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Conserved domains on  [gi|1731189529|ref|WP_148444677|]
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MULTISPECIES: phosphoribosylglycinamide formyltransferase [Limosilactobacillus]

Protein Classification

phosphoribosylglycinamide formyltransferase( domain architecture ID 10171287)

phosphoribosylglycinamide formyltransferase catalyzes the transfer of a formyl group from lO-formyltetrahydrofolate to glycinamide ribonucleotide

CATH:  3.40.50.170
EC:  2.1.2.2
Gene Ontology:  GO:0004644|GO:0006189
SCOP:  4000065

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 2-184 9.86e-99

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: 283.12  E-value: 9.86e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529   2 RVAIFASGNGTNFEVLAKHFQSGDIPGELSLLFCNHPDAPVMKRAQRLGVPAESFTVKSCGGKEEYEKQLLQLLKKYQID 81
Cdd:cd08645     1 RIAVLASGSGSNLQALIDAIKSGKLNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKVD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529  82 FIALAGYLRVVGPTILNQYEHRIVNLHPAWLPEYPGLHSIERAFNDRRKQTGVTVHYIDAGLDSGPIIAQRHVPILPSDT 161
Cdd:cd08645    81 LIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDT 160

                         170       180
                  ....*....|....*....|...
gi 1731189529 162 VETLEERVHETEHQLYPAAVKQV 184
Cdd:cd08645   161 PETLAERIHALEHRLYPEAIKLL 183
 
Name Accession Description Interval E-value
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 2-184 9.86e-99

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: 283.12  E-value: 9.86e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529   2 RVAIFASGNGTNFEVLAKHFQSGDIPGELSLLFCNHPDAPVMKRAQRLGVPAESFTVKSCGGKEEYEKQLLQLLKKYQID 81
Cdd:cd08645     1 RIAVLASGSGSNLQALIDAIKSGKLNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKVD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529  82 FIALAGYLRVVGPTILNQYEHRIVNLHPAWLPEYPGLHSIERAFNDRRKQTGVTVHYIDAGLDSGPIIAQRHVPILPSDT 161
Cdd:cd08645    81 LIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDT 160

                         170       180
                  ....*....|....*....|...
gi 1731189529 162 VETLEERVHETEHQLYPAAVKQV 184
Cdd:cd08645   161 PETLAERIHALEHRLYPEAIKLL 183
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 1-187 5.65e-93

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: 269.21  E-value: 5.65e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529   1 MRVAIFASGNGTNFEVLAKHFQSGDIPGELSLLFCNHPDAPVMKRAQRLGVPAESFTVKSCGGKEEYEKQLLQLLKKYQI 80
Cdd:COG0299     2 KRIAVLISGRGSNLQALIDAIEAGDLPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYGP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529  81 DFIALAGYLRVVGPTILNQYEHRIVNLHPAWLPEYPGLHSIERAFNDRRKQTGVTVHYIDAGLDSGPIIAQRHVPILPSD 160
Cdd:COG0299    82 DLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDD 161

                         170       180
                  ....*....|....*....|....*..
gi 1731189529 161 TVETLEERVHETEHQLYPAAVKQVLTE 187
Cdd:COG0299   162 TEETLAARILEQEHRLYPEAIRLLAEG 188
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 1-190 4.68e-70

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: 211.08  E-value: 4.68e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529   1 MRVAIFASGNGTNFEVLAKHFQSGDIPGELSLLFCNHPDAPVMKRAQRLGVPAESFTVKSCGGKEEYEKQLLQLLKKYQI 80
Cdd:TIGR00639   1 KRIVVLISGNGSNLQAIIDACKEGKIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529  81 DFIALAGYLRVVGPTILNQYEHRIVNLHPAWLPEYPGLHSIERAFNDRRKQTGVTVHYIDAGLDSGPIIAQRHVPILPSD 160
Cdd:TIGR00639  81 DLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPED 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1731189529 161 TVETLEERVHETEHQLYPAAVKQVLTELEK 190
Cdd:TIGR00639 161 TEETLEQRIHKQEHRIYPLAIAWFAQGRLK 190
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 1-181 1.59e-57

