Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup mandelate racemase

     ⌊ Family L-fuconate dehydratase

  ⌊ FunctionalDomain L-fuconate dehydratase (ID 338)

Superfamily Assignment Evidence Code(s) ISS
Family Assignment Evidence Code CFM PubMed:17144652
This entry was last updated onNov. 21, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Xanthomonas campestris pv. campestris str. ATCC 33913 Taxon ID: 190485 21233491 NP_639408.1 (RefSeq) PRP URP
Xanthomonas campestris Taxon ID: 339 499349845 WP_011039138.1 (RefSeq) URP
Xanthomonas campestris pv. campestris str. ATCC 33913 Taxon ID: 190485 21115341 AAM43290.1 (Genbank) PRP URP
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Uniprot

Protein NameAccessionEC Number Identifier
L-fuconate dehydratase {ECO:0000303|PubMed:17144652} Q8P3K2 FUCD_XANCP (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 441 | Length of Functional Domain: 435

1       10        20        30        40        50        60

MRTIIALETHDVRFPTSRELDGSDAMNPDPDYSAAYVVLRTDGAEDLAGYGLVFTIGRGN
DVQTAAVAALAEHVVGLSVDKVIADLGAFARRLTNDSQLRWLGPEKGVMHMAIGAVINAA
WDLAARAANKPLWRFIAELTPEQLVDTIDFRYLSDALTRDEALAILRDAQPQRAARTATL
IEQGYPAYTTSPGWLGYSDEKLVRLAKEAVADGFRTIKLKVGANVQDDIRRCRLARAAIG
PDIAMAVDANQRWDVGPAIDWMRQLAEFDIAWIEEPTSPDDVLGHAAIRQGITPVPVSTG
EHTQNRVVFKQLLQAGAVDLIQIDAARVGGVNENLAILLLAAKFGVRVFPHAGGVGLCEL
VQHLAMADFVAITGKMEDRAIEFVDHLHQHFLDPVRIQHGRYLAPEVPGFSAEMHPASIA
EFSYPDGRFWVEDLAASKAKA
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
248 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
274 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
301 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
248 Asp (D) side chain metal binding ligand metal ligand -- binding ICS
274 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
301 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
324 Asp (D) side chain controls pKa of catalytic His perturbates pKa -- spectator IDA
351 His (H) side chain proton abstraction (general base) proton relay -- reactant IDA
Family CAR This EFD conserves 6/6 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
220 Lys (K) side chain abstracts alpha proton (base); donates proton to enediolate intermediate proton relay -- reactant ICS PubMed:17144652
248 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:17144652
274 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:17144652
301 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:17144652
324 Asp (D) side chain Controls pKa of H407 perturbates pKa -- spectator ICS PubMed:17144652
351 His (H) side chain acid catalyst for beta elimination reaction proton relay -- reactant ICS PubMed:17144652

Catalyzed Reaction

L-fuconate dehydratase

+
L-fuconate
21291		 2-dehydro-3-deoxy-L-fuconate
37448		 water
15377

EC: 4.2.1.68 | IntEnz: 4.2.1.68 | Kegg: 4.2.1.68 | BioCyc: 4.2.1.68 | BRENDA: 4.2.1.68

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
2HXT Crystal Structure Of L-Fuconate Dehydratase From Xanthomonas Campestris Liganded With Mg++ And D-Erythronohydroxamate L-Fuconate Dehydratase 31 1.7 Magnesium Ion • (2R,3R)-N,2,3,4-Tetrahydroxybutanamide CSA • PDB • PDBSum
2HNE Crystal Structure Of L-Fuconate Dehydratase From Xanthomonas Campestris Pv. Campestris Str. Atcc 33913 L-Fuconate Dehydratase 31 2.0 Magnesium Ion CSA • PDB • PDBSum
1YEY Crystal Structure Of L-Fuconate Dehydratase From Xanthomonas Campestris Pv. Campestris Str. Atcc 33913 L-Fuconate Dehydratase 21 2.34 Selenomethionine • Magnesium Ion CSA • PDB • PDBSum
2HXU Crystal Structure Of K220A Mutant Of L-Fuconate Dehydratase From Xanthomonas Campestris Liganded With Mg++ And L-Fuconate L-Fuconate Dehydratase 25 1.8 Magnesium Ion
(2 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
April 30, 2014, 2:26 a.m. update curation agent sbrown setDomainBoundaries.py
update domain end position 432 435
update domain start position 3 1
EC number assigned by UniProtKB accession ID.