Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup mandelate racemase

     ⌊ Family D-galactonate dehydratase

  ⌊ FunctionalDomain D-galactonate dehydratase (ID 4899)

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
Taxon ID: 543 446627655 WP_000705001.1 (RefSeq)
Escherichia coli O104:H4 str. 2011C-3493 Taxon ID: 1133852 407479599 YP_006776748.1 (RefSeq) URP
Escherichia coli UMN026 Taxon ID: 585056 218707338 YP_002414857.1 (RefSeq) URP
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Uniprot

Protein NameAccessionEC Number Identifier
D-galactonate dehydratase 2 {ECO:0000255|HAMAP-Rule:MF_01289} B1LL17 DGOD2_ECOSM (Swiss-Prot)
D-galactonate dehydratase {ECO:0000255|HAMAP-Rule:MF_01289} A7ZTP7 DGOD_ECO24 (Swiss-Prot)
D-galactonate dehydratase {ECO:0000255|HAMAP-Rule:MF_01289} B7L836 DGOD_ECO55 (Swiss-Prot)
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Sequence

Length of Enzyme (full-length): 382 | Length of Functional Domain: 369

1       10        20        30        40        50        60

MKITKITTYRLPPRWMFLKIETDEGVVGWGEPVIEGRARTVEAAVHELGDYLIGQDPSRI
NDLWQVMYRAGFYRGGPILMSAIAGIDQALWDIKGKVLNAPVWQLMGGLVRDKIKAYSWV
GGDRPADVIDGIKTLREIGFDTFKLNGCEELGLIDNSRAVDAAVNTVAQIREAFGNQIEF
GLDFHGRVSAPMAKVLIKELEPYRPLFIEEPVLAEQAEYYPKLAAQTHIPLAAGERMFSR
FDFKRVLEAGGISILQPDLSHAGGITECYKIAGMAEAYDVTLAPHCPLGPIALAACLHID
FVSYNAVLQEQSMGIHYNKGAELLDFVKNKEDFSMVGGFFKPLTKPGLGVEIDEAKVIEF
SKNAPDWRNPLWRHEDNSVAEW
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
183 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
209 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
235 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
183 Asp (D) side chain metal binding ligand metal ligand -- binding ICS
209 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
235 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
258 Asp (D) side chain controls pKa of catalytic His perturbates pKa -- spectator IDA
285 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
183 Asp (D) side chain metal binding ligand metal ligand -- binding ICS
185 His (H) side chain general acid proton relay -- reactant IDA
209 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
235 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
258 Asp (D) side chain controls pKa of H287 perturbates pKa -- spectator ISS
285 His (H) side chain abstracts alpha proton (base) proton relay -- reactant IDA
310 Glu (E) side chain stabilizes transition state electrostatic stabiliser -- spectator IDA

Catalyzed Reaction

galactonate dehydratase

+
D-galactonate
12931		 2-dehydro-3-deoxy-D-galactonate
57989		 water
15377

EC: 4.2.1.6 | IntEnz: 4.2.1.6 | Kegg: 4.2.1.6 | BioCyc: 4.2.1.6 | BRENDA: 4.2.1.6

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.