LamB/YcsF family protein such as 5-oxoprolinase subunit PxpA, which is part of the enzyme complex that catalyzes the cleavage of 5-oxoproline to form L-glutamate, coupled to the hydrolysis of ATP to ADP and inorganic phosphate
LamB/YcsF family; This family includes LamB. The lam locus of Aspergillus nidulans consists of ...
4-240
9.50e-147
LamB/YcsF family; This family includes LamB. The lam locus of Aspergillus nidulans consists of two divergently transcribed genes, lamA and lamB, involved in the utilization of lactams such as 2-pyrrolidinone. Both genes are under the control of the positive regulatory gene amdR and are subject to carbon and nitrogen metabolite repression. The exact molecular function of the proteins in this family is unknown.
Pssm-ID: 461036 Cd Length: 238 Bit Score: 409.48 E-value: 9.50e-147
LamB/YcsF family of lactam utilization protein; The LamB/YbgL family includes the Aspergillus ...
3-240
1.40e-145
LamB/YcsF family of lactam utilization protein; The LamB/YbgL family includes the Aspergillus nidulans protein LamB, and its homologs from all three kingdoms of life. The lamb gene locates at the lam locus of Aspergillus nidulans, consisting of two divergently transcribed genes, lamA and lamB, needed for the utilization of lactams such as 2-pyrrolidinone. Both genes are under the control of the positive regulatory gene amdR and are subject to carbon and nitrogen metabolite repression. Although the exact molecular function of LamB is unknown, it might be required for conversion of exogenous 2-pyrrolidinone to endogenous GABA
Pssm-ID: 212099 Cd Length: 238 Bit Score: 406.43 E-value: 1.40e-145
LamB/YcsF family; This family includes LamB. The lam locus of Aspergillus nidulans consists of ...
4-240
9.50e-147
LamB/YcsF family; This family includes LamB. The lam locus of Aspergillus nidulans consists of two divergently transcribed genes, lamA and lamB, involved in the utilization of lactams such as 2-pyrrolidinone. Both genes are under the control of the positive regulatory gene amdR and are subject to carbon and nitrogen metabolite repression. The exact molecular function of the proteins in this family is unknown.
Pssm-ID: 461036 Cd Length: 238 Bit Score: 409.48 E-value: 9.50e-147
LamB/YcsF family of lactam utilization protein; The LamB/YbgL family includes the Aspergillus ...
3-240
1.40e-145
LamB/YcsF family of lactam utilization protein; The LamB/YbgL family includes the Aspergillus nidulans protein LamB, and its homologs from all three kingdoms of life. The lamb gene locates at the lam locus of Aspergillus nidulans, consisting of two divergently transcribed genes, lamA and lamB, needed for the utilization of lactams such as 2-pyrrolidinone. Both genes are under the control of the positive regulatory gene amdR and are subject to carbon and nitrogen metabolite repression. Although the exact molecular function of LamB is unknown, it might be required for conversion of exogenous 2-pyrrolidinone to endogenous GABA
Pssm-ID: 212099 Cd Length: 238 Bit Score: 406.43 E-value: 1.40e-145
uncharacterized proteins similar to the Aspergillus nidulans lactam utilization protein LamB; ...
3-240
4.46e-104
uncharacterized proteins similar to the Aspergillus nidulans lactam utilization protein LamB; This mainly bacterial subfamily of the LamB/YbgL family, contains many well conserved uncharacterized proteins. Although their molecular function remains unknown, those proteins show high sequence similarity to the Aspergillus nidulans lactam utilization protein LamB, which might be required for conversion of exogenous 2-pyrrolidinone to endogenous GABA.
Pssm-ID: 212112 Cd Length: 233 Bit Score: 301.40 E-value: 4.46e-104
Escherichia coli putative lactam utilization protein YbgL and similar proteins; This subfamily ...
3-247
1.58e-92
Escherichia coli putative lactam utilization protein YbgL and similar proteins; This subfamily of the LamB/YbgL family is represented by the Escherichia coli putative lactam utilization protein YbgL. Although their molecular function of member of this subfamily is unknown, they show high sequence similarity to the Aspergillus nidulans lactam utilization protein LamB, which might be required for conversion of exogenous 2-pyrrolidinone to endogenous GABA.
