methionyl-tRNA formyltransferase [Lactobacillus iners]
Protein Classification
methionyl-tRNA formyltransferase( domain architecture ID 11415469)
methionyl-tRNA formyltransferase catalyzes formylation of the initiator methionyl-tRNA
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| Fmt | COG0223 | Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis]; |
4-311 | 5.02e-135 | |||||
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis]; : Pssm-ID: 439993 [Multi-domain] Cd Length: 308 Bit Score: 385.23 E-value: 5.02e-135
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| Name | Accession | Description | Interval | E-value | ||||||
| Fmt | COG0223 | Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis]; |
4-311 | 5.02e-135 | ||||||
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis]; Pssm-ID: 439993 [Multi-domain] Cd Length: 308 Bit Score: 385.23 E-value: 5.02e-135
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| FMT_core_Met-tRNA-FMT_N | cd08646 | Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ... |
4-205 | 1.64e-97 | ||||||
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA formyltransferase (Met-tRNA-FMT), N-terminal formyltransferase domain. Met-tRNA-FMT transfers a formyl group from N-10 formyltetrahydrofolate to the amino terminal end of a methionyl-aminoacyl-tRNA acyl moiety, yielding formyl-Met-tRNA. Formyl-Met-tRNA plays essential role in protein translation initiation by forming complex with IF2. The formyl group plays a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and by impairing its binding to EFTU-GTP. The N-terminal domain contains a Rossmann fold and it is the catalytic domain of the enzyme. Pssm-ID: 187715 [Multi-domain] Cd Length: 204 Bit Score: 285.88 E-value: 1.64e-97
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| fmt | TIGR00460 | methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ... |
4-308 | 3.17e-87 | ||||||
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than methionyl-tRNA formyltransferase (fmt) itself are formyltetrahydrofolate dehydrogenases. The mitochondrial methionyl-tRNA formyltransferases are so divergent that, in a multiple alignment of bacterial fmt, mitochondrial fmt, and formyltetrahydrofolate dehydrogenases, the mitochondrial fmt appears the most different. However, because both bacterial and mitochondrial fmt are included in the seed alignment, all credible fmt sequences score higher than any non-fmt sequence. This enzyme modifies Met on initiator tRNA to f-Met. [Protein synthesis, tRNA aminoacylation] Pssm-ID: 273088 [Multi-domain] Cd Length: 313 Bit Score: 263.88 E-value: 3.17e-87
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| PLN02285 | PLN02285 | methionyl-tRNA formyltransferase |
4-300 | 8.73e-67 | ||||||
methionyl-tRNA formyltransferase Pssm-ID: 215159 [Multi-domain] Cd Length: 334 Bit Score: 212.25 E-value: 8.73e-67
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| Formyl_trans_N | pfam00551 | Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ... |
4-181 | 2.63e-36 | ||||||
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide transformylase catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyltetrahydrofolate deformylase produces formate from formyl- tetrahydrofolate. Methionyl-tRNA formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA. Inclusion of the following members is supported by PSI-blast. HOXX_BRAJA (P31907) contains a related domain of unknown function. PRTH_PORGI (P46071) contains a related domain of unknown function. Y09P_MYCTU (Q50721) contains a related domain of unknown function. Pssm-ID: 395436 [Multi-domain] Cd Length: 181 Bit Score: 128.56 E-value: 2.63e-36
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| Name | Accession | Description | Interval | E-value | ||||||
| Fmt | COG0223 | Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis]; |
4-311 | 5.02e-135 | ||||||
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis]; Pssm-ID: 439993 [Multi-domain] Cd Length: 308 Bit Score: 385.23 E-value: 5.02e-135
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| FMT_core_Met-tRNA-FMT_N | cd08646 | Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ... |
4-205 | 1.64e-97 | ||||||
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA formyltransferase (Met-tRNA-FMT), N-terminal formyltransferase domain. Met-tRNA-FMT transfers a formyl group from N-10 formyltetrahydrofolate to the amino terminal end of a methionyl-aminoacyl-tRNA acyl moiety, yielding formyl-Met-tRNA. Formyl-Met-tRNA plays essential role in protein translation initiation by forming complex with IF2. The formyl group plays a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and by impairing its binding to EFTU-GTP. The N-terminal domain contains a Rossmann fold and it is the catalytic domain of the enzyme. Pssm-ID: 187715 [Multi-domain] Cd Length: 204 Bit Score: 285.88 E-value: 1.64e-97
