6-phosphogluconolactonase catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate, which is the the second step of the oxidative phase of the pentose phosphate pathway
6-phosphogluconolactonase/Glucosamine-6-phosphate isomerase/deaminase [Carbohydrate transport ...
2-187
3.23e-15
6-phosphogluconolactonase/Glucosamine-6-phosphate isomerase/deaminase [Carbohydrate transport and metabolism]; 6-phosphogluconolactonase/Glucosamine-6-phosphate isomerase/deaminase is part of the Pathway/BioSystem: Pentose phosphate pathway
:
Pssm-ID: 440132 [Multi-domain] Cd Length: 248 Bit Score: 71.35 E-value: 3.23e-15
6-phosphogluconolactonase/Glucosamine-6-phosphate isomerase/deaminase [Carbohydrate transport ...
2-187
3.23e-15
6-phosphogluconolactonase/Glucosamine-6-phosphate isomerase/deaminase [Carbohydrate transport and metabolism]; 6-phosphogluconolactonase/Glucosamine-6-phosphate isomerase/deaminase is part of the Pathway/BioSystem: Pentose phosphate pathway
Pssm-ID: 440132 [Multi-domain] Cd Length: 248 Bit Score: 71.35 E-value: 3.23e-15
GlcN6P_deaminase: Glucosamine-6-phosphate (GlcN6P) deaminase subfamily; GlcN6P deaminase catalyzes the reversible conversion of GlcN6P to D-fructose-6-phosphate (Fru6P) and ammonium. The reaction is an aldo-keto isomerization coupled with an amination or deamination. It is the last step of the metabolic pathway of N-acetyl-D-glucosamine-6-phosphate (GlcNAc6P). GlcN6P deaminase is a hexameric enzyme that is allosterically activated by GlcNAc6P.
Pssm-ID: 238693 [Multi-domain] Cd Length: 232 Bit Score: 54.41 E-value: 4.05e-09
6-phosphogluconolactonase/Glucosamine-6-phosphate isomerase/deaminase [Carbohydrate transport ...
2-187
3.23e-15
6-phosphogluconolactonase/Glucosamine-6-phosphate isomerase/deaminase [Carbohydrate transport and metabolism]; 6-phosphogluconolactonase/Glucosamine-6-phosphate isomerase/deaminase is part of the Pathway/BioSystem: Pentose phosphate pathway
Pssm-ID: 440132 [Multi-domain] Cd Length: 248 Bit Score: 71.35 E-value: 3.23e-15
GlcN6P_deaminase: Glucosamine-6-phosphate (GlcN6P) deaminase subfamily; GlcN6P deaminase catalyzes the reversible conversion of GlcN6P to D-fructose-6-phosphate (Fru6P) and ammonium. The reaction is an aldo-keto isomerization coupled with an amination or deamination. It is the last step of the metabolic pathway of N-acetyl-D-glucosamine-6-phosphate (GlcNAc6P). GlcN6P deaminase is a hexameric enzyme that is allosterically activated by GlcNAc6P.
Pssm-ID: 238693 [Multi-domain] Cd Length: 232 Bit Score: 54.41 E-value: 4.05e-09
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
Click on the triangle to view details about the feature, including a multiple sequence alignment
of your query sequence and the protein sequences used to curate the domain model,
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The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
The Show Concise/Full Display button at the top of the page can be used to select the desired level of detail: only top scoring hits
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Domains are color coded according to superfamilies
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
or click on the triangles, if present, that represent functional sites (conserved features)
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
(labeled illustration) Four types of hits can be shown, as available,
for each region on the query sequence:
specific hits meet or exceed a domain-specific e-value threshold
(illustrated example)
and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
non-specific hits
meet or exceed the RPS-BLAST threshold for statistical significance (default E-value cutoff of 0.01, or an E-value selected by user via the
advanced search options)
the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains
Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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