Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup mandelate racemase

     ⌊ Family rhamnonate dehydratase

  ⌊ FunctionalDomain rhamnonate dehydratase (ID 454993)

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 Taxon ID: 562 486204195 WP_001551380.1 (RefSeq) URP
Escherichia coli Taxon ID: 562 767825376 KJH05690.1 (Genbank) URP
Escherichia coli 6-175-07_S1_C3 Taxon ID: 1444114 660159483 KEM52721.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
n/a A0A0D8W949 A0A0D8W949_ECOLX (TrEMBL)
n/a A0A064TKK3 A0A064TKK3_ECOLX (TrEMBL)
n/a T6A705 T6A705_ECOLX (TrEMBL)
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Sequence

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

1       10        20        30        40        50        60

MTLPKIKQVRAWFTGGATAEKGAGGGDYHDQGANHWIDDHIATPMSKYRDYEQSRQSFGI
NVLGTLIVEVEAENGQTGFAVSTAGEMGCFIVEKHLNRFIEGKCVSDIKLIHDQMLNATL
YYSGSGGLVMNTISCVDLALWDLFGKVVGLPVYKLLGGAVRDEIQFYATGARPDLAKEMG
FIGGKMPTHWGPHDGDAGIHKDAAMVADMREKCGEDFWLMLDCWMSQDVNYATKLAHACA
PYNLKWIEECLPPQQYEGYRELKRNAPVGMMVTSGEHHGTLQSFRTLSETGIDIMQPDVG
WCGGLTTLVEIAAIAKSRGQLVVPHGSSVYSHHAVITFTNTPFSEFLMTSPDCSTMRPQF
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 5/5 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 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
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 His (H) side chain abstracts proton from C2 of substrate; acid catalyst for vinylogous departure of 2-OH group; protonates C-3 to replace 3-OH group with a solvent-derived hydrogen proton relay -- reactant ICS PubMed:18754693
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, 2:56 a.m. update curation agent updateSuperfamily.py setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.