Cobalamin biosynthesis protein CbiK, Co2+ chelatase [Coenzyme transport and metabolism]; ...
1-262
5.96e-147
Cobalamin biosynthesis protein CbiK, Co2+ chelatase [Coenzyme transport and metabolism]; Cobalamin biosynthesis protein CbiK, Co2+ chelatase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
:
Pssm-ID: 443850 [Multi-domain] Cd Length: 265 Bit Score: 411.50 E-value: 5.96e-147
Cobalamin biosynthesis protein CbiK, Co2+ chelatase [Coenzyme transport and metabolism]; ...
1-262
5.96e-147
Cobalamin biosynthesis protein CbiK, Co2+ chelatase [Coenzyme transport and metabolism]; Cobalamin biosynthesis protein CbiK, Co2+ chelatase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 443850 [Multi-domain] Cd Length: 265 Bit Score: 411.50 E-value: 5.96e-147
Anaerobic cobalamin biosynthetic cobalt chelatase (CbiK), C-terminal domain. CbiK is part of ...
138-239
4.75e-53
Anaerobic cobalamin biosynthetic cobalt chelatase (CbiK), C-terminal domain. CbiK is part of the cobalt-early path for cobalamin biosynthesis. It catalyzes the insertion of cobalt into the oxidized form of precorrin-2, factor II (sirohydrochlorin), the second step of the anaerobic branch of vitamin B12 biosynthesis. CbiK belongs to the class II family of chelatases, and is a homomeric enzyme that does not require ATP for its enzymatic activity.
Pssm-ID: 239506 [Multi-domain] Cd Length: 103 Bit Score: 167.42 E-value: 4.75e-53
Cobalamin biosynthesis protein CbiK, Co2+ chelatase [Coenzyme transport and metabolism]; ...
1-262
5.96e-147
Cobalamin biosynthesis protein CbiK, Co2+ chelatase [Coenzyme transport and metabolism]; Cobalamin biosynthesis protein CbiK, Co2+ chelatase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 443850 [Multi-domain] Cd Length: 265 Bit Score: 411.50 E-value: 5.96e-147
Anaerobic cobalamin biosynthetic cobalt chelatase (CbiK), C-terminal domain. CbiK is part of ...
138-239
4.75e-53
Anaerobic cobalamin biosynthetic cobalt chelatase (CbiK), C-terminal domain. CbiK is part of the cobalt-early path for cobalamin biosynthesis. It catalyzes the insertion of cobalt into the oxidized form of precorrin-2, factor II (sirohydrochlorin), the second step of the anaerobic branch of vitamin B12 biosynthesis. CbiK belongs to the class II family of chelatases, and is a homomeric enzyme that does not require ATP for its enzymatic activity.
Pssm-ID: 239506 [Multi-domain] Cd Length: 103 Bit Score: 167.42 E-value: 4.75e-53
Anaerobic cobalamin biosynthetic cobalt chelatase (CbiK), N-terminal domain. CbiK is part of ...
3-131
7.07e-52
Anaerobic cobalamin biosynthetic cobalt chelatase (CbiK), N-terminal domain. CbiK is part of the cobalt-early path for cobalamin biosynthesis. It catalyzes the insertion of cobalt into the oxidized form of precorrin-2, factor II (sirohydrochlorin), the second step of the anaerobic branch of vitamin B12 biosynthesis. CbiK belongs to the class II family of chelatases and is a homomeric enzyme that does not require ATP for its enzymatic activity.
Pssm-ID: 239505 Cd Length: 127 Bit Score: 165.09 E-value: 7.07e-52
Class II Chelatase: a family of ATP-independent monomeric or homodimeric enzymes that catalyze ...
140-234
1.80e-13
Class II Chelatase: a family of ATP-independent monomeric or homodimeric enzymes that catalyze the insertion of metal into protoporphyrin rings. This family includes protoporphyrin IX ferrochelatase (HemH), sirohydrochlorin ferrochelatase (SirB) and the cobaltochelatases, CbiK and CbiX. HemH and SirB are involved in heme and siroheme biosynthesis, respectively, while the cobaltochelatases are associated with cobalamin biosynthesis. Excluded from this family are the ATP-dependent heterotrimeric chelatases (class I) and the multifunctional homodimeric enzymes with dehydrogenase and chelatase activities (class III).
Pssm-ID: 239503 [Multi-domain] Cd Length: 101 Bit Score: 64.70 E-value: 1.80e-13
Class II Chelatase: a family of ATP-independent monomeric or homodimeric enzymes that catalyze ...
4-91
7.07e-11
Class II Chelatase: a family of ATP-independent monomeric or homodimeric enzymes that catalyze the insertion of metal into protoporphyrin rings. This family includes protoporphyrin IX ferrochelatase (HemH), sirohydrochlorin ferrochelatase (SirB) and the cobaltochelatases, CbiK and CbiX. HemH and SirB are involved in heme and siroheme biosynthesis, respectively, while the cobaltochelatases are associated with cobalamin biosynthesis. Excluded from this family are the ATP-dependent heterotrimeric chelatases (class I) and the multifunctional homodimeric enzymes with dehydrogenase and chelatase activities (class III).
Pssm-ID: 239503 [Multi-domain] Cd Length: 101 Bit Score: 57.77 E-value: 7.07e-11
Sirohydrochlorin cobalt chelatase (CbiX) and sirohydrochlorin iron chelatase (SirB), ...
178-211
4.73e-03
Sirohydrochlorin cobalt chelatase (CbiX) and sirohydrochlorin iron chelatase (SirB), N-terminal domain. SirB catalyzes the ferro-chelation of sirohydrochlorin to siroheme, the prosthetic group of sulfite and nitrite reductases. CbiX is a cobaltochelatase, responsible for the chelation of Co2+ into sirohydrochlorin, an important step in the vitamin B12 biosynthetic pathway. CbiX often contains a C-terminal histidine-rich region that may be important for metal delivery and/or storage, and may also contain an iron-sulfur center. Both are found in a wide range of bacteria. This subgroup also contains single domain proteins from archaea and bacteria which may represent the ancestral form of class II chelatases before domain duplication occurred.
Pssm-ID: 239509 [Multi-domain] Cd Length: 101 Bit Score: 35.63 E-value: 4.73e-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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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
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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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