GapMind for catabolism of small carbon sources

 

Protein WP_013449869.1 in Sulfuricurvum kujiense DSM 16994

Annotation: NCBI__GCF_000183725.1:WP_013449869.1

Length: 231 amino acids

Source: GCF_000183725.1 in NCBI

Candidate for 16 steps in catabolism of small carbon sources

Pathway Step Score Similar to Id. Cov. Bits Other hit Other id. Other bits
L-glutamate catabolism gltL lo GluA aka CGL1950, component of Glutamate porter (characterized) 38% 89% 151.8 Putative hemin import ATP-binding protein HrtA; EC 7.6.2.- 43% 181.0
L-arginine catabolism artP lo Arginine transport ATP-binding protein ArtM (characterized) 37% 91% 146.4 Putative hemin import ATP-binding protein HrtA; EC 7.6.2.- 43% 181.0
L-asparagine catabolism bgtA lo ATPase (characterized, see rationale) 36% 85% 143.7 Putative hemin import ATP-binding protein HrtA; EC 7.6.2.- 43% 181.0
L-aspartate catabolism bgtA lo ATPase (characterized, see rationale) 36% 85% 143.7 Putative hemin import ATP-binding protein HrtA; EC 7.6.2.- 43% 181.0
L-asparagine catabolism glnQ lo 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) 35% 88% 139.4 Putative hemin import ATP-binding protein HrtA; EC 7.6.2.- 43% 181.0
L-asparagine catabolism aatP lo ABC transporter for L-asparagine and L-glutamate, ATPase component (characterized) 36% 89% 137.1 Putative hemin import ATP-binding protein HrtA; EC 7.6.2.- 43% 181.0
L-aspartate catabolism aatP lo ABC transporter for L-asparagine and L-glutamate, ATPase component (characterized) 36% 89% 137.1 Putative hemin import ATP-binding protein HrtA; EC 7.6.2.- 43% 181.0
L-lysine catabolism hisP lo Amino-acid ABC transporter, ATP-binding protein (characterized, see rationale) 36% 83% 134.8 Putative hemin import ATP-binding protein HrtA; EC 7.6.2.- 43% 181.0
L-histidine catabolism bgtA lo BgtA aka SLR1735, component of Arginine/lysine/histidine/glutamine porter (characterized) 35% 87% 132.9 Putative hemin import ATP-binding protein HrtA; EC 7.6.2.- 43% 181.0
L-asparagine catabolism peb1C lo PEB1C, component of Uptake system for glutamate and aspartate (characterized) 33% 89% 132.1 Putative hemin import ATP-binding protein HrtA; EC 7.6.2.- 43% 181.0
L-aspartate catabolism peb1C lo PEB1C, component of Uptake system for glutamate and aspartate (characterized) 33% 89% 132.1 Putative hemin import ATP-binding protein HrtA; EC 7.6.2.- 43% 181.0
D-glucosamine (chitosamine) catabolism AO353_21725 lo ABC transporter for D-Glucosamine, putative ATPase component (characterized) 34% 87% 128.6 Putative hemin import ATP-binding protein HrtA; EC 7.6.2.- 43% 181.0
L-fucose catabolism SM_b21106 lo ABC transporter for L-Fucose, ATPase component (characterized) 33% 59% 122.9 Putative hemin import ATP-binding protein HrtA; EC 7.6.2.- 43% 181.0
D-mannose catabolism TM1749 lo TM1749, component of Probable mannose/mannoside porter. Induced by beta-mannan (Conners et al., 2005). Regulated by mannose-responsive regulator manR (characterized) 31% 68% 103.2 Putative hemin import ATP-binding protein HrtA; EC 7.6.2.- 43% 181.0
D-cellobiose catabolism cbtF lo CbtF, component of Cellobiose and cellooligosaccharide porter (characterized) 33% 62% 100.9 Putative hemin import ATP-binding protein HrtA; EC 7.6.2.- 43% 181.0
D-cellobiose catabolism TM0028 lo TM0028, component of β-glucoside porter (Conners et al., 2005). Binds cellobiose, laminaribiose (Nanavati et al. 2006). Regulated by cellobiose-responsive repressor BglR (characterized) 31% 73% 96.3 Putative hemin import ATP-binding protein HrtA; EC 7.6.2.- 43% 181.0

Sequence Analysis Tools

View WP_013449869.1 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

MKHSVIKCEGIEKTYGSGDSAVLAIKKADFEIYSGETVALLGPSGSGKTTLITMIGCITE
PSGGKLTLSGECVYDSGWTIPDTRKIRREKIGFIFQSHNLIPFLNVRENITLVPQMNGVG
VNEANTKAVELLEYLGVGDKLEKMPSELSGGQSQRVAIARSLANNPQIILADEPTAALDS
QRALSVMELLRSLAHEHDVAIIVVTHDERMLPLFDRILRVEDGVVLEMANS

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