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: 179.02  E-value: 1.59e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529   1 MRVAIFASGNGTNFEVLAKHFQSGDIPGELSLLFCNHPDAPVMKRAQRLGVPAESFTVKSCGGKEEYEKQLLQLLKKYQI 80
Cdd:pfam00551   1 MKIAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529  81 DFIALAGYLRVVGPTILNQYEHRIVNLHPAWLPEYPGLHSIERAFNDRRKQTGVTVHYIDAGLDSGPIIAQRHVPILPSD 160
Cdd:pfam00551  81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160

                         170       180
                  ....*....|....*....|.
gi 1731189529 161 TVETLEERVHETEHQLYPAAV 181
Cdd:pfam00551 161 TAETLYNRVADLEHKALPRVL 181
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 2-181 6.93e-40

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 134.82  E-value: 6.93e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529   2 RVAIFASGNGTNFEVLAKHFQSGDIPGELSLLFCNHPDAPVMKRAQRLGVPAESFTVKSCGGKEEYEKQLLQLLKKYQID 81
Cdd:PLN02331    1 KLAVFVSGGGSNFRAIHDACLDGRVNGDVVVVVTNKPGCGGAEYARENGIPVLVYPKTKGEPDGLSPDELVDALRGAGVD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529  82 FIALAGYLRVVGPTILNQYEHRIVNLHPAWLPE-----YPGLHSIERAFNDRRKQTGVTVHYIDAGLDSGPIIAQRHVPI 156
Cdd:PLN02331   81 FVLLAGYLKLIPVELVRAYPRSILNIHPALLPAfggkgYYGIKVHKAVIASGARYSGPTVHFVDEHYDTGRILAQRVVPV 160

                         170       180
                  ....*....|....*....|....*
gi 1731189529 157 LPSDTVETLEERVHETEHQLYPAAV 181
Cdd:PLN02331  161 LATDTPEELAARVLHEEHQLYVEVV 185
 
Name Accession Description Interval E-value
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 2-184 9.86e-99

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: 283.12  E-value: 9.86e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529   2 RVAIFASGNGTNFEVLAKHFQSGDIPGELSLLFCNHPDAPVMKRAQRLGVPAESFTVKSCGGKEEYEKQLLQLLKKYQID 81
Cdd:cd08645     1 RIAVLASGSGSNLQALIDAIKSGKLNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKVD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529  82 FIALAGYLRVVGPTILNQYEHRIVNLHPAWLPEYPGLHSIERAFNDRRKQTGVTVHYIDAGLDSGPIIAQRHVPILPSDT 161
Cdd:cd08645    81 LIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDT 160

                         170       180
                  ....*....|....*....|...
gi 1731189529 162 VETLEERVHETEHQLYPAAVKQV 184
Cdd:cd08645   161 PETLAERIHALEHRLYPEAIKLL 183
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 1-187 5.65e-93

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: 269.21  E-value: 5.65e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529   1 MRVAIFASGNGTNFEVLAKHFQSGDIPGELSLLFCNHPDAPVMKRAQRLGVPAESFTVKSCGGKEEYEKQLLQLLKKYQI 80
Cdd:COG0299     2 KRIAVLISGRGSNLQALIDAIEAGDLPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYGP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529  81 DFIALAGYLRVVGPTILNQYEHRIVNLHPAWLPEYPGLHSIERAFNDRRKQTGVTVHYIDAGLDSGPIIAQRHVPILPSD 160
Cdd:COG0299    82 DLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDD 161

                         170       180
                  ....*....|....*....|....*..
gi 1731189529 161 TVETLEERVHETEHQLYPAAVKQVLTE 187
Cdd:COG0299   162 TEETLAARILEQEHRLYPEAIRLLAEG 188
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 1-190 4.68e-70