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| fmt | TIGR00460 | methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ... |
4-308 | 3.17e-87 | ||||||
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than methionyl-tRNA formyltransferase (fmt) itself are formyltetrahydrofolate dehydrogenases. The mitochondrial methionyl-tRNA formyltransferases are so divergent that, in a multiple alignment of bacterial fmt, mitochondrial fmt, and formyltetrahydrofolate dehydrogenases, the mitochondrial fmt appears the most different. However, because both bacterial and mitochondrial fmt are included in the seed alignment, all credible fmt sequences score higher than any non-fmt sequence. This enzyme modifies Met on initiator tRNA to f-Met. [Protein synthesis, tRNA aminoacylation] Pssm-ID: 273088 [Multi-domain] Cd Length: 313 Bit Score: 263.88 E-value: 3.17e-87
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| PLN02285 | PLN02285 | methionyl-tRNA formyltransferase |
4-300 | 8.73e-67 | ||||||
methionyl-tRNA formyltransferase Pssm-ID: 215159 [Multi-domain] Cd Length: 334 Bit Score: 212.25 E-value: 8.73e-67
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| PRK08125 | PRK08125 | bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ... |
1-287 | 1.46e-50 | ||||||
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ArnA; Pssm-ID: 236156 [Multi-domain] Cd Length: 660 Bit Score: 177.10 E-value: 1.46e-50
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| FMT_core_ArnA_N | cd08644 | ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ... |
3-197 | 1.06e-44 | ||||||
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for the modification of lipid A with 4-amino-4-deoxy-L-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. The C-terminal dehydrogenase domain of ArnA catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O), while the N-terminal formyltransferase domain of ArnA catalyzes the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). This domain family represents the catalytic core of the N-terminal formyltransferase domain. The formyltransferase also contains a smaller C-terminal domain the may be involved in substrate binding. ArnA forms a hexameric structure, in which the dehydrogenase domains are arranged at the center of the particle with the transformylase domains on the outside of the particle. Pssm-ID: 187713 [Multi-domain] Cd Length: 203 Bit Score: 150.96 E-value: 1.06e-44
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| PRK06988 | PRK06988 | formyltransferase; |
17-297 | 2.73e-42 | ||||||
formyltransferase; Pssm-ID: 235902 [Multi-domain] Cd Length: 312 Bit Score: 148.30 E-value: 2.73e-42
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| FMT_core | cd08369 | Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ... |
4-183 | 8.04e-42 | ||||||
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The proteins of this superfamily contain a formyltransferase domain that hydrolyzes the removal of a formyl group from its substrate as part of a multistep transfer mechanism, and this alignment model represents the catalytic core of the formyltransferase domain. This family includes the following known members; Glycinamide Ribonucleotide Transformylase (GART), Formyl-FH4 Hydrolase, Methionyl-tRNA Formyltransferase, ArnA, and 10-Formyltetrahydrofolate Dehydrogenase (FDH). Glycinamide Ribonucleotide Transformylase (GART) catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyl-FH4 Hydrolase catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate. Methionyl-tRNA Formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA, which plays important role in translation initiation. ArnA is required for the modification of lipid A with 4-amino-4-deoxy-l-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. 10-formyltetrahydrofolate dehydrogenase (FDH) catalyzes the conversion of 10-formyltetrahydrofolate, a precursor for nucleotide biosynthesis, to tetrahydrofolate. Members of this family are multidomain proteins. The formyltransferase domain is located at the N-terminus of FDH, Methionyl-tRNA Formyltransferase and ArnA, and at the C-terminus of Formyl-FH4 Hydrolase. Prokaryotic Glycinamide Ribonucleotide Transformylase (GART) is a single domain protein while eukaryotic GART is a trifunctional protein that catalyzes the second, third and fifth steps in de novo purine biosynthesis. Pssm-ID: 187712 [Multi-domain] Cd Length: 173 Bit Score: 142.81 E-value: 8.04e-42
