myo-inosose-2 dehydratase catalyzes the dehydration of inosose (2-keto-myo-inositol, 2KMI or 2,4,6/3,5-pentahydroxycyclohexanone) to 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione (D-2,3-diketo-4-deoxy-epi-inositol)
myo-inosose-2 dehydratase; Members of this family include the enzyme myo-inosose-2 dehydratase, ...
2-291
5.09e-179
myo-inosose-2 dehydratase; Members of this family include the enzyme myo-inosose-2 dehydratase, product of the gene iolE, as found in inositol utilization cassettes in many species. [Energy metabolism, Sugars]
:
Pssm-ID: 275172 Cd Length: 290 Bit Score: 494.87 E-value: 5.09e-179
myo-inosose-2 dehydratase; Members of this family include the enzyme myo-inosose-2 dehydratase, ...
2-291
5.09e-179
myo-inosose-2 dehydratase; Members of this family include the enzyme myo-inosose-2 dehydratase, product of the gene iolE, as found in inositol utilization cassettes in many species. [Energy metabolism, Sugars]
Pssm-ID: 275172 Cd Length: 290 Bit Score: 494.87 E-value: 5.09e-179
Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose ...
30-290
1.07e-23
Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose isomerase and in endonuclease IV (EC:3.1.21.2). This domain is also found in the N termini of bacterial myo-inositol catabolism proteins. These are involved in the myo-inositol catabolism pathway, and is required for growth on myo-inositol in Rhizobium leguminosarum bv. viciae.
Pssm-ID: 426164 [Multi-domain] Cd Length: 248 Bit Score: 96.67 E-value: 1.07e-23
C-terminal fragment of effector protein VpdB; This model represents the C-terminal fragment of ...
166-281
3.24e-08
C-terminal fragment of effector protein VpdB; This model represents the C-terminal fragment of the effector protein VpdB that binds the Legionella pneumophila Dot/Icm type IVB coupling protein (T4CP) complex which includes IcmS, IcmW, and LvgA. These L. pneumophila proteins are known to selectively assist the export of a subclass of effectors. The effector protein VpdB, like other L. pneumophila effectors VpdA, VpdC and VpdD, is a homolog of phospholipase A (PLA) patatin-like enzymes. However, VpdB does not appear to be involved in phospholipid metabolism. The structure reveals interactions between LvgA and a linear motif in the C-terminus of VpdB. This binding interface of LvgA also interacts with the C-terminal region of three additional L. pneumophila effectors, SidH, SetA, and PieA.
Pssm-ID: 408997 Cd Length: 126 Bit Score: 51.13 E-value: 3.24e-08
myo-inosose-2 dehydratase; Members of this family include the enzyme myo-inosose-2 dehydratase, ...
2-291
5.09e-179
myo-inosose-2 dehydratase; Members of this family include the enzyme myo-inosose-2 dehydratase, product of the gene iolE, as found in inositol utilization cassettes in many species. [Energy metabolism, Sugars]
Pssm-ID: 275172 Cd Length: 290 Bit Score: 494.87 E-value: 5.09e-179
Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose ...
30-290
1.07e-23
Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose isomerase and in endonuclease IV (EC:3.1.21.2). This domain is also found in the N termini of bacterial myo-inositol catabolism proteins. These are involved in the myo-inositol catabolism pathway, and is required for growth on myo-inositol in Rhizobium leguminosarum bv. viciae.
Pssm-ID: 426164 [Multi-domain] Cd Length: 248 Bit Score: 96.67 E-value: 1.07e-23
C-terminal fragment of effector protein VpdB; This model represents the C-terminal fragment of ...
166-281
3.24e-08
C-terminal fragment of effector protein VpdB; This model represents the C-terminal fragment of the effector protein VpdB that binds the Legionella pneumophila Dot/Icm type IVB coupling protein (T4CP) complex which includes IcmS, IcmW, and LvgA. These L. pneumophila proteins are known to selectively assist the export of a subclass of effectors. The effector protein VpdB, like other L. pneumophila effectors VpdA, VpdC and VpdD, is a homolog of phospholipase A (PLA) patatin-like enzymes. However, VpdB does not appear to be involved in phospholipid metabolism. The structure reveals interactions between LvgA and a linear motif in the C-terminus of VpdB. This binding interface of LvgA also interacts with the C-terminal region of three additional L. pneumophila effectors, SidH, SetA, and PieA.
Pssm-ID: 408997 Cd Length: 126 Bit Score: 51.13 E-value: 3.24e-08
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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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.
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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.
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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.
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