Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup mandelate racemase

     ⌊ Family rhamnonate dehydratase

  ⌊ FunctionalDomain rhamnonate dehydratase (ID 1559942)

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
Taxon ID: 570 516510853 WP_017899291.1 (RefSeq)
Klebsiella pneumoniae Taxon ID: 573 839707738 KMH81244.1 (Genbank) URP
Klebsiella pneumoniae Taxon ID: 573 839638992 KMH13621.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
n/a A0A1H5XIK9 A0A1H5XIK9_9ENTR (TrEMBL)
n/a A0A0J4TCB0 A0A0J4TCB0_KLEPN (TrEMBL)
n/a A0A1C1ET19 A0A1C1ET19_9ENTR (TrEMBL)

Sequence

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

1       10        20        30        40        50        60

MTLPKIKHVRAWFTGGATAEQGAGGGDYHDQGANHWIDDHIATPMSKYKQYEQSRQSFGI
NVLGTLIVEVEADNGQTGFAVSTAGEMGCFIVEKHLNRFIEGKCVSDIKLIHDQMLNATL
YYAGSGGLVMNTISCVDLALWDLFGKVVGLPVYKLLGGAVRDEIQFYATGARPDLAQEMG
FIGGKMPTHWGPHDGDAGIRKDVAMVADMREKCGPDFWLMLDCWMSQDVNYATKLAHACA
PYNLKWIEECLPPQQYEGYRELKRQAPAGMMVTSGEHHGTLQSFRTLSETGIDIMQPDVG
WCGGLTTLVEIAAIAKARGQLVVPHGSSVYSHHAVITFTNTPFSEFLMTSPDCATLRPQF
DPILLGEPVPERGRIHKSVLDKPGFGVELNRDCNLKRPYQH
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
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, 3:36 a.m. update curation agent updateSuperfamily.py setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.