (Y) side chain MISMATCH: This residue does not match the specified amino acid type of H, and thus may not function in the same manner as other sequences in the subgroup
Family CAR This EFD conserves 6/7 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
185 Lys (K) side chain electrophilic catalyst covalent catalysis -- reactant ICS PubMed:18754693
222 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:18754693
248 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:18754693
276 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:18754693
298 Asp (D) side chain controls pKa of catalytic His perturbates pKa -- spectator ICS PubMed:18754693
325 Tyr (Y) side chain MISMATCH: This residue does not match the specified amino acid type of H, and thus may not function in the same manner as other sequences in the family
345 Glu (E) side chain electrophilic catalyst covalent catalysis -- reactant ICS PubMed:18754693

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
2I5Q Crystal Structure Of Apo L-Rhamnonate Dehydratase From Escherichia Coli L-Rhamnonate Dehydratase 319 2.1 CSA • PDB • PDBSum
3CXO Crystal Structure Of L-Rhamnonate Dehydratase From Salmonella Typhimurium Complexed With Mg And 3-Deoxy-L-Rhamnonate Putative Galactonate Dehydratase 312 2.0 3,6-Dideoxy-L-Arabino-Hexonic Acid
(2 more ⇓) 		CSA • PDB • PDBSum
2P3Z Crystal Structure Of L-Rhamnonate Dehydratase From Salmonella Typhimurium L-Rhamnonate Dehydratase 312 1.8 Sodium Ion CSA • PDB • PDBSum
3BOX Crystal Structure Of L-Rhamnonate Dehydratase From Salmonella Typhimurium Complexed With Mg L-Rhamnonate Dehydratase 312 1.8 Magnesium Ion CSA • PDB • PDBSum
2GSH Crystal Structure Of L-Rhamnonate Dehydratase From Salmonella Typhimurium L-Rhamnonate Dehydratase 312 2.39 Magnesium Ion • Glycerol CSA • PDB • PDBSum
3D47 Crystal Structure Of L-Rhamnonate Dehydratase From Salmonella Typhimurium Complexed With Mg And D-Malate Putative Galactonate Dehydratase 312 1.8 Magnesium Ion • Malate Ion CSA • PDB • PDBSum
3D46 Crystal Structure Of L-Rhamnonate Dehydratase From Salmonella Typhimurium Complexed With Mg And L-Tartrate Putative Galactonate Dehydratase 312 1.9 Magnesium Ion • L(+)-Tartaric Acid 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, 3:13 a.m. update curation agent updateSuperfamily.py setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.