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: 211.08  E-value: 4.68e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529   1 MRVAIFASGNGTNFEVLAKHFQSGDIPGELSLLFCNHPDAPVMKRAQRLGVPAESFTVKSCGGKEEYEKQLLQLLKKYQI 80
Cdd:TIGR00639   1 KRIVVLISGNGSNLQAIIDACKEGKIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529  81 DFIALAGYLRVVGPTILNQYEHRIVNLHPAWLPEYPGLHSIERAFNDRRKQTGVTVHYIDAGLDSGPIIAQRHVPILPSD 160
Cdd:TIGR00639  81 DLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPED 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1731189529 161 TVETLEERVHETEHQLYPAAVKQVLTELEK 190
Cdd:TIGR00639 161 TEETLEQRIHKQEHRIYPLAIAWFAQGRLK 190
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 1-181 1.59e-57

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: 179.02  E-value: 1.59e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529   1 MRVAIFASGNGTNFEVLAKHFQSGDIPGELSLLFCNHPDAPVMKRAQRLGVPAESFTVKSCGGKEEYEKQLLQLLKKYQI 80
Cdd:pfam00551   1 MKIAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529  81 DFIALAGYLRVVGPTILNQYEHRIVNLHPAWLPEYPGLHSIERAFNDRRKQTGVTVHYIDAGLDSGPIIAQRHVPILPSD 160
Cdd:pfam00551  81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160

                         170       180
                  ....*....|....*....|.
gi 1731189529 161 TVETLEERVHETEHQLYPAAV 181
Cdd:pfam00551 161 TAETLYNRVADLEHKALPRVL 181
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 2-181 6.93e-40

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 134.82  E-value: 6.93e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529   2 RVAIFASGNGTNFEVLAKHFQSGDIPGELSLLFCNHPDAPVMKRAQRLGVPAESFTVKSCGGKEEYEKQLLQLLKKYQID 81
Cdd:PLN02331    1 KLAVFVSGGGSNFRAIHDACLDGRVNGDVVVVVTNKPGCGGAEYARENGIPVLVYPKTKGEPDGLSPDELVDALRGAGVD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529  82 FIALAGYLRVVGPTILNQYEHRIVNLHPAWLPE-----YPGLHSIERAFNDRRKQTGVTVHYIDAGLDSGPIIAQRHVPI 156
Cdd:PLN02331   81 FVLLAGYLKLIPVELVRAYPRSILNIHPALLPAfggkgYYGIKVHKAVIASGARYSGPTVHFVDEHYDTGRILAQRVVPV 160

                         170       180
                  ....*....|....*....|....*
gi 1731189529 157 LPSDTVETLEERVHETEHQLYPAAV 181
Cdd:PLN02331  161 LATDTPEELAARVLHEEHQLYVEVV 185
FMT_core cd08369
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...
 36-183 9.47e-36

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: 123.17  E-value: 9.47e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529  36 NHPDAPVmKRAQRLGVPAESFTVKScggKEEYEKQLLQLLKKYQIDFIALAGYLRVVGPTILNQYEHRIVNLHPAWLPEY 115
Cdd:cd08369    30 THPDSPR-GTAQLSLELVGGKVYLD---SNINTPELLELLKEFAPDLIVSINFRQIIPPEILKLPPGGAINIHPSLLPRY 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1731189529 116 PGLHSIERAFNDRRKQTGVTVHYIDAGLDSGPIIAQRHVPILPSDTVETLEERVHETEHQLYPAAVKQ 183
Cdd:cd08369   106 RGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTAGTLYQRLIELGPKLLKEALQK 173
FMT_core_Formyl-FH4-Hydrolase_C cd08648
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ...
 1-185 6.55e-35

