cobalamin-independent methionine synthase, partial [Saccharomyces bayanus x Saccharomyces cerevisiae x Saccharomyces kudriavzevii]
uroporphyrinogen decarboxylase/cobalamine-independent methonine synthase family protein( domain architecture ID 1254)
uroporphyrinogen decarboxylase (URO-D)/cobalamine-independent methonine synthase (CIMS) family protein, similar to URO-D that decarboxylates the four acetate side chains of uroporphyrinogen III (uro-III) to create coproporphyrinogen III, an important branching point of the tetrapyrrole biosynthetic pathway
List of domain hits
Name | Accession | Description | Interval | E-value | |||
URO-D_CIMS_like super family | cl00464 | The URO-D_CIMS_like protein superfamily includes bacterial and eukaryotic uroporphyrinogen ... |
1-138 | 1.06e-58 | |||
The URO-D_CIMS_like protein superfamily includes bacterial and eukaryotic uroporphyrinogen decarboxylases (URO-D), coenzyme M methyltransferases and other putative bacterial methyltransferases, as well as cobalamine (B12) independent methionine synthases. Despite their sequence similarities, members of this family have clearly different functions. Uroporphyrinogen decarboxylase (URO-D) decarboxylates the four acetate side chains of uroporphyrinogen III (uro-III) to create coproporphyrinogen III, an important branching point of the tetrapyrrole biosynthetic pathway. The methyltransferases represented here are important for ability of methanogenic organisms to use other compounds than carbon dioxide for reduction to methane, and methionine synthases transfer a methyl group from a folate cofactor to L-homocysteine in a reaction requiring zinc. The actual alignment was detected with superfamily member cd03312: Pssm-ID: 469779 [Multi-domain] Cd Length: 360 Bit Score: 185.43 E-value: 1.06e-58
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Name | Accession | Description | Interval | E-value | |||
CIMS_N_terminal_like | cd03312 | CIMS - Cobalamine-independent methonine synthase, or MetE, N-terminal domain_like. Many ... |
1-138 | 1.06e-58 | |||
CIMS - Cobalamine-independent methonine synthase, or MetE, N-terminal domain_like. Many members have been characterized as 5-methyltetrahydropteroyltriglutamate-homocysteine methyltransferases, EC:2.1.1.14, mostly from bacteria and plants. This enzyme catalyses the last step in the production of methionine by transferring a methyl group from 5-methyltetrahydrofolate to L-homocysteine without using an intermediate methyl carrier. The active enzyme has a dual (beta-alpha)8-barrel structure, and this model covers the N-terminal barrel, and a few single-barrel sequences most similar to the N-terminal barrel. It is assumed that the homologous N-terminal barrel has evolved from the C-terminus via gene duplication and has subsequently lost binding sites, and it seems as if the two barrels forming the active enzyme may sometimes reside on different polypeptides. The C-terminal domain incorporates the Zinc ion, which binds and activates homocysteine. Side chains from both barrels contribute to the binding of the folate substrate. Pssm-ID: 239428 [Multi-domain] Cd Length: 360 Bit Score: 185.43 E-value: 1.06e-58
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PRK05222 | PRK05222 | 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional |
1-138 | 3.49e-53 | |||
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional Pssm-ID: 235367 [Multi-domain] Cd Length: 758 Bit Score: 178.38 E-value: 3.49e-53
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Meth_synt_1 | pfam08267 | Cobalamin-independent synthase, N-terminal domain; The N-terminal domain and C-terminal ... |
1-125 | 1.18e-48 | |||
Cobalamin-independent synthase, N-terminal domain; The N-terminal domain and C-terminal domains of cobalamin-independent synthases together define a catalytic cleft in the enzyme. The N-terminal domain is thought to bind the substrate, in particular, the negatively charged polyglutamate chain. The N-terminal domain is also thought to stabilize a loop from the C-terminal domain. Pssm-ID: 400526 [Multi-domain] Cd Length: 310 Bit Score: 158.13 E-value: 1.18e-48
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MetE | COG0620 | Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
1-138 | 5.72e-35 | |||
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; Methionine synthase II (cobalamin-independent) is part of the Pathway/BioSystem: Methionine biosynthesis Pssm-ID: 440385 [Multi-domain] Cd Length: 325 Bit Score: 122.94 E-value: 5.72e-35
