nucleoside triphosphate pyrophosphohydrolase [Pelosinus fermentans]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| YabN | COG3956 | Uncharacterized conserved protein YabN, contains tetrapyrrole methylase and MazG-like ... |
228-483 | 1.64e-151 | |||||
Uncharacterized conserved protein YabN, contains tetrapyrrole methylase and MazG-like pyrophosphatase domain [General function prediction only]; : Pssm-ID: 443156 [Multi-domain] Cd Length: 268 Bit Score: 432.23 E-value: 1.64e-151
|
|||||||||
| YabN_N_like | cd11723 | N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and ... |
4-222 | 1.95e-106 | |||||
N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and similar domains; This family includes the S-AdoMet (S-adenosyl-L-methionine or SAM)-dependent tetrapyrrole methylase (TP-methylase) domain of Bacillus subtilis YabN, and similar domains. YabN is a fusion of an N-terminal TP-methylase and a C-terminal MazG-type nucleotide pyrophosphohydrolase domain. MazG-like NTP-PPases have been implicated in house-cleaning functions such as degrading abnormal (d)NTPs. TP-methylases use S-AdoMet in the methylation of diverse substrates. Most TP-methylase family members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis, other members like diphthine synthase and ribosomal RNA small subunit methyltransferase I (RsmI) act on other substrates. The specific function of YabN's TP-methylase domain is not known. : Pssm-ID: 381177 Cd Length: 218 Bit Score: 315.58 E-value: 1.95e-106
|
|||||||||
| Name | Accession | Description | Interval | E-value | |||||
| YabN | COG3956 | Uncharacterized conserved protein YabN, contains tetrapyrrole methylase and MazG-like ... |
228-483 | 1.64e-151 | |||||
Uncharacterized conserved protein YabN, contains tetrapyrrole methylase and MazG-like pyrophosphatase domain [General function prediction only]; Pssm-ID: 443156 [Multi-domain] Cd Length: 268 Bit Score: 432.23 E-value: 1.64e-151
|
|||||||||
| mazG | PRK09562 | nucleoside triphosphate pyrophosphohydrolase; Reviewed |
231-481 | 1.68e-131 | |||||
nucleoside triphosphate pyrophosphohydrolase; Reviewed Pssm-ID: 236569 [Multi-domain] Cd Length: 262 Bit Score: 381.05 E-value: 1.68e-131
|
|||||||||
| YabN_N_like | cd11723 | N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and ... |
4-222 | 1.95e-106 | |||||
N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and similar domains; This family includes the S-AdoMet (S-adenosyl-L-methionine or SAM)-dependent tetrapyrrole methylase (TP-methylase) domain of Bacillus subtilis YabN, and similar domains. YabN is a fusion of an N-terminal TP-methylase and a C-terminal MazG-type nucleotide pyrophosphohydrolase domain. MazG-like NTP-PPases have been implicated in house-cleaning functions such as degrading abnormal (d)NTPs. TP-methylases use S-AdoMet in the methylation of diverse substrates. Most TP-methylase family members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis, other members like diphthine synthase and ribosomal RNA small subunit methyltransferase I (RsmI) act on other substrates. The specific function of YabN's TP-methylase domain is not known. Pssm-ID: 381177 Cd Length: 218 Bit Score: 315.58 E-value: 1.95e-106
|
|||||||||
| mazG | TIGR00444 | MazG family protein; This family of prokaryotic proteins has no known function. It includes ... |
238-481 | 2.11e-98 | |||||
MazG family protein; This family of prokaryotic proteins has no known function. It includes the uncharacterized protein MazG in E. coli. [Unknown function, General] Pssm-ID: 273082 [Multi-domain] Cd Length: 248 Bit Score: 296.35 E-value: 2.11e-98
|
|||||||||
| NTP-PPase_MazG_Cterm | cd11529 | Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) C-terminal tandem-domain of MazG ... |
366-481 | 3.80e-59 | |||||