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: 121.52  E-value: 6.55e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529   1 MRVAIFASGNGTNFEVLAKHFQSGDIPGELSLLFCNHPDApvMKRAQRLGVPAESFTVkSCGGKEEYEKQLLQLLKKYQI 80
Cdd:cd08648     1 KRVAIFVSKEDHCLYDLLHRWREGELPCEIPLVISNHPDL--RPLAERFGIPFHHIPV-TKDTKAEAEAEQLELLEEYGV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529  81 DFIALAGYLRVVGPTILNQYEHRIVNLHPAWLPEYPGLHSIERAFNDRRKQTGVTVHYIDAGLDSGPIIAQRHVPILPSD 160
Cdd:cd08648    78 DLVVLARYMQILSPDFVERYPNRIINIHHSFLPAFKGAKPYHQAFERGVKLIGATAHYVTEELDEGPIIEQDVERVSHRD 157

                         170       180
                  ....*....|....*....|....*
gi 1731189529 161 TVETLEERVHETEHQLYPAAVKQVL 185
Cdd:cd08648   158 SVEDLVRKGRDIEKQVLARAVKWHL 182
PurU COG0788
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ...
 1-165 8.74e-29

Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate hydrolase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440551 [Multi-domain]  Cd Length: 282  Bit Score: 107.83  E-value: 8.74e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529   1 MRVAIFASgngtNF-----EVLAKHfQSGDIPGELSLLFCNHPD-APVmkrAQRLGVPAESFTVKScGGKEEYEKQLLQL 74
Cdd:COG0788    87 KRVAILVS----KEdhclnDLLYRW-RSGELPAEIPAVISNHPDlRPL---AEWFGIPFHHIPVTK-ETKAEAEARLLEL 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529  75 LKKYQIDFIALAGYLRVVGPTILNQYEHRIVNLHPAWLPEYPGLHSIERAFnDRR-KQTGVTVHYIDAGLDSGPIIAQRH 153
Cdd:COG0788   158 LEEYDIDLVVLARYMQILSPDFCARLPGRIINIHHSFLPAFKGAKPYHQAY-ERGvKLIGATAHYVTADLDEGPIIEQDV 236

                         170
                  ....*....|..
gi 1731189529 154 VPILPSDTVETL 165
Cdd:COG0788   237 ERVDHRDTPEDL 248
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
41-190 1.42e-27

Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 105.19  E-value: 1.42e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529  41 PVMKRAQRLGVPAesFTVKSCGGKEEYEKqllqlLKKYQIDFIALAGYLRVVGPTILNQYEHRIVNLHPAWLPEYPGLHS 120
Cdd:COG0223    47 PVKELALEHGIPV--LQPESLKDPEFLEE-----LRALNPDLIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAAP 119

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529 121 IERAFNDRRKQTGVTVHYIDAGLDSGPIIAQRHVPILPSDTVETLEERVHEtehqLYPAAVKQVLTELEK 190
Cdd:COG0223   120 IQWAILNGDTETGVTIMQMDEGLDTGDILLQEEVPIGPDDTAGSLHDKLAE----LGAELLLETLDALEA 185
FMT_core_Met-tRNA-FMT_N cd08646
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ...
 41-168 4.59e-23

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: 90.97  E-value: 4.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529  41 PVMKRAQRLGVPAesFTVKSCGGKEEYEkqllqLLKKYQIDFIALAGYLRVVGPTILNQYEHRIVNLHPAWLPEYPGLHS 120
Cdd:cd08646    47 PVKELALELGLPV--LQPEKLKDEEFLE-----ELKALKPDLIVVVAYGQILPKEILDLPPYGCINVHPSLLPKYRGAAP 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1731189529 121 IERAFNDRRKQTGVTVHYIDAGLDSGPIIAQRHVPILPSDTVETLEER 168
Cdd:cd08646   120 IQRAILNGDKETGVTIMKMDEGLDTGDILAQEEVPIDPDDTAGELLDK 167
purU PRK06027
formyltetrahydrofolate deformylase; Reviewed
 1-165 1.66e-20

