Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup mandelate racemase

     ⌊ Family D-arabinonate dehydratase

Total 100% <100%
Functional domains 10 0 10
UniProtKB 19 0 19
GI 48 0 48
Structures 0
Reactions 1
Functional domains of this family were last updated on Nov. 22, 2017
New functional domains were last added to this family on Aug. 1, 2014

Enzymes in the D-arabinonate dehydratase family catalyze the dehydration of D-arabinonate to 2-keto-3-deoxy-D-arabinonate, as part of the pentose oxidation pathway.

Brouns SJ, Walther J, Snijders AP, van de Werken HJ, Willemen HL, Worm P, de Vos MG, Andersson A, Lundgren M, Mazon HF, van den Heuvel RH, Nilsson P, Salmon L, de Vos WM, Wright PC, Bernander R, van der Oost J

Identification of the missing links in prokaryotic pentose oxidation pathways: evidence for enzyme recruitment

▸ Abstract

J Biol Chem 2006;281(37):27378-27388 | PubMed ID: 16849334

No notes.

Static File Downloads

File Name Description Parameters Stats
network.fam156.bs60.mek250K.xgmml One node per sequence network min bit score = 60
max edge count = 250K
size = 31K
num_edges = 45
num_nodes = 10
sfld_alignment_fam156.msa Annotated Sequence Alignment, Stockholm format 3 sequences
size: 2.4K

Total number of functional domains in this group.
Number of Functional Domains that have been manually or automatically been assigned to a family.
Number of Functional Domains that have not been assigned to a family.
Number of structures available from the PDB for members of this group.
Number of Functional Domains with 100% of Conserved Residues
Number of Functional Domains with less than 100% Conserved Residues

Catalyzed Reaction(s)

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