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) C-terminal tandem-domain of MazG proteins from Escherichia coli and bacterial homologs'; MazG is a NTP-PPase that hydrolyzes all canonical NTPs into their corresponding nucleoside monophosphates and pyrophosphate. The prototype of this family is MazG proteins from Escherichia coli (EcMazG) that represents the most abundant form consisting two sequence-related domains in tandem, this family corresponding to the C-terminal MazG-like domain. EcMazG functions as a regulator of cellular response to starvation by lowering the cellular concentration of guanosine 3',5'-bispyrophosphate (ppGpp). EcMazG exists as a dimer. Each monomer contains two tandem MazG-like domains with similarly folded globular structures. However, only the C-terminal domain has well-ordered active sites and exhibits an NTPase activity responsible for the regulation of bacterial cell survival under nutritional stress. Divalent ions, such as Mg2+ or Mn2+, are required for activity, along with structural features such as EEXX(E/D) motifs and key basic catalytic residues. It has been shown that the C-terminus NTPase activity is responsible for regulation of bacterial cell survival under nutritional stress. Pssm-ID: 212136 Cd Length: 116 Bit Score: 190.37 E-value: 3.80e-59
|
|||||||||
| TP_methylase | pfam00590 | Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
4-207 | 6.96e-30 | |||||
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of diverse substrates. This family includes a related group of bacterial proteins of unknown function. This family includes the methylase Dipthine synthase. Pssm-ID: 425769 [Multi-domain] Cd Length: 209 Bit Score: 115.90 E-value: 6.96e-30
|
|||||||||
| MazG | pfam03819 | MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in ... |
254-327 | 1.89e-27 | |||||
MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in length. It is found in the MazG protein from E. coli. It contains four conserved negatively charged residues that probably form an active site or metal binding site. This domain is found in isolation in some proteins as well as associated with pfam00590. This domain is clearly related to pfam01503 another pyrophosphohydrolase involved in histidine biosynthesis. This family may be structurally related to the NUDIX domain pfam00293 (Bateman A pers. obs.). Pssm-ID: 427525 Cd Length: 74 Bit Score: 104.60 E-value: 1.89e-27
|
|||||||||
| CobJ | COG1010 | Precorrin-3B methylase [Coenzyme transport and metabolism]; Precorrin-3B methylase is part of ... |
1-229 | 1.79e-10 | |||||
Precorrin-3B methylase [Coenzyme transport and metabolism]; Precorrin-3B methylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis Pssm-ID: 440634 Cd Length: 250 Bit Score: 61.24 E-value: 1.79e-10
|
|||||||||
| PRK05787 | PRK05787 | cobalt-precorrin-7 (C(5))-methyltransferase; |
4-223 | 5.53e-06 | |||||
cobalt-precorrin-7 (C(5))-methyltransferase; Pssm-ID: 235609 [Multi-domain] Cd Length: 210 Bit Score: 47.17 E-value: 5.53e-06
|
|||||||||
| Name | Accession | Description | Interval | E-value | |||||
| YabN | COG3956 | Uncharacterized conserved protein YabN, contains tetrapyrrole methylase and MazG-like ... |
228-483 | 1.64e-151 | |||||
Uncharacterized conserved protein YabN, contains tetrapyrrole methylase and MazG-like pyrophosphatase domain [General function prediction only]; Pssm-ID: 443156 [Multi-domain] Cd Length: 268 Bit Score: 432.23 E-value: 1.64e-151
|
|||||||||
| mazG | PRK09562 | nucleoside triphosphate pyrophosphohydrolase; Reviewed |
231-481 | 1.68e-131 | |||||
nucleoside triphosphate pyrophosphohydrolase; Reviewed Pssm-ID: 236569 [Multi-domain] Cd Length: 262 Bit Score: 381.05 E-value: 1.68e-131
|
|||||||||
| YabN_N_like | cd11723 | N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and ... |
4-222 | 1.95e-106 | |||||
N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and similar domains; This family includes the S-AdoMet (S-adenosyl-L-methionine or SAM)-dependent tetrapyrrole methylase (TP-methylase) domain of Bacillus subtilis YabN, and similar domains. YabN is a fusion of an N-terminal TP-methylase and a C-terminal MazG-type nucleotide pyrophosphohydrolase domain. MazG-like NTP-PPases have been implicated in house-cleaning functions such as degrading abnormal (d)NTPs. TP-methylases use S-AdoMet in the methylation of diverse substrates. Most TP-methylase family members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis, other members like diphthine synthase and ribosomal RNA small subunit methyltransferase I (RsmI) act on other substrates. The specific function of YabN's TP-methylase domain is not known. Pssm-ID: 381177 Cd Length: 218 Bit Score: 315.58 E-value: 1.95e-106
|
|||||||||
| mazG | TIGR00444 | MazG family protein; This family of prokaryotic proteins has no known function. It includes ... |