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 235676 [Multi-domain]  Cd Length: 286  Bit Score: 85.93  E-value: 1.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529   1 MRVAIFAS--GNGTNfEVLAKHfQSGDIPGELSLLFCNHPD-APVmkrAQRLGVPAESFTVkSCGGKEEYEKQLLQLLKK 77
Cdd:PRK06027   90 KRVVILVSkeDHCLG-DLLWRW-RSGELPVEIAAVISNHDDlRSL---VERFGIPFHHVPV-TKETKAEAEARLLELIDE 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529  78 YQIDFIALAGYLRVVGPTILNQYEHRIVNLHPAWLPEYPGLHSIERAFnDRR-KQTGVTVHYIDAGLDSGPIIAQRHVPI 156
Cdd:PRK06027  164 YQPDLVVLARYMQILSPDFVARFPGRIINIHHSFLPAFKGAKPYHQAY-ERGvKLIGATAHYVTADLDEGPIIEQDVIRV 242


                  ....*....
gi 1731189529 157 LPSDTVETL 165
Cdd:PRK06027  243 DHRDTAEDL 251
PLN02828 PLN02828
formyltetrahydrofolate deformylase
 1-182 1.37e-18

formyltetrahydrofolate deformylase


Pssm-ID: 178422  Cd Length: 268  Bit Score: 80.56  E-value: 1.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529   1 MRVAIFASGNGTNFEVLAKHFQSGDIPGELSLLFCNH---PDAPVMKRAQRLGVPAEsFTVKSCGGKEEYEkqLLQLLKK 77
Cdd:PLN02828   71 YKIAVLASKQDHCLIDLLHRWQDGRLPVDITCVISNHergPNTHVMRFLERHGIPYH-YLPTTKENKREDE--ILELVKG 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529  78 yqIDFIALAGYLRVVGPTILNQYEHRIVNLHPAWLPEYPGLHSIERAFNDRRKQTGVTVHYIDAGLDSGPIIAQRHVPIL 157
Cdd:PLN02828  148 --TDFLVLARYMQILSGNFLKGYGKDIINIHHGLLPSFKGGNPSKQAFDAGVKLIGATSHFVTEELDAGPIIEQMVERVS 225

                         170       180
                  ....*....|....*....|....*
gi 1731189529 158 PSDTVETLEERVHETEHQLYPAAVK 182
Cdd:PLN02828  226 HRDNLRSFVQKSENLEKQCLAKAIK 250
FMT_core_like_4 cd08651
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 69-188 4.75e-18

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: 77.31  E-value: 4.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529  69 KQLLQLLKKYQIDFIALAGYLRVVGPTILNQYEHRIVNLHPAWLPEYPGLHSIERAFNDRRKQTGVTVHYIDAGLDSGPI 148
Cdd:cd08651    65 EEIIEWIKEANPDIIFVFGWSQLLKPEILAIPRLGVIGFHPTKLPKNRGRAPIPWAILLGLKETASTFFWMDEGADSGDI 144

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1731189529 149 IAQRHVPILPSDTVETLEERVHETEHQLypaaVKQVLTEL 188
Cdd:cd08651   145 LSQEPFPIDKDDTANSLYDKIMEAAKQQ----IDKFLPRL 180
FMT_core_like_3 cd08653
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 72-184 2.06e-17

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: 74.94  E-value: 2.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529  72 LQLLKKYQIDFIALAGyLRVVGPTILNQYEHRIVNLHPAWLPEYPGLHSIERAF-NDRRKQTGVTVHYIDAGLDSGPIIA 150
Cdd:cd08653    40 VAALRALAPDVVSVYG-CGIIKDALLAIPPLGVLNLHGGILPDYRGVHTGFWALaNGDPDNVGVTVHLVDAGIDTGDVLA 118

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1731189529 151 QRHVPILPSDTVETLEERVHETEHQLYPAAVKQV 184
Cdd:cd08653   119 QARPPLAAGDTLLSLYLRLYRAGVELMVEAIADL 152
FMT_core_like_5 cd08823
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 69-169 2.14e-17