Pssm-ID: 212111 Cd Length: 240 Bit Score: 272.33 E-value: 1.58e-92
Aspergillus nidulans lactam utilization protein LamB and similar proteins; This eukaryotic and ...
3-238
1.44e-79
Aspergillus nidulans lactam utilization protein LamB and similar proteins; This eukaryotic and bacterial subfamily of the LamB/YbgL family, includes Aspergillus nidulans protein LamB. The lamb gene locates at the lam locus of Aspergillus nidulans, consisting of two divergently transcribed genes, lamA and lamB, needed for the utilization of lactams such as 2-pyrrolidinone. Both genes are under the control of the positive regulatory gene amdR and are subject to carbon and nitrogen metabolite repression. Although the exact molecular function of lamb encoding protein LamB is unknown, it might be required for conversion of exogenous 2-pyrrolidinone to endogenous GABA.
Pssm-ID: 212130 Cd Length: 238 Bit Score: 239.52 E-value: 1.44e-79
uncharacterized proteins similar to the Aspergillus nidulans lactam utilization protein LamB; ...
3-240
3.31e-76
uncharacterized proteins similar to the Aspergillus nidulans lactam utilization protein LamB; This bacterial subfamily of the LamB/YbgL family, contains many well conserved uncharacterized proteins. Although their molecular function is unknown, those proteins show high sequence similarity to the Aspergillus nidulans lactam utilization protein LamB, which might be required for conversion of exogenous 2-pyrrolidinone to endogenous GABA.
Pssm-ID: 212129 Cd Length: 238 Bit Score: 230.80 E-value: 3.31e-76
Catalytic domain of glycoside hydrolase (GH) families 38 and 57, lactam utilization protein ...
27-155
1.69e-04
Catalytic domain of glycoside hydrolase (GH) families 38 and 57, lactam utilization protein LamB/YcsF family proteins, YdjC-family proteins, and similar proteins; The superfamily possesses strong sequence similarities across a wide range of all three kingdoms of life. It mainly includes four families, glycoside hydrolases family 38 (GH38), heat stable retaining glycoside hydrolases family 57 (GH57), lactam utilization protein LamB/YcsF family, and YdjC-family. The GH38 family corresponds to class II alpha-mannosidases (alphaMII, EC 3.2.1.24), which contain intermediate Golgi alpha-mannosidases II, acidic lysosomal alpha-mannosidases, animal sperm and epididymal alpha -mannosidases, neutral ER/cytosolic alpha-mannosidases, and some putative prokaryotic alpha-mannosidases. AlphaMII possess a-1,3, a-1,6, and a-1,2 hydrolytic activity, and catalyzes the degradation of N-linked oligosaccharides by employing a two-step mechanism involving the formation of a covalent glycosyl enzyme complex. GH57 is a purely prokaryotic family with the majority of thermostable enzymes from extremophiles (many of them are archaeal hyperthermophiles), which exhibit the enzyme specificities of alpha-amylase (EC 3.2.1.1), 4-alpha-glucanotransferase (EC 2.4.1.25), amylopullulanase (EC 3.2.1.1/41), and alpha-galactosidase (EC 3.2.1.22). This family also includes many hypothetical proteins with uncharacterized activity and specificity. GH57 cleaves alpha-glycosidic bond by employing a retaining mechanism, which involves a glycosyl-enzyme intermediate, allowing transglycosylation. Although the exact molecular function of LamB/YcsF family and YdjC-family remains unclear, they show high sequence and structure homology to the members of GH38 and GH57. Their catalytic domains adopt a similar parallel 7-stranded beta/alpha barrel, which is remotely related to catalytic NodB homology domain of the carbohydrate esterase 4 superfamily.
Pssm-ID: 212097 [Multi-domain] Cd Length: 203 Bit Score: 41.47 E-value: 1.69e-04
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),
they are mapped to the query sequence and indicated through sets of triangles
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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)
mapped to the query sequence.
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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