238-481 | 2.11e-98 | |||||
MazG family protein; This family of prokaryotic proteins has no known function. It includes the uncharacterized protein MazG in E. coli. [Unknown function, General] Pssm-ID: 273082 [Multi-domain] Cd Length: 248 Bit Score: 296.35 E-value: 2.11e-98
|
|||||||||
| NTP-PPase_MazG_Cterm | cd11529 | Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) C-terminal tandem-domain of MazG ... |
366-481 | 3.80e-59 | |||||
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) C-terminal tandem-domain of MazG proteins from Escherichia coli and bacterial homologs'; MazG is a NTP-PPase that hydrolyzes all canonical NTPs into their corresponding nucleoside monophosphates and pyrophosphate. The prototype of this family is MazG proteins from Escherichia coli (EcMazG) that represents the most abundant form consisting two sequence-related domains in tandem, this family corresponding to the C-terminal MazG-like domain. EcMazG functions as a regulator of cellular response to starvation by lowering the cellular concentration of guanosine 3',5'-bispyrophosphate (ppGpp). EcMazG exists as a dimer. Each monomer contains two tandem MazG-like domains with similarly folded globular structures. However, only the C-terminal domain has well-ordered active sites and exhibits an NTPase activity responsible for the regulation of bacterial cell survival under nutritional stress. Divalent ions, such as Mg2+ or Mn2+, are required for activity, along with structural features such as EEXX(E/D) motifs and key basic catalytic residues. It has been shown that the C-terminus NTPase activity is responsible for regulation of bacterial cell survival under nutritional stress. Pssm-ID: 212136 Cd Length: 116 Bit Score: 190.37 E-value: 3.80e-59
|
|||||||||
| PRK12334 | PRK12334 | nucleoside triphosphate pyrophosphohydrolase; Reviewed |
238-450 | 2.20e-58 | |||||
nucleoside triphosphate pyrophosphohydrolase; Reviewed Pssm-ID: 237065 [Multi-domain] Cd Length: 277 Bit Score: 194.12 E-value: 2.20e-58
|
|||||||||
| NTP-PPase_MazG_Nterm | cd11528 | Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) N-terminal tandem-domain of MazG ... |
233-346 | 1.19e-57 | |||||
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) N-terminal tandem-domain of MazG proteins from Escherichia coli and bacterial homologs; MazG is a NTP-PPase that hydrolyzes all canonical NTPs into their corresponding nucleoside monophosphates and pyrophosphate. The prototype of this family is MazG proteins from Escherichia coli (EcMazG) that represents the most abundant form consisting two sequence-related domains in tandem, this family corresponding to the N-terminal MazG-like domain. EcMazG functions as a regulator of cellular response to starvation by lowering the cellular concentration of guanosine 3',5'-bispyrophosphate (ppGpp). EcMazG exists as a dimer; each monomer contains two tandem MazG-like domains with similarly folded globular structures. However, only the C-terminal domain has well-ordered active site and exhibits an NTPase activity responsible for the regulation of bacterial cell survival under nutritional stress. Divalent ions, such as Mg2+ or Mn2+, are required for activity; however, this domain does not exhibit an NTPase activity despite containing structural features such as the EEXX(E/D) motif and key basic catalytic residues responsible for nucleotide pyrophosphohydrolysis activity. It is suggested that the N-terminal domain of EcMazG might have a house-cleaning function by hydrolyzing noncanonical NTPs whose incorporation into the nascent DNA leads to increased mutagenesis and DNA damage. Pssm-ID: 212135 Cd Length: 114 Bit Score: 186.18 E-value: 1.19e-57
|
|||||||||
| PRK12333 | PRK12333 | nucleoside triphosphate pyrophosphohydrolase; Reviewed |
235-440 | 1.69e-54 | |||||
nucleoside triphosphate pyrophosphohydrolase; Reviewed Pssm-ID: 237064 [Multi-domain] Cd Length: 204 Bit Score: 181.54 E-value: 1.69e-54
|
|||||||||
| TP_methylase | pfam00590 | Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
4-207 | 6.96e-30 | |||||
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of diverse substrates. This family includes a related group of bacterial proteins of unknown function. This family includes the methylase Dipthine synthase. Pssm-ID: 425769 [Multi-domain] Cd Length: 209 Bit Score: 115.90 E-value: 6.96e-30
