Finding step gltL for L-glutamate catabolism in Mucilaginibacter mallensis MP1X4
5 candidates for gltL: L-glutamate ABC transporter, ATPase component (GltL/GluA/BztD/GlnQ/AatP/PEB1C)
| Score | Gene | Description | Similar to | Id. | Cov. | Bits | Other hit | Other id. | Other bits |
|---|
| med | BLU33_RS00530 | methionine ABC transporter ATP-binding protein MetN | PEB1C, component of Uptake system for glutamate and aspartate (characterized) | 41% | 99% | 183.7 | Methionine import ATP-binding protein MetN; EC 7.4.2.11 | 66% | 448.0 |
| lo | BLU33_RS17915 | phosphate ABC transporter ATP-binding protein | 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) | 38% | 97% | 158.7 | phosphate import ATP-binding protein pstB; EC 3.6.3.27 | 55% | 283.5 |
| lo | BLU33_RS19505 | ATP-binding cassette domain-containing protein | 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) | 38% | 98% | 152.5 | Protein TRIGALACTOSYLDIACYLGLYCEROL 3, chloroplastic; ABC transporter I family member 13; ABC transporter ABCI.13; AtABCI13; Non-intrinsic ABC protein 11; AtNAP11 | 36% | 166.4 |
| lo | BLU33_RS19840 | ABC transporter ATP-binding protein | PEB1C, component of Uptake system for glutamate and aspartate (characterized) | 36% | 98% | 152.1 | Glycine betaine/carnitine/choline transport ATP-binding protein OpuCA | 54% | 268.9 |
| lo | BLU33_RS22445 | ATP-binding cassette domain-containing protein | PEB1C, component of Uptake system for glutamate and aspartate (characterized) | 36% | 93% | 147.1 | Probable bifunctional ABC transport system, component of The cholesterol uptake porter (Mohn et al., 2008). Takes up cholesterol, 5-α-cholestanol, 5-α-cholestanone, β-sitosterol, etc. (It is not established that all of these proteins comprise the system or that other gene products are not involved.) | 39% | 188.0 |
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.
Definition of step gltL
- Curated sequence A3ZI83: PEB1C, component of Uptake system for glutamate and aspartate
- Curated sequence P0AAG3: Glutamate/aspartate transport ATP-binding protein GltL aka B0652, component of Glutamate/aspartate porter. glutamate/aspartate ABC transporter ATP binding subunit (EC 7.4.2.1). glutamate/aspartate ABC transporter ATP binding subunit (EC 7.4.2.1)
- Curated sequence P48243: GluA aka CGL1950, component of Glutamate porter
- Curated sequence Q52666: BztD, component of Glutamate/glutamine/aspartate/asparagine porter
- Curated sequence Q88NY5: PP1068, component of Acidic amino acid uptake porter, AatJMQP
- Curated sequence Q9CES4: 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
- Curated sequence Pf1N1B4_774: ABC transporter for L-asparagine and L-glutamate, ATPase component
- Curated sequence AO353_16275: ABC transporter for L-aspartate, L-asparagine, L-glutamate, and L-glutamine, ATPase component
- Curated sequence Q9I405: Amino acid ABC transporter ATP binding protein, component of Amino acid transporter, AatJMQP. Probably transports L-glutamic acid, D-glutamine acid, L-glutamine and N-acetyl L-glutamic acid (Johnson et al. 2008). Very similar to 3.A.1.3.19 of P. putida
- Ignore hits to PfGW456L13_4773 when looking for 'other' hits (ABC transporter for L-Asparagine and possibly other L-amino acids, putative ATPase component)
- Ignore hits to SMc02121 when looking for 'other' hits (ABC transporter for L-Glutamine, L-Histidine, and other L-amino acids, ATPase component)
- Ignore hits to Q52815 when looking for 'other' hits (AapP, component of General L-amino acid porter; transports basic and acidic amino acids preferentially, but also transports aliphatic amino acids (catalyzes both uptake and efflux))
- Comment: SMc02121 is quite similar and is the ATPase component of a putative amino acid transporter, so it is ignored. Similarly for Q52815
Or cluster all characterized gltL proteins
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:
- ublast finds a hit to a characterized protein at above 40% identity and 80% coverage, and bits >= other bits+10.
- (Hits to curated proteins without experimental data as to their function are never considered high confidence.)
- HMMer finds a hit with 80% coverage of the model, and either other identity < 40 or other coverage < 0.75.
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:
- ublast finds a hit at above 40% identity and 70% coverage (ignoring otherBits).
- ublast finds a hit at above 30% identity and 80% coverage, and bits >= other bits.
- HMMer finds a hit (regardless of coverage or other bits).
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:
- our ignorance of proteins' functions,
- omissions in the gene models,
- frame-shift errors in the genome sequence, or
- the organism lacks the pathway.
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