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: 75.56  E-value: 2.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529  69 KQLLQLLKKYQIDFIALAGYLRVVGPTILNQYEHRIVNLHPAWLPEYPGLHSIERAFNDRRKQTGVTVHYIDAGLDSGPI 148
Cdd:cd08823    61 EQLAEWLRALAADTVVVFTFPYRIPQHILDLPPLGFYNLHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMTAEIDRGPI 140

                          90       100
                  ....*....|....*....|.
gi 1731189529 149 IAQRHVPILPSDTVETLEERV 169
Cdd:cd08823   141 VLEQFTPIHPDDTYGLLCSRL 161
fmt TIGR00460
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ...
 41-185 2.22e-16

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: 75.13  E-value: 2.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529  41 PVMKRAQRLGVPAESFTVKScggkeeyEKQLLQLLKKYQIDFIALAGYLRVVGPTILNQYEHRIVNLHPAWLPEYPGLHS 120
Cdd:TIGR00460  47 PVKVLAEEKGIPVFQPEKQR-------QLEELPLVRELKPDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAP 119

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1731189529 121 IERAFNDRRKQTGVTVHYIDAGLDSGPIIAQRHVPILPSDTVETLEERVHETEHQLYPAAVKQVL 185
Cdd:TIGR00460 120 IQRAILNGDKKTGVTIMQMVPKMDAGDILKQETFPIEEEDNSGTLSDKLSELGAQLLIETLKELP 184
PRK13011 PRK13011
formyltetrahydrofolate deformylase; Reviewed
 25-165 1.03e-15

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 237266 [Multi-domain]  Cd Length: 286  Bit Score: 73.09  E-value: 1.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529  25 DIPGELSllfcNHPDapVMKRAQRLGVPAESFTVKScGGKEEYEKQLLQLLKKYQIDFIALAGYLRVVGPTILNQYEHRI 104
Cdd:PRK13011  118 DIVGVVS----NHPD--LEPLAAWHGIPFHHFPITP-DTKPQQEAQVLDVVEESGAELVVLARYMQVLSPELCRKLAGRA 190

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1731189529 105 VNLHPAWLPEYPGLHSIERAFNDRRKQTGVTVHYIDAGLDSGPIIAQRHVPILPSDTVETL 165
Cdd:PRK13011  191 INIHHSFLPGFKGAKPYHQAYERGVKLIGATAHYVTDDLDEGPIIEQDVERVDHAYSPEDL 251
purU PRK13010
formyltetrahydrofolate deformylase; Reviewed
 1-182 8.38e-15

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 139334 [Multi-domain]  Cd Length: 289  Bit Score: 70.59  E-value: 8.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529   1 MRVAIFASGNGTNFEVLAKHFQSGDIPGELSLLFCNHPDApvMKRAQRLGVPAESFTVKScGGKEEYEKQLLQLLKKYQI 80
Cdd:PRK13010   94 PKVVIMVSKFDHCLNDLLYRWRMGELDMDIVGIISNHPDL--QPLAVQHDIPFHHLPVTP-DTKAQQEAQILDLIETSGA 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529  81 DFIALAGYLRVVGPTILNQYEHRIVNLHPAWLPEYPGLHSIERAFNDRRKQTGVTVHYIDAGLDSGPIIAQRHVPILPSD 160
Cdd:PRK13010  171 ELVVLARYMQVLSDDLSRKLSGRAINIHHSFLPGFKGARPYHQAHARGVKLIGATAHFVTDDLDEGPIIEQDVERVDHSY 250

