Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup mandelate racemase

     ⌊ Family L-fuconate dehydratase

  ⌊ FunctionalDomain L-fuconate dehydratase (ID 331)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Xanthomonas axonopodis pv. citri str. 306 Taxon ID: 190486 21110617 AAM39023.1 (Genbank) URP

Uniprot

Protein NameAccessionEC Number Identifier
n/a Q8PF00 Q8PF00_XANAC (TrEMBL)

Sequence

Length of Enzyme (full-length): 415 | Length of Functional Domain: 410

1       10        20        30        40        50        60

MNPDPDYSAAYVVLRTDAADDLAGYGLVFTIGRGNDVQTAAVAALAEHVVGLSVEEVIAD
LGAFARRLTNDSQLRWLGPEKGVMHMAIGAVINAAWDLAARAAKKPLWRYIAELSPEQLV
DTIDFRYLTDALTRDEALAILRAAQPQRAQRIATLIEQGYPAYTTSPGWLGYSDEKLVRL
AKEAVADGFRTIKLKVGANVRDDIRRCRLAREAIGPDIAMAVDANQRWDVGPAIDWMRQL
AEFDIAWIEEPTSPDDVLGHAAIRQGIAPVPVSTGEHTQNRVVFKQLLQAGAVDLIQIDA
ARVGGVNENLAILLLAAKFNVRVFPHAGGVGLCELVQHLAMADFVAITGKMEDRAIEFVD
HLHQHFLDPVRIRHGRYLAPEAAGFSAEMHAASIAEFSYPGGRFWVEDLAASAKG
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
223 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
249 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
223 Asp (D) side chain metal binding ligand metal ligand -- binding ICS
249 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
276 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
299 Asp (D) side chain controls pKa of catalytic His perturbates pKa -- spectator IDA
326 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
195 Lys (K) side chain abstracts alpha proton (base); donates proton to enediolate intermediate proton relay -- reactant ICS PubMed:17144652
223 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:17144652
249 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:17144652
276 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:17144652
299 Asp (D) side chain Controls pKa of H407 perturbates pKa -- spectator ICS PubMed:17144652
326 His (H) side chain acid catalyst for beta elimination reaction proton relay -- reactant ICS PubMed:17144652

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
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
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
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
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 407 410
EC number assigned by UniProtKB accession ID.