GapMind for catabolism of small carbon sources


Finding step fruII-ABC for sucrose catabolism in Escherichia coli BW25113

4 candidates for fruII-ABC: fructose-specific PTS system (fructose 1-phosphate forming), EII-ABC components

Score Gene Description Similar to Id. Cov. Bits Other hit Other id. Other bits
med b2167 fused fructose-specific PTS enzymes: IIBcomponent/IIC components (NCBI) The fructose porter, FruA (fructose-1-P forming IIABC) (Delobbe et al. 1975) FruA is 39% identical to 4.A.2.1.1). fructose can be metabolized to Fru-1-P via this system as well as Fru-6-P by another PTS system (characterized) 45% 74% 411.8 PTS system fructose-specific EIIB'BC component; EIIB'BC-Fru; EC 100% 1087.4
lo b0731 fused 2-O-a-mannosyl-D-glycerate specific PTS enzymes: IIA component/IIB component/IIC component (NCBI) The fructose inducible fructose/xylitol porter, FruI (characterized) 36% 99% 351.3 PTS system 2-O-alpha-mannosyl-D-glycerate-specific EIIABC component; 2-O-alpha-mannosyl-D-glycerate-specific phosphotransferase enzyme MngA; Protein-Npi-phosphohistidine--2-O-alpha-mannosyl-D-glycerate phosphotransferase; EC 100% 1288.9
lo b3949 predicted enzyme IIC component of PTS (NCBI) The fructose-specific PTS Enzyme IIABC FruA (characterized) 42% 52% 263.5 Fructose-like permease IIC component 2; PTS system fructose-like EIIC component 2 100% 702.6
lo b3899 PTS system, fructose-like enzyme IIBC component (VIMSS) The fructose porter, FruA (fructose-1-P forming IIABC) (Delobbe et al. 1975) FruA is 39% identical to 4.A.2.1.1). fructose can be metabolized to Fru-1-P via this system as well as Fru-6-P by another PTS system (characterized) 31% 72% 245.7 Fructose-like PTS system EIIBC component, component of Fructose-like PTS Enzyme II complex, FrvA (IIA of 148 aas) - FrvB (IIBC of 483 aas and 9 predicted TMSs) 100% 937.9

Confidence: high confidence medium confidence low confidence
transporter – transporters and PTS systems are shaded because predicting their specificity is particularly challenging.

GapMind searches the predicted proteins for candidates by using ublast (a fast alternative to protein BLAST) to find similarities to characterized proteins or by using HMMer to find similarities to enzyme models (usually from TIGRFams). For alignments to characterized proteins (from ublast), scores of 44 bits correspond to an expectation value (E) of about 0.001.

Also see fitness data for the candidates

Definition of step fruII-ABC

Or cluster all characterized fruII-ABC proteins

This GapMind analysis is from Sep 17 2021. The underlying query database was built on Sep 17 2021.



Related tools

About GapMind

Each pathway is defined by a set of rules based on individual steps or genes. Candidates for each step are identified by using ublast (a fast alternative to protein BLAST) against a database of manually-curated proteins (most of which are experimentally characterized) or by using HMMer with enzyme models (usually from TIGRFam). Ublast hits may be split across two different proteins.

A candidate for a step is "high confidence" if either:

where "other" refers to the best ublast hit to a sequence that is not annotated as performing this step (and is not "ignored").

Otherwise, a candidate is "medium confidence" if either:

Other blast hits with at least 50% coverage are "low confidence."

Steps with no high- or medium-confidence candidates may be considered "gaps." For the typical bacterium that can make all 20 amino acids, there are 1-2 gaps in amino acid biosynthesis pathways. For diverse bacteria and archaea that can utilize a carbon source, there is a complete high-confidence catabolic pathway (including a transporter) just 38% of the time, and there is a complete medium-confidence pathway 63% of the time. Gaps may be due to:

GapMind relies on the predicted proteins in the genome and does not search the six-frame translation. In most cases, you can search the six-frame translation by clicking on links to Curated BLAST for each step definition (in the per-step page).

For more information, see:

If you notice any errors or omissions in the step descriptions, or any questionable results, please let us know

by Morgan Price, Arkin group, Lawrence Berkeley National Laboratory