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| Formyl_trans_N | pfam00551 | Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ... |
4-181 | 2.63e-36 | ||||||
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide transformylase catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyltetrahydrofolate deformylase produces formate from formyl- tetrahydrofolate. Methionyl-tRNA formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA. Inclusion of the following members is supported by PSI-blast. HOXX_BRAJA (P31907) contains a related domain of unknown function. PRTH_PORGI (P46071) contains a related domain of unknown function. Y09P_MYCTU (Q50721) contains a related domain of unknown function. Pssm-ID: 395436 [Multi-domain] Cd Length: 181 Bit Score: 128.56 E-value: 2.63e-36
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| FMT_core_like_4 | cd08651 | Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
4-184 | 1.50e-25 | ||||||
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme. Pssm-ID: 187720 [Multi-domain] Cd Length: 180 Bit Score: 100.42 E-value: 1.50e-25
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| Formyl_trans_C | pfam02911 | Formyl transferase, C-terminal domain; |
204-302 | 4.08e-23 | ||||||
Formyl transferase, C-terminal domain; Pssm-ID: 460744 [Multi-domain] Cd Length: 99 Bit Score: 91.18 E-value: 4.08e-23
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| FMT_core_NRPS_like | cd08649 | N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ... |
18-184 | 8.35e-18 | ||||||
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins involved in the synthesis of Oxazolomycin; This family represents the N-terminal formyl transferase catalytic core domain present in a subgroup of non-ribosomal peptide synthetases. In Streptomyces albus a member of this family has been shown to be involved in the synthesis of oxazolomycin (OZM). OZM is a hybrid peptide-polyketide antibiotic and exhibits potent antitumor and antiviral activities. It is a multi-domain protein consisting of a formyl transferase domain, a Flavin-utilizing monoxygenase domain, a LuxE domain functioning as an acyl protein synthetase and a pp-binding domain, which may function as an acyl carrier. It shows sequence similarity with other peptide-polyketide biosynthesis proteins. Pssm-ID: 187718 [Multi-domain] Cd Length: 166 Bit Score: 79.22 E-value: 8.35e-18
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| Met_tRNA_FMT_C | cd08704 | C-terminal domain of Formyltransferase and other enzymes; C-terminal domain of formyl ... |
208-294 | 2.04e-17 | ||||||
C-terminal domain of Formyltransferase and other enzymes; C-terminal domain of formyl transferase and other proteins with diverse enzymatic activities. Proteins found in this family include methionyl-tRNA formyltransferase, ArnA, and 10-formyltetrahydrofolate dehydrogenase. Methionyl-tRNA formyltransferases constitute the majority of the family and also demonstrate greater sequence diversity. Although most proteins with formyltransferase activity contain the C-terminal domain, some formyltransferases ( for example, prokaryotic glycinamide ribonucleotide transformylase (GART)) only have the core catalytic domain, indicating that the C-terminal domain is not a requirement for catalytic activity and may be involved in substrate binding. For example, the C-terminal domain of methionyl-tRNA formyltransferase is involved in the tRNA binding. Pssm-ID: 187732 [Multi-domain] Cd Length: 87 Bit Score: 75.65 E-value: 2.04e-17
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| FMT_core_like_2 | cd08822 | Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
4-203 | 2.30e-16 | ||||||
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme. Pssm-ID: 187724 [Multi-domain] Cd Length: 192 Bit Score: 75.96 E-value: 2.30e-16
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| FMT_core_GART | cd08645 | Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ... |
72-184 | 7.03e-15 | ||||||
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); Phosphoribosylglycinamide formyltransferase, also known as GAR transformylase or GART, is an essential enzyme that catalyzes the third step in de novo purine biosynthesis. This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. In prokaryotes, GART is a single domain protein but in most eukaryotes it is the C-terminal portion of a large multifunctional protein which also contains GAR synthetase and aminoimidazole ribonucleotide synthetase activities. Pssm-ID: 187714 [Multi-domain] Cd Length: 183 Bit Score: 71.26 E-value: 7.03e-15