|
|||||||||
| MazG | pfam03819 | MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in ... |
254-327 | 1.89e-27 | |||||
MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in length. It is found in the MazG protein from E. coli. It contains four conserved negatively charged residues that probably form an active site or metal binding site. This domain is found in isolation in some proteins as well as associated with pfam00590. This domain is clearly related to pfam01503 another pyrophosphohydrolase involved in histidine biosynthesis. This family may be structurally related to the NUDIX domain pfam00293 (Bateman A pers. obs.). Pssm-ID: 427525 Cd Length: 74 Bit Score: 104.60 E-value: 1.89e-27
|
|||||||||
| TP_methylase | cd09815 | S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ... |
7-221 | 1.49e-23 | |||||
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet (S-adenosyl-L-methionine or SAM) in the methylation of diverse substrates. Most members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis. There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. The enzymes involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Most of the enzymes are shared by both pathways and a few enzymes are pathway-specific. Diphthine synthase and ribosomal RNA small subunit methyltransferase I (RsmI) are two superfamily members that are not involved in cobalamin biosynthesis. Diphthine synthase participates in the posttranslational modification of a specific histidine residue in elongation factor 2 (EF-2) of eukaryotes and archaea to diphthamide. RsmI catalyzes the 2-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA. Other superfamily members not involved in cobalamin biosynthesis include the N-terminal tetrapyrrole methylase domain of Bacillus subtilis YabN whose specific function is unknown, and Omphalotus olearius omphalotin methyltransferase which catalyzes the automethylation of its own C-terminus; this C terminus is subsequently released and macrocyclized to give Omphalotin A, a potent nematicide. Pssm-ID: 381167 [Multi-domain] Cd Length: 219 Bit Score: 98.62 E-value: 1.49e-23
|
|||||||||
| OphMA_like | cd19916 | tetrapyrrole methylase family protein similar to Omphalotus olearius omphalotin ... |
2-221 | 2.41e-20 | |||||
tetrapyrrole methylase family protein similar to Omphalotus olearius omphalotin methyltransferase (OphMA) and Dendrothele bispora dbOphMA; OphMA, is the precursor protein of the fungal cyclic peptide Omphalotin A. Omphalotin A is a potent nematicide, having 9 out of 12 of its residues methylated at the backbone amide. Omphalotin A derives from the C-terminus of OphMA (also known as OphA). OphMA catalyzes the automethylation of its own C-terminus using S-adenosyl methionine (SAM); this C terminus is subsequently released and macrocyclized by the protease OphP to give Omphalotin A. Pssm-ID: 381179 Cd Length: 237 Bit Score: 89.85 E-value: 2.41e-20
|
|||||||||
| CobJ | COG1010 | Precorrin-3B methylase [Coenzyme transport and metabolism]; Precorrin-3B methylase is part of ... |
1-229 | 1.79e-10 | |||||
Precorrin-3B methylase [Coenzyme transport and metabolism]; Precorrin-3B methylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis Pssm-ID: 440634 Cd Length: 250 Bit Score: 61.24 E-value: 1.79e-10
|
|||||||||
| Precorrin_3B_C17_MT | cd11646 | Precorrin-3B C(17)-methyltransferase (also named CobJ or CbiH); Precorrin-3B C(17) ... |
4-229 | 2.13e-09 | |||||
Precorrin-3B C(17)-methyltransferase (also named CobJ or CbiH); Precorrin-3B C(17)-methyltransferase participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. This model includes CobJ of the aerobic pathway and CbiH of the anaerobic pathway, both as stand-alone enzymes and when CobJ or CbiH form part of bifunctional enzymes, such as in Mycobacterium tuberculosis CobIJ where CobJ fuses with a precorrin-2 C(20)-methyltransferase domain, or Bacillus megaterium CbiH60, where CbiH is fused to a nitrite and sulfite reductase-like domain. In the aerobic pathway, once CobG has generated precorrin-3b, CobJ catalyzes the methylation of precorrin-3b at C-17 to form precorrin-4 (the extruded methylated C-20 fragment is left attached as an acyl group at C-1). In the corresponding anaerobic pathway, CbiH carries out this ring contraction, using cobalt-precorrin-3b as a substrate to generate a tetramethylated delta-lactone. Pssm-ID: 381173 [Multi-domain] Cd Length: 238 Bit Score: 57.81 E-value: 2.13e-09
