Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup mandelate racemase

     ⌊ Family L-lyxonate dehydratase

  ⌊ FunctionalDomain L-lyxonate dehydratase (ID 282)

Superfamily Assignment Evidence Code(s) ISS PubMed:24831290
Family Assignment Evidence Code IGS PubMed:24831290
This entry was last updated onNov. 21, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Pseudomonas aeruginosa PAO1 Taxon ID: 208964 15597411 NP_250905.1 (RefSeq) PRP URP
Pseudomonas aeruginosa PAO1-VE13 Taxon ID: 1367494 651879623 YP_008706369.1 (RefSeq) URP
Pseudomonas aeruginosa PAO1-VE2 Taxon ID: 1367493 651874250 YP_008694088.1 (RefSeq) URP
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Uniprot

Protein NameAccessionEC Number Identifier
n/a A0A1G5IR37 A0A1G5IR37_ACIBA (TrEMBL)
n/a A0A1E9BUL2 A0A1E9BUL2_9PSED (TrEMBL)
n/a A0A0P1DBK0 A0A0P1DBK0_PSEAI (TrEMBL)
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Sequence

Length of Enzyme (full-length): 391 | Length of Functional Domain: 391

1       10        20        30        40        50        60

MKIKSVRTRVFEWKGKVVPPQAHFCTNASDILFEKGDAMGSFRFHGWLVVEIETDDGLVG
IGNCALAPRVAKEIVDLYLAPICIGEDPFDNEYIWQKMYRRTHAWGRKGIGMAAISAVDL
AIWDIMGKAVNKPVFKLLGGRTKEKIWTYASKLYANDNLDAFLEEAQGYLNQGFTALKMR
FGYGPKDGPTGMRRNIEQVRALRELAGPDIDIMLECYMGWTLEYARRMLPKLAEFEPRWL
EEPVIADDIEGYVELKKMGIMPISGGEHEFTGHGFKDLLERRAVDVIQYDTNRVGGITAA
RKINAMAEAWSVPVIPHAGQLHNYHLTMASTASPMAEFFPVFDVEVGNELFYYVFKGEPQ
PVDGYIQLDDHKPGLGLEISEEHLKDFIIIE
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 Glu (E) 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
267 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 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
241 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
267 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
290 Asp (D) side chain controls pKa of catalytic His perturbates pKa -- spectator IDA
317 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 Electrophile electrophile -- reactant ISS PubMed:24831290
180 Arg (R) side chain None -- IME PubMed:24831290
215 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:24831290
241 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:24831290
267 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:24831290
290 Asp (D) side chain General base proton relay -- reactant ISS PubMed:24831290
317 His (H) side chain Forms hydrogen bond dyad with Asp general base activation -- spectator IME PubMed:24831290

Catalyzed Reaction

L-lyxonate dehydratase

+
L-Lyxonate
6268		 2-dehydro-3-deoxy-L-arabinonic acid
17647		 water
15377

EC: 4.2.1.- | IntEnz: 4.2.1.- | Kegg: 4.2.1.- | BioCyc: 4.2.1.- | BRENDA: 4.2.1.- |

Curation History
Time Change Annotation Old Value New Value
Nov. 3, 2014, 2:33 a.m. update curation agent sbrown setDomainBoundaries.py
July 9, 2015, 3:08 a.m. update curation agent setDomainBoundaries.py sbrown
update curation agent sbrown setDomainBoundaries.py
update name uncharacterized mandelate racemase subgroup sequence, enolase superfamily L-lyxonate dehydratase
EC number assigned by UniProtKB accession ID.