Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup mandelate racemase

     ⌊ Family D-arabinonate dehydratase

  ⌊ FunctionalDomain D-arabinonate dehydratase (ID 295)

Superfamily Assignment Evidence Code(s) ISS
Family Assignment Evidence Code CFM PubMed:16849334
This entry was last updated onNov. 22, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Sulfolobus solfataricus Taxon ID: 2287 497675762 WP_009989946.1 (RefSeq) URP
Sulfolobus solfataricus Taxon ID: 2287 800906464 AKA78645.1 (Genbank) URP
Sulfolobus solfataricus Taxon ID: 2287 800903770 AKA75952.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
Arabinonate dehydratase Q97U96 ARAD_SULSO (Swiss-Prot)
n/a A0A0E3KBR6 A0A0E3KBR6_SULSF (TrEMBL)
n/a D0KQU1 D0KQU1_SULS9 (TrEMBL)

Sequence

Length of Enzyme (full-length): 373 | Length of Functional Domain: 373

1       10        20        30        40        50        60

MIKDIRTYKLCYEGINDERDALAIKGLAEHPMEIVATEIETSDGYVGYGESLAYGCSDAV
QVTIEKILKPLLLKEDEELIEYLWDKMYKATLRFGRRGIAIAGISGVDTALWDIMGKKAK
KPIYKLLGGSKRKVRAYITGGYYSEKKDLEKLRDEEAYYVKMGFKGIKVKIGAKSMEEDI
ERLKAIREVVGEDVKIAVDANNVYTFEEALEMGRRLEKLGIWFFEEPIQTDYLDLSARLA
EELEVPIAGYETAYTRWEFYEIMRKRAVDIVQTDVMWTGGISEMMKIGNMAKVMGYPLIP
HYSAGGISLIGNLHVAAALNSPWIEMHLRKNDLRDKIFKESIEIDNGHLVVPDRPGLGYT
IRDGVFEEYKCKS
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
199 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
225 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
251 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
199 Asp (D) side chain metal binding ligand metal ligand -- binding ICS
225 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
251 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
274 Asp (D) side chain controls pKa of catalytic His perturbates pKa -- spectator IDA
301 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
170 Lys (K) side chain None -- ISS
199 Asp (D) side chain metal ligand metal ligand -- binding ISS PubMed:16849334
225 Glu (E) side chain metal ligand metal ligand -- binding ISS PubMed:16849334
251 Glu (E) side chain metal ligand metal ligand -- binding ISS PubMed:16849334
274 Asp (D) side chain controls pKa of catalytic His perturbates pKa -- spectator ISS
301 His (H) side chain None -- ISS

Catalyzed Reaction

arabinonate dehydratase

+
D-arabinonate
16157		 2-dehydro-3-deoxy-D-arabinonate
16699		 water
15377

EC: 4.2.1.5 | IntEnz: 4.2.1.5 | Kegg: 4.2.1.5 | BioCyc: 4.2.1.5 | BRENDA: 4.2.1.5

Curation History
Time Change Annotation Old Value New Value
Nov. 3, 2014, 2:33 a.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.