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| FMT_core_like_6 | cd08820 | Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
4-181 | 3.11e-14 | ||||||
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme. Pssm-ID: 187722 [Multi-domain] Cd Length: 173 Bit Score: 69.39 E-value: 3.11e-14
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| FMT_core_like_5 | cd08823 | Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
70-181 | 3.64e-14 | ||||||
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme. Pssm-ID: 187725 [Multi-domain] Cd Length: 177 Bit Score: 69.40 E-value: 3.64e-14
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| PurN | COG0299 | Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ... |
72-204 | 9.93e-14 | ||||||
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and metabolism]; Folate-dependent phosphoribosylglycinamide formyltransferase PurN is part of the Pathway/BioSystem: Purine biosynthesis Pssm-ID: 440068 [Multi-domain] Cd Length: 202 Bit Score: 68.52 E-value: 9.93e-14
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| FMT_core_like_1 | cd08821 | Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
53-242 | 6.07e-13 | ||||||
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme. Pssm-ID: 187723 [Multi-domain] Cd Length: 211 Bit Score: 66.57 E-value: 6.07e-13
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| FMT_core_FDH_N | cd08647 | 10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ... |
7-168 | 9.63e-12 | ||||||
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family represents the N-terminal hydrolase domain of the bifunctional protein 10-formyltetrahydrofolate dehydrogenase (FDH). This domain contains a 10-formyl-tetrahydrofolate (10-formyl-THF) binding site and shares sequence homology and structural topology with other enzymes utilizing this substrate. This domain functions as a hydrolase, catalyzing the conversion of 10-formyl-THF, a precursor for nucleotide biosynthesis, to tetrahydrofolate (THF). The overall FDH reaction mechanism is a coupling of two sequential reactions, a hydrolase and a formyl dehydrogenase, bridged by a substrate transfer step. The N-terminal hydrolase domain removes the formyl group from 10-formyl-THF and the C-terminal NADP-dependent dehydrogenase domain then reduces the formyl group to carbon dioxide. The two catalytic domains are connected by a third intermediate linker domain that transfers the formyl group, covalently attached to the sulfhydryl group of the phosphopantetheine arm, from the N-terminal domain to the C-terminal domain. Pssm-ID: 187716 [Multi-domain] Cd Length: 203 Bit Score: 63.24 E-value: 9.63e-12
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| PurN | TIGR00639 | phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ... |
17-181 | 1.04e-11 | ||||||
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model describes phosphoribosylglycinamide formyltransferase (GAR transformylase), one of several proteins in formyl_transf (pfam00551). This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. PurT, a different GAR transformylase, uses ATP and formate rather than formyl tetrahydrofolate. Experimental proof includes complementation of E. coli purN mutants by orthologs from vertebrates (where it is a domain of a multifunctional protein), Bacillus subtilis, and Arabidopsis. No archaeal example was detected. In phylogenetic analyses, the member from Saccharomyces cerevisiae shows a long branch length but membership in the family, while the formyltetrahydrofolate deformylases form a closely related outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis] Pssm-ID: 161973 [Multi-domain] Cd Length: 190 Bit Score: 62.77 E-value: 1.04e-11
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| FMT_core_like_3 | cd08653 | Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
78-181 | 1.18e-11 | ||||||
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme. Pssm-ID: 187721 [Multi-domain] Cd Length: 152 Bit Score: 61.84 E-value: 1.18e-11
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| PRK07579 | PRK07579 | dTDP-4-amino-4,6-dideoxyglucose formyltransferase; |
66-228 | 1.53e-11 | ||||||
dTDP-4-amino-4,6-dideoxyglucose formyltransferase; Pssm-ID: 236058 [Multi-domain] Cd Length: 245 Bit Score: 63.38 E-value: 1.53e-11