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Name | Accession | Description | Interval | E-value | |||
CIMS_N_terminal_like | cd03312 | CIMS - Cobalamine-independent methonine synthase, or MetE, N-terminal domain_like. Many ... |
1-138 | 1.06e-58 | |||
CIMS - Cobalamine-independent methonine synthase, or MetE, N-terminal domain_like. Many members have been characterized as 5-methyltetrahydropteroyltriglutamate-homocysteine methyltransferases, EC:2.1.1.14, mostly from bacteria and plants. This enzyme catalyses the last step in the production of methionine by transferring a methyl group from 5-methyltetrahydrofolate to L-homocysteine without using an intermediate methyl carrier. The active enzyme has a dual (beta-alpha)8-barrel structure, and this model covers the N-terminal barrel, and a few single-barrel sequences most similar to the N-terminal barrel. It is assumed that the homologous N-terminal barrel has evolved from the C-terminus via gene duplication and has subsequently lost binding sites, and it seems as if the two barrels forming the active enzyme may sometimes reside on different polypeptides. The C-terminal domain incorporates the Zinc ion, which binds and activates homocysteine. Side chains from both barrels contribute to the binding of the folate substrate. Pssm-ID: 239428 [Multi-domain] Cd Length: 360 Bit Score: 185.43 E-value: 1.06e-58
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PRK05222 | PRK05222 | 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional |
1-138 | 3.49e-53 | |||
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional Pssm-ID: 235367 [Multi-domain] Cd Length: 758 Bit Score: 178.38 E-value: 3.49e-53
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Meth_synt_1 | pfam08267 | Cobalamin-independent synthase, N-terminal domain; The N-terminal domain and C-terminal ... |
1-125 | 1.18e-48 | |||
Cobalamin-independent synthase, N-terminal domain; The N-terminal domain and C-terminal domains of cobalamin-independent synthases together define a catalytic cleft in the enzyme. The N-terminal domain is thought to bind the substrate, in particular, the negatively charged polyglutamate chain. The N-terminal domain is also thought to stabilize a loop from the C-terminal domain. Pssm-ID: 400526 [Multi-domain] Cd Length: 310 Bit Score: 158.13 E-value: 1.18e-48
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MetE | COG0620 | Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
1-138 | 5.72e-35 | |||
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; Methionine synthase II (cobalamin-independent) is part of the Pathway/BioSystem: Methionine biosynthesis Pssm-ID: 440385 [Multi-domain] Cd Length: 325 Bit Score: 122.94 E-value: 5.72e-35
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PLN02475 | PLN02475 | 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase |
1-138 | 1.44e-25 | |||
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase Pssm-ID: 215264 [Multi-domain] Cd Length: 766 Bit Score: 100.62 E-value: 1.44e-25
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CIMS_like | cd03310 | CIMS - Cobalamine-independent methonine synthase, or MetE. Many members have been ... |
2-136 | 4.26e-04 | |||
CIMS - Cobalamine-independent methonine synthase, or MetE. Many members have been characterized as 5-methyltetrahydropteroyltriglutamate-homocysteine methyltransferases, EC:2.1.1.14, mostly from bacteria and plants. This enzyme catalyses the last step in the production of methionine by transferring a methyl group from 5-methyltetrahydrofolate to L-homocysteine without using an intermediate methyl carrier. The active enzyme has a dual (beta-alpha)8-barrel structure, and this model covers both the N-and C-terminal barrel, and some single-barrel sequences, mostly from Archaea. It is assumed that the homologous N-terminal barrel has evolved from the C-terminus via gene duplication and has subsequently lost binding sites, and it seems as if the two barrels forming the active enzyme may sometimes reside on different polypeptides. The C-terminal domain incorporates the Zinc ion, which binds and activates homocysteine. Side chains from both barrels contribute to the binding of the folate substrate. Pssm-ID: 239426 [Multi-domain] Cd Length: 321 Bit Score: 38.95 E-value: 4.26e-04
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Blast search parameters | ||||
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