                         170       180
                  ....*....|....*....|..
gi 1731189529 161 TVETLEERVHETEHQLYPAAVK 182
Cdd:PRK13010  251 SPEDLVAKGRDVECLTLARAVK 272
FMT_core_like_6 cd08820
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 70-170 1.45e-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: 68.24  E-value: 1.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529  70 QLLQLLKKYQIDFIALAGYLRVVGPTILNQYEHRIVNLHPAWLPEYPGLHSIERAFNDRRKQTGVTVHYIDAGLDSGPII 149
Cdd:cd08820    60 KLLEILENKGVDILISVQYHWILPGSILEKAKEIAFNLHNAPLPEYRGCNQFSHAILNGDDQFGTTIHWMAEGIDSGDII 139

                          90       100
                  ....*....|....*....|.
gi 1731189529 150 AQRHVPILPSDTVETLEERVH 170
Cdd:cd08820   140 FEKRFPIPSDCTVISLYILAH 160
FMT_core_ArnA_N cd08644
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ...
 1-190 7.43e-14

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: 66.99  E-value: 7.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529   1 MRVAIFASGN----------GTNFEVLAKhFQSGDIPGElsllfcNHPDAPVMKRAQRLGVPAesFTVKSCGGKEEYEKq 70
Cdd:cd08644     1 MKAVVFAYHEvgyrcleallAAGFEVVAV-FTHTDNPGE------NIWFGSVAQLAREHGIPV--FTPDDINHPEWVER- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529  71 llqlLKKYQIDFIALAGYLRVVGPTILNQYEHRIVNLHPAWLPEYPGLHSIERAFNDRRKQTGVTVHYIDAGLDSGPIIA 150
Cdd:cd08644    71 ----LRALKPDLIFSFYYRHMISEDILEIARLGAFNLHGSLLPKYRGRAPLNWALINGETETGVTLHRMTKKPDAGAIVD 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1731189529 151 QRHVPILPSDTVETLEERVHETEHQLypaaVKQVLTELEK 190
Cdd:cd08644   147 QEKVPILPDDTAKSLFHKLCVAARRL----LARTLPALKA 182
PLN02285 PLN02285
methionyl-tRNA formyltransferase
 41-176 1.41e-13

methionyl-tRNA formyltransferase


Pssm-ID: 215159 [Multi-domain]  Cd Length: 334  Bit Score: 67.80  E-value: 1.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529  41 PVMKRAQRLGVPAESFTVKSCGGKEEYekqlLQLLKKYQIDFIALAGYLRVVGPTILNQYEHRIVNLHPAWLPEYPGLHS 120
Cdd:PLN02285   59 PVAQLALDRGFPPDLIFTPEKAGEEDF----LSALRELQPDLCITAAYGNILPQKFLDIPKLGTVNIHPSLLPLYRGAAP 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1731189529 121 IERAFNDRRKQTGVTVHYIDAGLDSGPIIAQRHVPILPSDTVETLEERVHETEHQL 176
Cdd:PLN02285  135 VQRALQDGVNETGVSVAFTVRALDAGPVIAQERVEVDEDIKAPELLPLLFELGTKL 190
FMT_core_like_2 cd08822
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 81-192 3.29e-12

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: 62.09  E-value: 3.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529  81 DFIALAGYLRVVGPTILNQYEHRIVNLHPAWLPEYPGLHSIERAFNDRRKQTGVTVHYIDAGLDSGPIIAQRHVPILPSD 160
Cdd:cd08822    68 DLIVAAHCHAFISAKTRARARLGAIGYHPSLLPRHRGRDAVEWTIRMRDPITGGTVYHLDDGVDGGPIAAQDWCHVRPGD 147

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1731189529 161 TVETLEERVhetehqLYPAAVK---QVLTELEKEN 192
Cdd:cd08822   148 TAAELWRRA------LAPMGVKlltQVIDALLRGG 176
FMT_core_NRPS_like cd08649
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ...
 66-165 1.67e-11

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: 59.58  E-value: 1.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529  66 EYEKQLLQLLKKYQIDFIALAGYLRVVGPTILNQYEHRIVNLHPAWLPEYPGLHSIERAFNDRRKQTGVTVHYIDAGLDS 145
Cdd:cd08649    48 EPGEALEELLSDEPFDWLFSIVNLRILPSEVLALPRKGAINFHDGPLPRYAGLNATSWALLAGETRHGVTWHRIEEGVDA 127

