GapMind for catabolism of small carbon sources

 

Protein WP_011654689.1 in Rhizobium leguminosarum 3841

Annotation: NCBI__GCF_000009265.1:WP_011654689.1

Length: 267 amino acids

Source: GCF_000009265.1 in NCBI

Candidate for 13 steps in catabolism of small carbon sources

Pathway Step Score Similar to Id. Cov. Bits Other hit Other id. Other bits
D-glucosamine (chitosamine) catabolism AO353_21725 med ABC transporter for D-Glucosamine, putative ATPase component (characterized) 56% 94% 276.9 Arginine transport ATP-binding protein ArtM 54% 273.5
L-arginine catabolism artP med Arginine transport ATP-binding protein ArtM (characterized) 54% 100% 273.5 ABC transporter for D-Glucosamine, putative ATPase component 56% 276.9
L-asparagine catabolism bgtA med ATPase (characterized, see rationale) 55% 100% 272.3 ABC transporter for D-Glucosamine, putative ATPase component 56% 276.9
L-aspartate catabolism bgtA med ATPase (characterized, see rationale) 55% 100% 272.3 ABC transporter for D-Glucosamine, putative ATPase component 56% 276.9
L-citrulline catabolism AO353_03040 med ABC transporter for L-Arginine and L-Citrulline, ATPase component (characterized) 56% 98% 266.5 ABC transporter for D-Glucosamine, putative ATPase component 56% 276.9
L-asparagine catabolism glnQ med Glutamine ABC transporter ATP-binding protein, component of Glutamine transporter, GlnQP. Takes up glutamine, asparagine and glutamate which compete for each other for binding both substrate and the transmembrane protein constituent of the system (Fulyani et al. 2015). Tandem substrate binding domains (SBDs) differ in substrate specificity and affinity, allowing cells to efficiently accumulate different amino acids via a single ABC transporter. Analysis revealed the roles of individual residues in determining the substrate affinity (characterized) 53% 98% 263.5 ABC transporter for D-Glucosamine, putative ATPase component 56% 276.9
L-glutamate catabolism gltL med Glutamine ABC transporter ATP-binding protein, component of Glutamine transporter, GlnQP. Takes up glutamine, asparagine and glutamate which compete for each other for binding both substrate and the transmembrane protein constituent of the system (Fulyani et al. 2015). Tandem substrate binding domains (SBDs) differ in substrate specificity and affinity, allowing cells to efficiently accumulate different amino acids via a single ABC transporter. Analysis revealed the roles of individual residues in determining the substrate affinity (characterized) 53% 98% 263.5 ABC transporter for D-Glucosamine, putative ATPase component 56% 276.9
L-histidine catabolism bgtA med BgtA aka SLR1735, component of Arginine/lysine/histidine/glutamine porter (characterized) 55% 94% 260 ABC transporter for D-Glucosamine, putative ATPase component 56% 276.9
L-histidine catabolism hisP med Probable ATP-binding component of ABC transporter, component of Amino acid transporter, PA5152-PA5155. Probably transports numerous amino acids including lysine, arginine, histidine, D-alanine and D-valine (Johnson et al. 2008). Regulated by ArgR (characterized) 53% 98% 256.1 ABC transporter for D-Glucosamine, putative ATPase component 56% 276.9
L-histidine catabolism BPHYT_RS24015 med ABC transporter related (characterized, see rationale) 54% 94% 250.4 ABC transporter for D-Glucosamine, putative ATPase component 56% 276.9
L-asparagine catabolism peb1C med PEB1C, component of Uptake system for glutamate and aspartate (characterized) 49% 99% 233.8 ABC transporter for D-Glucosamine, putative ATPase component 56% 276.9
L-aspartate catabolism peb1C med PEB1C, component of Uptake system for glutamate and aspartate (characterized) 49% 99% 233.8 ABC transporter for D-Glucosamine, putative ATPase component 56% 276.9
L-histidine catabolism PA5503 med Methionine import ATP-binding protein MetN 2, component of L-Histidine uptake porter, MetIQN (characterized) 42% 72% 182.2 ABC transporter for D-Glucosamine, putative ATPase component 56% 276.9

Sequence Analysis Tools

View WP_011654689.1 at NCBI

Find papers: PaperBLAST

Find functional residues: SitesBLAST

Search for conserved domains

Find the best match in UniProt

Compare to protein structures

Predict transmenbrane helices: Phobius

Predict protein localization: PSORTb

Find homologs in fast.genomics

Fitness BLAST: loading...

Sequence

MTAPGTHHERFGIASTTMVHAKGIRKSYGHLEVLKGVDLTVPSGSVACIIGPSGSGKSTF
LRCINHLEEINGGLMLVDGDFVGYRLEGNKLYELPPSAICQRRAEIGMVFQQFNLFPHMT
VIENLMEAPLRVKREPVAQATAKAIELLKRVGLAEKRDAYPRQLSGGQQQRVAIARALAM
NPKVLLFDEPTSALDPELVGEVLEVMKSLAREGITMVVVTHEIGFAREVADQLIFMDGGL
VVESGNPREMIANPQSPRTREFLARVL

This GapMind analysis is from Sep 24 2021. The underlying query database was built on Sep 17 2021.

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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