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| Arna_FMT_C | cd08702 | C-terminal subdomain of the formyltransferase domain on ArnA, which modifies lipid A with ... |
210-297 | 3.40e-08 | ||||||
C-terminal subdomain of the formyltransferase domain on ArnA, which modifies lipid A with 4-amino-4-deoxy-l-arabinose; Domain found in ArnA with similarity to the C-terminal domain of Formyltransferase. ArnA is a bifunctional enzyme required for the modification of lipid A with 4-amino-4-deoxy-l-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. The C-terminal domain of ArnA is a dehydrogenase domain that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the N-terminal domain is a formyltransferase domain that catalyzes the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). This domain family represents the C-terminal subdomain of the formyltransferase domain, downstream of the N-terminal subdomain containing the catalytic center. ArnA forms a hexameric structure (a dimer of trimers), in which the dehydrogenase domains are arranged at the center with the transformylase domains on the outside of the complex. Pssm-ID: 187730 Cd Length: 92 Bit Score: 50.32 E-value: 3.40e-08
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| PLN02828 | PLN02828 | formyltetrahydrofolate deformylase |
61-161 | 1.08e-07 | ||||||
formyltetrahydrofolate deformylase Pssm-ID: 178422 Cd Length: 268 Bit Score: 52.06 E-value: 1.08e-07
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| FMT_core_Formyl-FH4-Hydrolase_C | cd08648 | Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ... |
67-176 | 5.44e-07 | ||||||
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; Formyl-FH4 Hydrolase catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate. Formate is the substrate of phosphoribosylglycinamide transformylase for step three of de novo purine nucleotide synthesis. Formyl-FH4 hydrolase has been proposed to regulate the balance of FH4 and C1-FH4 in the cell. The enzyme uses methionine and glycine to sense the pools of C1-FH4 and FH4, respectively. This domain belongs to the formyltransferase (FMT) domain superfamily. Members of this family have an N-terminal ACT domain, which is commonly involved in specifically bind an amino acid or other small ligand leading to regulation of the enzyme. The N-terminal of this protein family may be responsible for the binding of the regulators methionine and glycine. Pssm-ID: 187717 [Multi-domain] Cd Length: 196 Bit Score: 49.10 E-value: 5.44e-07
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| PLN02331 | PLN02331 | phosphoribosylglycinamide formyltransferase |
66-161 | 2.28e-05 | ||||||
phosphoribosylglycinamide formyltransferase Pssm-ID: 177965 [Multi-domain] Cd Length: 207 Bit Score: 44.68 E-value: 2.28e-05
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| FMT_core_HypX_N | cd08650 | HypX protein, N-terminal hydrolase domain; The family represents the N-terminal hydrolase ... |
116-166 | 6.40e-05 | ||||||
HypX protein, N-terminal hydrolase domain; The family represents the N-terminal hydrolase domain of HypX protein. HypX is involved in the maturation process of active [NiFe] hydrogenase. [NiFe] hydrogenases function in H2 metabolism in a variety of microorganisms, enabling them to use H2 as a source of reducing equivalent under aerobic and anaerobic conditions. [NiFe] hydrogenases consist of a large and a small subunit. The large subunit contains [NiFe] active site, which is synthesized as a precursor without the [NiFe] active site. This precursor then undergoes a complex post-translational maturation process that requires the presence of a number of accessory proteins. HypX has been shown to be involved in this maturation process and have been proposed to participate in the generation and transport of the CO and CN ligands. However, HypX is not present in all hydrogen-metabolizing bacteria. Furthermore, hypX deletion mutants have a reduced but detectable level of hydrogenase activity. Thus, HypX might not be a determining factor in the matur ation process. Members of this group have an N-terminal formyl transferase domain and a C-terminal enoyl-CoA hydratase/isomerase domain. Pssm-ID: 187719 [Multi-domain] Cd Length: 151 Bit Score: 42.22 E-value: 6.40e-05
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| purU | PRK13010 | formyltetrahydrofolate deformylase; Reviewed |
81-176 | 9.96e-04 | ||||||
formyltetrahydrofolate deformylase; Reviewed Pssm-ID: 139334 [Multi-domain] Cd Length: 289 Bit Score: 40.16 E-value: 9.96e-04
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