Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup mandelate racemase

     ⌊ Family rhamnonate dehydratase

  ⌊ FunctionalDomain rhamnonate dehydratase (ID 5823)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Polaromonas sp. JS666 Taxon ID: 296591 499801706 WP_011482440.1 (RefSeq) URP
Polaromonas sp. JS666 Taxon ID: 296591 91696612 ABE43441.1 (Genbank) URP
Polaromonas sp. JS666 Taxon ID: 296591 123355908 URP

Uniprot

Protein NameAccessionEC Number Identifier
L-rhamnonate dehydratase Q12DF1 4.2.1.90 RHMD_POLSJ (Swiss-Prot)

Sequence

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

1       10        20        30        40        50        60

MNNMPTIKHVRAFTVRGGGADYHDQGSGHWIDDHISTPMGRYPEYRQSRQSFGINVLGTL
VVEIEASDGTVGFSVTTGGELGCWIVEKHLARFIEGAKVTDIEKIWDQMFNATLYYGRKG
IVLNTISGVDLALWDLLAKVRKEPVHALLGGPVRDELTFYATGARPDLAKKMGFIGGKLP
LHHGPAEREEGLKKNLELLGEMRQRVGDDFWLMYDCWMSLDVEYATRLANAASEYKLKWI
EEALPPDDYWGYAELRRNVPRGMLVTTGEHEATRWGFRMLLEMECCDILQPDVGWCGGIT
ELLKISALADAHGKLVVPHGSSVYSYHFVITRHNSPFSEFLMMAPKADEVVPMFNPMLLD
EPVPVNGRMKASALDAPGFGVRLNPECALQRPFPR
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
215 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
241 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
269 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
215 Asp (D) side chain metal binding ligand metal ligand -- binding ICS
241 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
269 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
292 Asp (D) side chain controls pKa of catalytic His perturbates pKa -- spectator IDA
319 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
178 Lys (K) side chain electrophilic catalyst covalent catalysis -- reactant ICS PubMed:18754693
215 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:18754693
241 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:18754693
269 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:18754693
292 Asp (D) side chain controls pKa of catalytic His perturbates pKa -- spectator ICS PubMed:18754693
319 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
339 Glu (E) side chain electrophilic catalyst covalent catalysis -- reactant ICS PubMed:18754693

Catalyzed Reaction

L-rhamnonate dehydratase

+
L-rhamnonate
58118		 2-dehydro-3-deoxy-L-rhamnonate
58371		 water
15377

EC: 4.2.1.90 | IntEnz: 4.2.1.90 | Kegg: 4.2.1.90 | BioCyc: 4.2.1.90 | BRENDA: 4.2.1.90

Curation History
Time Change Annotation Old Value New Value
Nov. 3, 2014, 2:34 a.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.