RPI_A: Ribose 5-phosphate isomerase type A (RPI_A) subfamily; RPI catalyzes the reversible ...
77-294
6.80e-114
RPI_A: Ribose 5-phosphate isomerase type A (RPI_A) subfamily; RPI catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate, the first step of the non-oxidative branch of the pentose phosphate pathway. This reaction leads to the conversion of phosphosugars into glycolysis intermediates, which are precursors for the synthesis of amino acids, vitamins, nucleotides, and cell wall components. In plants, RPI is part of the Calvin cycle as ribulose 5-phosphate is the carbon dioxide receptor in the first dark reaction of photosynthesis. There are two unrelated types of RPIs (A and B), which catalyze the same reaction, at least one type of RPI is present in an organism. RPI_A is more widely distributed than RPI_B in bacteria, eukaryotes, and archaea.
:
Pssm-ID: 238692 Cd Length: 213 Bit Score: 327.51 E-value: 6.80e-114
RPI_A: Ribose 5-phosphate isomerase type A (RPI_A) subfamily; RPI catalyzes the reversible ...
77-294
6.80e-114
RPI_A: Ribose 5-phosphate isomerase type A (RPI_A) subfamily; RPI catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate, the first step of the non-oxidative branch of the pentose phosphate pathway. This reaction leads to the conversion of phosphosugars into glycolysis intermediates, which are precursors for the synthesis of amino acids, vitamins, nucleotides, and cell wall components. In plants, RPI is part of the Calvin cycle as ribulose 5-phosphate is the carbon dioxide receptor in the first dark reaction of photosynthesis. There are two unrelated types of RPIs (A and B), which catalyze the same reaction, at least one type of RPI is present in an organism. RPI_A is more widely distributed than RPI_B in bacteria, eukaryotes, and archaea.
Pssm-ID: 238692 Cd Length: 213 Bit Score: 327.51 E-value: 6.80e-114
ribose 5-phosphate isomerase; This model describes ribose 5-phosphate isomerase, an enzyme of ...
78-299
4.34e-113
ribose 5-phosphate isomerase; This model describes ribose 5-phosphate isomerase, an enzyme of the non-oxidative branch of the pentose phosphate pathway. [Energy metabolism, Pentose phosphate pathway]
Pssm-ID: 272859 Cd Length: 218 Bit Score: 325.72 E-value: 4.34e-113
Ribose 5-phosphate isomerase [Carbohydrate transport and metabolism]; Ribose 5-phosphate ...
75-297
6.09e-97
Ribose 5-phosphate isomerase [Carbohydrate transport and metabolism]; Ribose 5-phosphate isomerase is part of the Pathway/BioSystem: Pentose phosphate pathway
Pssm-ID: 439890 Cd Length: 225 Bit Score: 285.00 E-value: 6.09e-97
Ribose 5-phosphate isomerase A (phosphoriboisomerase A); This family consists of several ...
123-297
7.81e-93
Ribose 5-phosphate isomerase A (phosphoriboisomerase A); This family consists of several ribose 5-phosphate isomerase A or phosphoriboisomerase A (EC:5.3.1.6) from bacteria, eukaryotes and archaea.
Pssm-ID: 461804 Cd Length: 172 Bit Score: 272.71 E-value: 7.81e-93
RPI_A: Ribose 5-phosphate isomerase type A (RPI_A) subfamily; RPI catalyzes the reversible ...
77-294
6.80e-114
RPI_A: Ribose 5-phosphate isomerase type A (RPI_A) subfamily; RPI catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate, the first step of the non-oxidative branch of the pentose phosphate pathway. This reaction leads to the conversion of phosphosugars into glycolysis intermediates, which are precursors for the synthesis of amino acids, vitamins, nucleotides, and cell wall components. In plants, RPI is part of the Calvin cycle as ribulose 5-phosphate is the carbon dioxide receptor in the first dark reaction of photosynthesis. There are two unrelated types of RPIs (A and B), which catalyze the same reaction, at least one type of RPI is present in an organism. RPI_A is more widely distributed than RPI_B in bacteria, eukaryotes, and archaea.
Pssm-ID: 238692 Cd Length: 213 Bit Score: 327.51 E-value: 6.80e-114
ribose 5-phosphate isomerase; This model describes ribose 5-phosphate isomerase, an enzyme of ...
78-299
4.34e-113
ribose 5-phosphate isomerase; This model describes ribose 5-phosphate isomerase, an enzyme of the non-oxidative branch of the pentose phosphate pathway. [Energy metabolism, Pentose phosphate pathway]
Pssm-ID: 272859 Cd Length: 218 Bit Score: 325.72 E-value: 4.34e-113
Ribose 5-phosphate isomerase [Carbohydrate transport and metabolism]; Ribose 5-phosphate ...
75-297
6.09e-97
Ribose 5-phosphate isomerase [Carbohydrate transport and metabolism]; Ribose 5-phosphate isomerase is part of the Pathway/BioSystem: Pentose phosphate pathway
Pssm-ID: 439890 Cd Length: 225 Bit Score: 285.00 E-value: 6.09e-97
Ribose 5-phosphate isomerase A (phosphoriboisomerase A); This family consists of several ...
123-297
7.81e-93
Ribose 5-phosphate isomerase A (phosphoriboisomerase A); This family consists of several ribose 5-phosphate isomerase A or phosphoriboisomerase A (EC:5.3.1.6) from bacteria, eukaryotes and archaea.
Pssm-ID: 461804 Cd Length: 172 Bit Score: 272.71 E-value: 7.81e-93
Putative sugar-binding domain; This probable domain is found in bacterial transcriptional ...
64-126
9.65e-03
Putative sugar-binding domain; This probable domain is found in bacterial transcriptional regulators such as DeoR and SorC. These proteins have an amino-terminal helix-turn-helix pfam00325 that binds to DNA. This domain is probably the ligand regulator binding region. SorC is regulated by sorbose and other members of this family are likely to be regulated by other sugar substrates.
Pssm-ID: 427778 Cd Length: 256 Bit Score: 36.83 E-value: 9.65e-03
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.
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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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Others (non-specific hits) and
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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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