ATP:cob(I)alamin adenosyltransferase containing a GlcG/heme-degrading domain, catalyzes the final step in the conversion of cyanocobalamin (vitamin B12) to adenosylcobalamin, catalyzing the transfer of the adenosyl moiety from ATP to cobalamin
Cob(II)alamin adenosyltransferase [Coenzyme transport and metabolism]; Cob(II)alamin ...
1-167
1.37e-75
Cob(II)alamin adenosyltransferase [Coenzyme transport and metabolism]; Cob(II)alamin adenosyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
:
Pssm-ID: 441699 Cd Length: 180 Bit Score: 230.01 E-value: 1.37e-75
Cob(II)alamin adenosyltransferase [Coenzyme transport and metabolism]; Cob(II)alamin ...
1-167
1.37e-75
Cob(II)alamin adenosyltransferase [Coenzyme transport and metabolism]; Cob(II)alamin adenosyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 441699 Cd Length: 180 Bit Score: 230.01 E-value: 1.37e-75
Cobalamin adenosyltransferase; Cobalamin adenosyltransferase This family contains the gene ...
4-166
1.45e-66
Cobalamin adenosyltransferase; Cobalamin adenosyltransferase This family contains the gene products of PduO and EutT which are both cobalamin adenosyltransferases. PduO is a protein with ATP:cob(I)alamin adenosyltransferase activity. The main role of this protein is the conversion of inactive cobalamins to AdoCbl for 1,2-propanediol degradation.The EutT enzyme appears to be an adenosyl transferase, converting CNB12 to AdoB12.
Pssm-ID: 460384 Cd Length: 163 Bit Score: 206.58 E-value: 1.45e-66
ATP:cob(I)alamin adenosyltransferase; This model represents as ATP:cob(I)alamin ...
4-166
3.21e-50
ATP:cob(I)alamin adenosyltransferase; This model represents as ATP:cob(I)alamin adenosyltransferase family corresponding to the N-terminal half of Salmonella PduO, a 1,2-propanediol utilization protein that probably is bifunctional. PduO represents one of at least three families of ATP:corrinoid adenosyltransferase: others are CobA (which partially complements PduO) and EutT. It was not clear originally whether ATP:cob(I)alamin adenosyltransferase activity resides in the N-terminal region of PduO, modeled here, but this has now become clear from the characterization of MeaD from Methylobacterium extorquens. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 213544 Cd Length: 171 Bit Score: 164.81 E-value: 3.21e-50
Haem degrading protein HbpS-like; This entry includes haem degrading protein HbpS from ...
200-323
3.89e-17
Haem degrading protein HbpS-like; This entry includes haem degrading protein HbpS from Streptomyces reticuli (swiss:Q9RIM2) and and GlcG from Escherichia coli. HbpS is up-regulated in response to haemin- and peroxide-based oxidative stress. It interacts with the SenS/SenR two-component signal transduction system. Iron binds to surface-exposed lysine residues of an octomeric assembly of the protein. The structure of GlcG is composed of an alpha-beta(2)-alpha(3)-beta(2)-alpha fold, similar to the Roadblock/LC7 domain.
Pssm-ID: 461095 [Multi-domain] Cd Length: 116 Bit Score: 76.00 E-value: 3.89e-17
Cob(II)alamin adenosyltransferase [Coenzyme transport and metabolism]; Cob(II)alamin ...
1-167
1.37e-75
Cob(II)alamin adenosyltransferase [Coenzyme transport and metabolism]; Cob(II)alamin adenosyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 441699 Cd Length: 180 Bit Score: 230.01 E-value: 1.37e-75
Cobalamin adenosyltransferase; Cobalamin adenosyltransferase This family contains the gene ...
4-166
1.45e-66
Cobalamin adenosyltransferase; Cobalamin adenosyltransferase This family contains the gene products of PduO and EutT which are both cobalamin adenosyltransferases. PduO is a protein with ATP:cob(I)alamin adenosyltransferase activity. The main role of this protein is the conversion of inactive cobalamins to AdoCbl for 1,2-propanediol degradation.The EutT enzyme appears to be an adenosyl transferase, converting CNB12 to AdoB12.
Pssm-ID: 460384 Cd Length: 163 Bit Score: 206.58 E-value: 1.45e-66
ATP:cob(I)alamin adenosyltransferase; This model represents as ATP:cob(I)alamin ...
4-166
3.21e-50
ATP:cob(I)alamin adenosyltransferase; This model represents as ATP:cob(I)alamin adenosyltransferase family corresponding to the N-terminal half of Salmonella PduO, a 1,2-propanediol utilization protein that probably is bifunctional. PduO represents one of at least three families of ATP:corrinoid adenosyltransferase: others are CobA (which partially complements PduO) and EutT. It was not clear originally whether ATP:cob(I)alamin adenosyltransferase activity resides in the N-terminal region of PduO, modeled here, but this has now become clear from the characterization of MeaD from Methylobacterium extorquens. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 213544 Cd Length: 171 Bit Score: 164.81 E-value: 3.21e-50
Haem degrading protein HbpS-like; This entry includes haem degrading protein HbpS from ...
200-323
3.89e-17
Haem degrading protein HbpS-like; This entry includes haem degrading protein HbpS from Streptomyces reticuli (swiss:Q9RIM2) and and GlcG from Escherichia coli. HbpS is up-regulated in response to haemin- and peroxide-based oxidative stress. It interacts with the SenS/SenR two-component signal transduction system. Iron binds to surface-exposed lysine residues of an octomeric assembly of the protein. The structure of GlcG is composed of an alpha-beta(2)-alpha(3)-beta(2)-alpha fold, similar to the Roadblock/LC7 domain.
Pssm-ID: 461095 [Multi-domain] Cd Length: 116 Bit Score: 76.00 E-value: 3.89e-17
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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