                          90       100
                  ....*....|....*....|
gi 1731189529 146 GPIIAQRHVPILPSDTVETL 165
Cdd:cd08649   128 GDILVQRPFDIAPDDTALSL 147
FMT_core_FDH_N cd08647
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ...
 96-189 3.13e-11

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: 59.77  E-value: 3.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529  96 ILNQYEHRIVNLHPAWLPEYPGLHSIERAFNDRRKQTGVTVHYIDAGLDSGPIIAQRHVPILPSDTVETLEERVhetehq 175
Cdd:cd08647    94 VIDAPKHGSIIYHPSILPRHRGASAINWTLIHGDKKAGFTIFWADDGLDTGPILLQKECDVLPNDTVDTLYNRF------ 167

                          90
                  ....*....|....
gi 1731189529 176 LYPAAVKQVLTELE 189
Cdd:cd08647   168 LYPEGIKAMVEAVR 181
PRK06988 PRK06988
formyltransferase;
1-169 1.44e-10

formyltransferase;


Pssm-ID: 235902 [Multi-domain]  Cd Length: 312  Bit Score: 58.94  E-value: 1.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529   1 MRVAIFASGNgTNFEVLAKHFQSGDipgELSLLFcNHPDAP--------VMKRAQRLGVPAesFTVKSCGGKEeyekqLL 72
Cdd:PRK06988    3 PRAVVFAYHN-VGVRCLQVLLARGV---DVALVV-THEDNPteniwfgsVAAVAAEHGIPV--ITPADPNDPE-----LR 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529  73 QLLKKYQIDFIALAGYLRVVGPTILNQYEHRIVNLHPAWLPEYPGLHSIERAFNDRRKQTGVTVHYIDAGLDSGPIIAQR 152
Cdd:PRK06988   71 AAVAAAAPDFIFSFYYRHMIPVDLLALAPRGAYNMHGSLLPKYRGRVPVNWAVLNGETETGATLHEMVAKPDAGAIVDQT 150

                         170
                  ....*....|....*..
gi 1731189529 153 HVPILPSDTVETLEERV 169
Cdd:PRK06988  151 AVPILPDDTAAQVFDKV 167
PRK08125 PRK08125
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ...
 75-176 1.24e-09

bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ArnA;


Pssm-ID: 236156 [Multi-domain]  Cd Length: 660  Bit Score: 56.53  E-value: 1.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731189529  75 LKKYQIDFIALAGYLRVVGPTILNQYEHRIVNLHPAWLPEYPGLHSIERAFNDRRKQTGVTVHYIDAGLDSGPIIAQRHV 154
Cdd:PRK08125   71 IRELAPDVIFSFYYRNLLSDEILQLAPAGAFNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQQRV 150

                          90       100
                  ....*....|....*....|..
gi 1731189529 155 PILPSDTVETLEERVHETEHQL 176
Cdd:PRK08125  151 AIAPDDTALTLHHKLCHAARQL 172
PRK07579 PRK07579
dTDP-4-amino-4,6-dideoxyglucose formyltransferase;
103-177 5.12e-08

dTDP-4-amino-4,6-dideoxyglucose formyltransferase;


Pssm-ID: 236058 [Multi-domain]  Cd Length: 245  Bit Score: 51.06  E-value: 5.12e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1731189529 103 RIVNLHPAWLPE----YPGLHSIeraFNDrrKQTGVTVHYIDAGLDSGPIIAQRHVPILPSDTVETLEERVHETEHQLY 177
Cdd:PRK07579   87 RCINIHPGFNPYnrgwFPQVFSI---ING--LKIGATIHEMDEQLDHGPIIAQREVEIESWDSSGSVYARVMDIERELV 160
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options: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.
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