|
|||||||||
| CobL | COG2241 | Precorrin-6B methylase 1 [Coenzyme transport and metabolism]; Precorrin-6B methylase 1 is part ... |
1-223 | 2.64e-08 | |||||
Precorrin-6B methylase 1 [Coenzyme transport and metabolism]; Precorrin-6B methylase 1 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis Pssm-ID: 441842 [Multi-domain] Cd Length: 207 Bit Score: 54.00 E-value: 2.64e-08
|
|||||||||
| Precorrin-6Y-MT | cd11644 | Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also ... |
7-220 | 3.77e-07 | |||||
Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also known as cobalt-precorrin-7 C(5)-methyltransferase, also known as cobalt-precorrin-6Y C(5)-methyltransferase) catalyzes the methylation of C-5 in cobalt-precorrin-7 to form cobalt-precorrin-8. It participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. CbiE functions in the anaerobic pathway, it is a subunit of precorrin-6Y C5,15-methyltransferase, a bifunctional enzyme: cobalt-precorrin-7 C(5)-methyltransferase (CbiE)/cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating) (CbiT), that catalyzes 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. CbiE and CbiT can be found fused (CbiET, also called CobL), or on separate protein chains (CbiE and CbiT). In the aerobic pathway, a single enzyme called CobL catalyzes the methylations at C-5 and C-15, and the decarboxylation of the C-12 acetate side chain of precorrin-6B. Pssm-ID: 381171 [Multi-domain] Cd Length: 198 Bit Score: 50.57 E-value: 3.77e-07
|
|||||||||
| PRK05787 | PRK05787 | cobalt-precorrin-7 (C(5))-methyltransferase; |
4-223 | 5.53e-06 | |||||
cobalt-precorrin-7 (C(5))-methyltransferase; Pssm-ID: 235609 [Multi-domain] Cd Length: 210 Bit Score: 47.17 E-value: 5.53e-06
|
|||||||||
| CobF | COG2243 | Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of ... |
1-200 | 2.62e-05 | |||||
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis Pssm-ID: 441844 [Multi-domain] Cd Length: 229 Bit Score: 45.47 E-value: 2.62e-05
|
|||||||||
| PLN02625 | PLN02625 | uroporphyrin-III C-methyltransferase |
1-121 | 3.10e-05 | |||||
uroporphyrin-III C-methyltransferase Pssm-ID: 178232 [Multi-domain] Cd Length: 263 Bit Score: 45.39 E-value: 3.10e-05
|
|||||||||
| MazG | pfam03819 | MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in ... |
397-450 | 1.21e-04 | |||||
MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in length. It is found in the MazG protein from E. coli. It contains four conserved negatively charged residues that probably form an active site or metal binding site. This domain is found in isolation in some proteins as well as associated with pfam00590. This domain is clearly related to pfam01503 another pyrophosphohydrolase involved in histidine biosynthesis. This family may be structurally related to the NUDIX domain pfam00293 (Bateman A pers. obs.). Pssm-ID: 427525 Cd Length: 74 Bit Score: 40.27 E-value: 1.21e-04
|
|||||||||
| Precorrin_2_C20_MT | cd11645 | Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase ... |
7-221 | 4.44e-04 | |||||
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase (also known as S-adenosyl-L-methionine--precorrin-2 methyltransferase) participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. Precorrin-2 C20-methyltransferase catalyzes methylation at the C-20 position of a cyclic tetrapyrrole ring of precorrin-2 using S-adenosylmethionine as a methyl group source to produce precorrin-3A. In the anaerobic pathway, cobalt is inserted into precorrin-2 by CbiK to generate cobalt-precorrin-2, which is the substrate for CbiL, a C20 methyltransferase. In Clostridium difficile, CbiK and CbiL are fused into a bifunctional enzyme. In the aerobic pathway, the precorrin-2 C20-methyltransferase is named CobI. This family includes CbiL and CobI precorrin-2 C20-methyltransferases, both as stand-alone enzymes and when CbiL forms part of a bifunctional enzyme. Pssm-ID: 381172 [Multi-domain] Cd Length: 223 Bit Score: 41.72 E-value: 4.44e-04
|
|||||||||
| Blast search parameters | ||||
|
