cobalt-precorrin 5A hydrolase catalyzes the hydrolysis of the ring A acetate delta-lactone of cobalt-precorrin-5A, resulting in the loss of the C-20 carbon and its attached methyl group in the form of acetaldehyde
Cobalamin biosynthesis protein CbiG [Coenzyme transport and metabolism]; Cobalamin ...
2-317
1.54e-109
Cobalamin biosynthesis protein CbiG [Coenzyme transport and metabolism]; Cobalamin biosynthesis protein CbiG is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
:
Pssm-ID: 441676 [Multi-domain] Cd Length: 334 Bit Score: 322.12 E-value: 1.54e-109
Cobalamin biosynthesis protein CbiG [Coenzyme transport and metabolism]; Cobalamin ...
2-317
1.54e-109
Cobalamin biosynthesis protein CbiG [Coenzyme transport and metabolism]; Cobalamin biosynthesis protein CbiG is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 441676 [Multi-domain] Cd Length: 334 Bit Score: 322.12 E-value: 1.54e-109
Cobalamin synthesis G N-terminal; Members of this family are involved in cobalamin synthesis. ...
23-101
1.39e-43
Cobalamin synthesis G N-terminal; Members of this family are involved in cobalamin synthesis. The gene refered to by Swiss:P72862 has been designated cbiH but in fact represents a fusion between cbiH and cbiG. As other multi-functional proteins involved in cobalamin biosynthesis catalyze adjacent steps in the pathway, including CysG, CobL (CbiET), CobIJ and CobA-HemD, it is therefore possible that CbiG catalyzes a reaction step adjacent to CbiH. In the anaerobic pathway such a step could be the formation of a gamma lactone, which is thought to help to mediate the anaerobic ring contraction process. Within the cobalamin synthesis pathway CbiG catalyzes the both the opening of the lactone ring and the extrusion of the two-carbon fragment of cobalt-precorrin-5A from C-20 and its associated methyl group (deacylation) to give cobalt-precorrin-5B. The N-terminal of the enzyme is conserved in this family, and the C-terminal and the mid-sections are conserved independently in other families, CbiG_C and CbiG_mid, although the distinct function of each region is unclear.
Pssm-ID: 463343 [Multi-domain] Cd Length: 79 Bit Score: 144.47 E-value: 1.39e-43
Cobalamin biosynthesis protein CbiG [Coenzyme transport and metabolism]; Cobalamin ...
2-317
1.54e-109
Cobalamin biosynthesis protein CbiG [Coenzyme transport and metabolism]; Cobalamin biosynthesis protein CbiG is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 441676 [Multi-domain] Cd Length: 334 Bit Score: 322.12 E-value: 1.54e-109
Cobalamin synthesis G N-terminal; Members of this family are involved in cobalamin synthesis. ...
23-101
1.39e-43
Cobalamin synthesis G N-terminal; Members of this family are involved in cobalamin synthesis. The gene refered to by Swiss:P72862 has been designated cbiH but in fact represents a fusion between cbiH and cbiG. As other multi-functional proteins involved in cobalamin biosynthesis catalyze adjacent steps in the pathway, including CysG, CobL (CbiET), CobIJ and CobA-HemD, it is therefore possible that CbiG catalyzes a reaction step adjacent to CbiH. In the anaerobic pathway such a step could be the formation of a gamma lactone, which is thought to help to mediate the anaerobic ring contraction process. Within the cobalamin synthesis pathway CbiG catalyzes the both the opening of the lactone ring and the extrusion of the two-carbon fragment of cobalt-precorrin-5A from C-20 and its associated methyl group (deacylation) to give cobalt-precorrin-5B. The N-terminal of the enzyme is conserved in this family, and the C-terminal and the mid-sections are conserved independently in other families, CbiG_C and CbiG_mid, although the distinct function of each region is unclear.
Pssm-ID: 463343 [Multi-domain] Cd Length: 79 Bit Score: 144.47 E-value: 1.39e-43
Cobalamin synthesis G C-terminus; Members of this family are involved in cobalamin synthesis. ...
201-317
3.09e-27
Cobalamin synthesis G C-terminus; Members of this family are involved in cobalamin synthesis. The gene encoded by Swiss:P72862 has been designated cbiH but in fact represents a fusion between cbiH and cbiG. As other multi-functional proteins involved in cobalamin biosynthesis catalyze adjacent steps in the pathway, including CysG, CobL (CbiET), CobIJ and CobA-HemD, it is therefore possible that CbiG catalyzes a reaction step adjacent to CbiH. In the anaerobic pathway such a step could be the formation of a gamma lactone, which is thought to help to mediate the anaerobic ring contraction process. Within the cobalamin synthesis pathway CbiG catalyzes the both the opening of the lactone ring and the extrusion of the two-carbon fragment of cobalt-precorrin-5A from C-20 and its associated methyl group (deacylation) to give cobalt-precorrin-5B. This family is the C-terminal region, and the mid- and N-termival parts are conserved independently in other families.
Pssm-ID: 460374 [Multi-domain] Cd Length: 120 Bit Score: 103.28 E-value: 3.09e-27
Cobalamin biosynthesis central region; Members of this family are involved in cobalamin ...
108-196
1.80e-10
Cobalamin biosynthesis central region; Members of this family are involved in cobalamin synthesis. The gene refered to by Swiss:P72862 has been designated cbiH but in fact represents a fusion between cbiH and cbiG. As other multi-functional proteins involved in cobalamin biosynthesis catalyze adjacent steps in the pathway, including CysG, CobL (CbiET), CobIJ and CobA-HemD, it is therefore possible that CbiG catalyzes a reaction step adjacent to CbiH. In the anaerobic pathway such a step could be the formation of a gamma lactone, which is thought to help to mediate the anaerobic ring contraction process.
Pssm-ID: 432055 Cd Length: 88 Bit Score: 56.58 E-value: 1.80e-10
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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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,
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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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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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