Domains within Sanguibacter keddieii DSM 10542 protein D1BB86_SANKS (D1BB86)

Ribulose-5-phosphate 4-epimerase-like epimerase or aldolase

Alternative representations: 1 /

Protein length234 aa
Source databaseUniProt
Identifiers D1BB86_SANKS, D1BB86

Domain architecture analysis

Display all proteins with similar:

Domain organisationProteins having all the domains as the query in the same order. Additional domains are allowed.
Domain compositionProteins with the same domain composition have at least one copy of each of the domains of the query.

Predicted functional partners

D1BB86_SANKS is shown as ACZ20652.1 in the network

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The network on the left comes from STRING, a database of known and predicted protein interactions. Displayed here is the evidence view, where different line colors represent the types of evidence for the association.

Open the STRING annotation page for ACZ20652.1

Protein D1BB86_SANKS is possibly involved in these pathways, based on its similarity to the listed KEGG orthologous groups:

KEGG pathways

PathwayDescription
map00040Pentose and glucuronate interconversions iPath3
Some of these pathways are included in the interactive Pathways Explorer overview maps. Select an overview map and click the button below to highlight them in iPath.

KEGG orthologous groups

KONameDescription
K03077araD, ulaF, sgaE, sgbEL-ribulose-5-phosphate 4-epimerase [EC:5.1.3.4] iPath3
K01628fucAL-fuculose-phosphate aldolase [EC:4.1.2.17] iPath3
Some of these orthologous groups are included in the interactive Pathways Explorer overview maps. Select an overview map and click the button below to highlight them in iPath.

Orthologous groups

Orthology information is taken from eggNOG, a database of orthologous groups of genes. Orthologous groups containing this protein are listed below. This protein is named 446469.Sked_06950 in eggNOG.

OGTaxonomic classDescription
LCOG0235All organisms (root)L-fuculose-phosphate aldolase [EC:4.1.2.17],L-ribulose-5-phosphate 4-epimerase [EC:5.1.3.4],methylthioribulose-1-phosphate dehydratase [EC:4.2.1.109]
COG0235Bacteria (superkingdom)L-fuculose-phosphate aldolase [EC:4.1.2.17],L-ribulose-5-phosphate 4-epimerase [EC:5.1.3.4],methylthioribulose-1-phosphate dehydratase [EC:4.2.1.109]
68UQGActinobacteria (phylum)L-ribulose-5-phosphate 4-epimerase [EC:5.1.3.4],L-fuculose-phosphate aldolase [EC:4.1.2.17],3-dehydro-4-phosphotetronate decarboxylase [EC:4.1.1.104]
FAR0QActinomycetia (class)L-ribulose-5-phosphate 4-epimerase [EC:5.1.3.4],L-fuculose-phosphate aldolase [EC:4.1.2.17],3-dehydro-4-phosphotetronate decarboxylase [EC:4.1.1.104]
EVTHSMicrococcales (order)L-ribulose-5-phosphate 4-epimerase [EC:5.1.3.4],3-dehydro-4-phosphotetronate decarboxylase [EC:4.1.1.104],L-fuculose-phosphate aldolase [EC:4.1.2.17]
6HG97Sanguibacter (genus)L-ribulose-5-phosphate 4-epimerase [EC:5.1.3.4]

The SMART diagram above represents a summary of the results shown below. Domains with scores less significant than established cutoffs are not shown in the diagram. Features are also not shown when two or more occupy the same piece of sequence; the priority for display is given by SMART > PFAM > PROSPERO repeats > Signal peptide > Transmembrane > Coiled coil > Low complexity. In either case, features not shown in the above diagram are listed in the right side table below, and the reason for their omission is shown in the 'Reason' column.

Confidently predicted domains, repeats, motifs and features:

Outlier homologues and homologues of known structure:

Features NOT shown in the diagram: