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Search results 401 to 439 out of 439 for Cobl

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Type Details Score
Publication
- | J:144086
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
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Publication
- | J:262123
     
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
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Publication
1732195 | -
First Author: Blanche F
Year: 1992
Journal: J Bacteriol
Title: Biosynthesis of vitamin B12 in Pseudomonas denitrificans: the biosynthetic sequence from precorrin-6y to precorrin-8x is catalyzed by the cobL gene product.
Volume: 174
Issue: 3
Pages: 1050-2
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Protein
B1AZ20
Organism: Mus musculus/domesticus
Length: 175  
Fragment?: true
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Protein
Q8BJK8
Organism: Mus musculus/domesticus
Length: 155  
Fragment?: true
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Protein
F6ZEZ1
Organism: Mus musculus/domesticus
Length: 159  
Fragment?: true
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Protein
B1AZ25
Organism: Mus musculus/domesticus
Length: 142  
Fragment?: true
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Protein
G3UWP1
Organism: Mus musculus/domesticus
Length: 208  
Fragment?: true
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Publication
21816349 | -
First Author: Husson C
Year: 2011
Journal: Mol Cell
Title: Cordon-Bleu uses WH2 domains as multifunctional dynamizers of actin filament assembly.
Volume: 43
Issue: 3
Pages: 464-77
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Publication
29233863 | J:255503
First Author: Izadi M
Year: 2018
Journal: J Cell Biol
Title: Cobl-like promotes actin filament formation and dendritic branching using only a single WH2 domain.
Volume: 217
Issue: 1
Pages: 211-230
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Protein Domain
IPR039895 | COBL-like
Type: Family
Description: This entry includes protein cordon-bleu (COBL) and COBLL1. Single WH2 domains can sequester G-actin. COBL contains three G-actin-binding WH2 domains and act as a dynamizer of actin assembly. COBL has profilin-like filament nucleating and severing activities []. It is a CaM-controlled component important for early neuronal morphogenesis []. Cordon-Bleu-like (COBLL), an evolutionary ancestor of the actin nucleator Cobl, contains only one WH2 domain. It functions with the F-actin-binding protein Abp1 in Ca2+/CaM regulated dendritic branching [].
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Protein
Q3UMF0
Organism: Mus musculus/domesticus
Length: 1273  
Fragment?: false
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Protein
B1AZ14
Organism: Mus musculus/domesticus
Length: 1241  
Fragment?: false
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Protein
B1AZ26
Organism: Mus musculus/domesticus
Length: 346  
Fragment?: true
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Protein
B1AZ15
Organism: Mus musculus/domesticus
Length: 1240  
Fragment?: false
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Protein
G3UZ73
Organism: Mus musculus/domesticus
Length: 410  
Fragment?: false
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Protein Domain
IPR021745 | CbiG_mid
Type: Domain
Description: Members of this family are involved in cobalamin synthesis. The gene encoded by has been designated cbiH but in fact represents a fusion between cbiH and cbiG. As other multi-functional proteins involved in cobalamin biosynthesis catalyse adjacent steps in the pathway, including CysG, CobL (CbiET), CobIJ and CobA-HemD, it is therefore possible that CbiG catalyses 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 [].
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Publication
36791197 | J:333393
First Author: Tsukita K
Year: 2023
Journal: Sci Adv
Title: Phase separation of an actin nucleator by junctional microtubules regulates epithelial function.
Volume: 9
Issue: 7
Pages: eadf6358
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Protein
F6RR81
Organism: Mus musculus/domesticus
Length: 216  
Fragment?: true
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Protein Domain
IPR021744 | CbiG_N
Type: Domain
Description: Members of this family are involved in cobalamin synthesis. The gene encoded by has been designated cbiH but in fact represents a fusion between cbiH and cbiG. As other multi-functional proteins involved in cobalamin biosynthesis catalyse adjacent steps in the pathway, including CysG, CobL (CbiET), CobIJ and CobA-HemD, it is therefore possible that CbiG catalyses 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 catalyses 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.
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Protein Domain
IPR006365 | Cbl_synth_CobL
Type: Family
Description: Cobalamin (vitamin B12) is a structurally complex cofactor, consisting of a modified tetrapyrrole with a centrally chelated cobalt. Cobalamin is usually found in one of two biologically active forms: methylcobalamin and adocobalamin. Most prokaryotes, as well as animals, have cobalamin-dependent enzymes, whereas plants and fungi do not appear to use it. In bacteria and archaea, these include methionine synthase, ribonucleotide reductase, glutamate and methylmalonyl-CoA mutases, ethanolamine ammonia lyase, and diol dehydratase []. In mammals, cobalamin is obtained through the diet, and is required for methionine synthase and methylmalonyl-CoA mutase []. There are at least two distinct cobalamin biosynthetic pathways in bacteria []:Aerobic pathway that requires oxygen and in which cobalt is inserted late in the pathway []; found in Pseudomonas denitrificans and Rhodobacter capsulatus.Anaerobic pathway in which cobalt insertion is the first committed step towards cobalamin synthesis [, ]; found in Salmonella typhimurium, Bacillus megaterium, and Propionibacterium freudenreichii subsp. shermanii. Either pathway can be divided into two parts: (1) corrin ring synthesis (differs in aerobic and anaerobic pathways) and (2) adenosylation of corrin ring, attachment of aminopropanol arm, and assembly of the nucleotide loop (common to both pathways) []. There are about 30 enzymes involved in either pathway, where those involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Several of these enzymes are pathway-specific: CbiD, CbiG, and CbiK are specific to the anaerobic route of S. typhimurium, whereas CobE, CobF, CobG, CobN, CobS, CobT, and CobW are unique to the aerobic pathway of P. denitrificans.This entry represents CobL precorrin-6Y C5,15-methyltransferase () from the aerobic pathway. CobL is a bifunctional enzyme that catalyses two methylations (at C-5 and C-15) in precorrin-6Y, as well as the decarboxylation of the acetate side chain located in ring C, in order to generate precorrin-8X. []. In the anaerobic pathway, two enzymes are required to produce precorrin-8X: CbiE and CbiT, which can be fused as CbiET (sometimes also called CobL) [].
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Publication
32768501 | J:301090
First Author: Cracknell T
Year: 2020
Journal: Exp Cell Res
Title: Proteomic resolution of IGFN1 complexes reveals a functional interaction with the actin nucleating protein COBL.
Volume: 395
Issue: 2
Pages: 112179
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Protein
Q5NBX1
Organism: Mus musculus/domesticus
Length: 1337  
Fragment?: false
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Protein
G5E8P4
Organism: Mus musculus/domesticus
Length: 1312  
Fragment?: false
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Protein
G3UWY3
Organism: Mus musculus/domesticus
Length: 1330  
Fragment?: false
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Protein
B2RWU4
Organism: Mus musculus/domesticus
Length: 1337  
Fragment?: false
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Protein Domain
IPR014008 | Cbl_synth_MTase_CbiT
Type: Family
Description: Cobalamin (vitamin B12) is a structurally complex cofactor, consisting of a modified tetrapyrrole with a centrally chelated cobalt. Cobalamin is usually found in one of two biologically active forms: methylcobalamin and adocobalamin. Most prokaryotes, as well as animals, have cobalamin-dependent enzymes, whereas plants and fungi do not appear to use it. In bacteria and archaea, these include methionine synthase, ribonucleotide reductase, glutamate and methylmalonyl-CoA mutases, ethanolamine ammonia lyase, and diol dehydratase []. In mammals, cobalamin is obtained through the diet, and is required for methionine synthase and methylmalonyl-CoA mutase []. There are at least two distinct cobalamin biosynthetic pathways in bacteria []:Aerobic pathway that requires oxygen and in which cobalt is inserted late in the pathway []; found in Pseudomonas denitrificans and Rhodobacter capsulatus.Anaerobic pathway in which cobalt insertion is the first committed step towards cobalamin synthesis [, ]; found in Salmonella typhimurium, Bacillus megaterium, and Propionibacterium freudenreichii subsp. shermanii. Either pathway can be divided into two parts: (1) corrin ring synthesis (differs in aerobic and anaerobic pathways) and (2) adenosylation of corrin ring, attachment of aminopropanol arm, and assembly of the nucleotide loop (common to both pathways) []. There are about 30 enzymes involved in either pathway, where those involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Several of these enzymes are pathway-specific: CbiD, CbiG, and CbiK are specific to the anaerobic route of S. typhimurium, whereas CobE, CobF, CobG, CobN, CobS, CobT, and CobW are unique to the aerobic pathway of P. denitrificans.The CbiT subunit of precorrin-6Y C5,15-methyltransferase () is a bifunctional enzyme that catalyses two methylations (at C-5 and C-15) in precorrin-6Y, as well as the decarboxylation of the acetate side chain located in ring C, in order to generate precorrin-8X. In the anaerobic pathway, two enzymes are required to produce precorrin-8X: CbiE and CbiT, which can be fused as CbiET (sometimes called CobL) []. In the aerobic pathway, the enzyme is a fusion of CbiE and CbiT which is refered to as CobL []. CbiT is thought to catalyse one of the methylation reactions, though this has not been completely proven [].This entry represents the CbiT subunit of the aerobic and anaerobic enzymes. In the anaerobic proteins it comproses the entire length of the protein, while in the aerobic enzymes it is fused with CbiE to form the bifunctional CobL protein.
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Publication
12429089 | -
First Author: Keller JP
Year: 2002
Journal: Structure
Title: The crystal structure of MT0146/CbiT suggests that the putative precorrin-8w decarboxylase is a methyltransferase.
Volume: 10
Issue: 11
Pages: 1475-87
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Protein Domain
IPR012818 | CbiE
Type: Domain
Description: Cobalamin (vitamin B12) is a structurally complex cofactor, consisting of a modified tetrapyrrole with a centrally chelated cobalt. Cobalamin is usually found in one of two biologically active forms: methylcobalamin and adocobalamin. Most prokaryotes, as well as animals, have cobalamin-dependent enzymes, whereas plants and fungi do not appear to use it. In bacteria and archaea, these include methionine synthase, ribonucleotide reductase, glutamate and methylmalonyl-CoA mutases, ethanolamine ammonia lyase, and diol dehydratase []. In mammals, cobalamin is obtained through the diet, and is required for methionine synthase and methylmalonyl-CoA mutase []. There are at least two distinct cobalamin biosynthetic pathways in bacteria []:Aerobic pathway that requires oxygen and in which cobalt is inserted late in the pathway []; found in Pseudomonas denitrificans and Rhodobacter capsulatus.Anaerobic pathway in which cobalt insertion is the first committed step towards cobalamin synthesis [, ]; found in Salmonella typhimurium, Bacillus megaterium, and Propionibacterium freudenreichii subsp. shermanii. Either pathway can be divided into two parts: (1) corrin ring synthesis (differs in aerobic and anaerobic pathways) and (2) adenosylation of corrin ring, attachment of aminopropanol arm, and assembly of the nucleotide loop (common to both pathways) []. There are about 30 enzymes involved in either pathway, where those involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Several of these enzymes are pathway-specific: CbiD, CbiG, and CbiK are specific to the anaerobic route of S. typhimurium, whereas CobE, CobF, CobG, CobN, CobS, CobT, and CobW are unique to the aerobic pathway of P. denitrificans.This entry represents CbiE subunit of precorrin-6Y C5,15-methyltransferase () from the anaerobic pathway, a bifunctional enzyme that catalyses two methylations (at C-5 and C-15) in precorrin-6Y, as well as the decarboxylation of the acetate side chain located in ring C, in order to generate precorrin-8X. In the anaerobic pathway, two enzymes are required to produce precorrin-8X: CbiE and CbiT, which can be fused as CbiET (sometimes called CobL) []. In the aerobic pathway, the bifunctional enzyme is CobL [].
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Publication
16198574 | -
First Author: Santander PJ
Year: 2006
Journal: Bioorg Med Chem
Title: Structural characterization of novel cobalt corrinoids synthesized by enzymes of the vitamin B12 anaerobic pathway.
Volume: 14
Issue: 3
Pages: 724-31
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Protein Domain
IPR023475 | CbiT
Type: Family
Description: CbiT is a bifunctional enzyme that catalyses two methylations (at C-5 and C-15) in precorrin-6Y, as well as the decarboxylation of the acetate side chain located in ring C, in order to generate precorrin-8X. It participates in the biosynthesis of vitamin B12 []. In the anaerobic pathway, two enzymes are required to produce precorrin-8X: CbiE and CbiT, which can be fused as CbiET (sometimes called CobL) []. In the aerobic pathway, the enzyme is a fusion of CbiE and CbiT which is refered to as CobL []. CbiT is thought to catalyse one of the methylation reactions [, ].Cobalamin (vitamin B12) is a structurally complex cofactor, consisting of a modified tetrapyrrole with a centrally chelated cobalt. Cobalamin is usually found in one of two biologically active forms: methylcobalamin and adocobalamin. Most prokaryotes, as well as animals, have cobalamin-dependent enzymes, whereas plants and fungi do not appear to use it. In bacteria and archaea, these include methionine synthase, ribonucleotide reductase, glutamate and methylmalonyl-CoA mutases, ethanolamine ammonia lyase, and diol dehydratase []. In mammals, cobalamin is obtained through the diet, and is required for methionine synthase and methylmalonyl-CoA mutase []. There are at least two distinct cobalamin biosynthetic pathways in bacteria []:Aerobic pathway that requires oxygen and in which cobalt is inserted late in the pathway []; found in Pseudomonas denitrificans and Rhodobacter capsulatus.Anaerobic pathway in which cobalt insertion is the first committed step towards cobalamin synthesis [, ]; found in Salmonella typhimurium, Bacillus megaterium, and Propionibacterium freudenreichii subsp. shermanii. Either pathway can be divided into two parts: (1) corrin ring synthesis (differs in aerobic and anaerobic pathways) and (2) adenosylation of corrin ring, attachment of aminopropanol arm, and assembly of the nucleotide loop (common to both pathways) []. There are about 30 enzymes involved in either pathway, where those involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Several of these enzymes are pathway-specific: CbiD, CbiG, and CbiK are specific to the anaerobic route of S. typhimurium, whereas CobE, CobF, CobG, CobN, CobS, CobT, and CobW are unique to the aerobic pathway of P. denitrificans.
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Publication
9742225 | -
 
First Author: Raux E
Year: 1998
Journal: Biochem J
Title: Cobalamin (vitamin B12) biosynthesis: identification and characterization of a Bacillus megaterium cobI operon.
Volume: 335 ( Pt 1)
Pages: 159-66
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Publication
12869542 | -
First Author: Rodionov DA
Year: 2003
Journal: J Biol Chem
Title: Comparative genomics of the vitamin B12 metabolism and regulation in prokaryotes.
Volume: 278
Issue: 42
Pages: 41148-59
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Publication
17163662 | -
First Author: Banerjee R
Year: 2006
Journal: ACS Chem Biol
Title: B12 trafficking in mammals: A for coenzyme escort service.
Volume: 1
Issue: 3
Pages: 149-59
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Publication
16042605 | -
First Author: Heldt D
Year: 2005
Journal: Biochem Soc Trans
Title: Aerobic synthesis of vitamin B12: ring contraction and cobalt chelation.
Volume: 33
Issue: Pt 4
Pages: 815-9
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Publication
12055304 | -
First Author: Roessner CA
Year: 2002
Journal: Microbiology
Title: Isolation and characterization of 14 additional genes specifying the anaerobic biosynthesis of cobalamin (vitamin B12) in Propionibacterium freudenreichii (P. shermanii).
Volume: 148
Issue: Pt 6
Pages: 1845-53
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Publication
23922391 | -
First Author: Moore SJ
Year: 2013
Journal: Proc Natl Acad Sci U S A
Title: Elucidation of the anaerobic pathway for the corrin component of cobalamin (vitamin B12).
Volume: 110
Issue: 37
Pages: 14906-11
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Publication
11153269 | -
 
First Author: Roessner CA
Year: 2001
Journal: Vitam Horm
Title: Multiple biosynthetic pathways for vitamin B12: variations on a central theme.
Volume: 61
Pages: 267-97
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Publication
11215515 | -
First Author: Raux E
Year: 2000
Journal: Cell Mol Life Sci
Title: Biosynthesis of cobalamin (vitamin B12): a bacterial conundrum.
Volume: 57
Issue: 13-14
Pages: 1880-93
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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