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Conserved domains on  [gi|544678888|ref|WP_021111112|]
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phosphoribosylglycinamide formyltransferase [Glaesserella parasuis]

Protein Classification

phosphoribosylglycinamide formyltransferase( domain architecture ID 10001018)

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 Symbol:  purN
Gene Ontology:  GO:0006974|GO:0004644|GO:0006189
SCOP:  4000065

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 1-202 5.54e-115

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: 325.83  E-value: 5.54e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888   1 MKNIVVMISGNGSNLQAIIDAIDTGKINGRICAVISNKATAYGLERAKQAGISTFIFTKKDFSDNLEMDNAIAEQIEALQ 80
Cdd:COG0299    1 MKRIAVLISGRGSNLQALIDAIEAGDLPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888  81 ADLIVLAGYMKILTPEFTARFTGKILNIHPSLLPKYAGLNPHQRAMDAGDTEHGTTIHFVNEEVDGGAIILQAKVPIYPD 160
Cdd:COG0299   81 PDLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPD 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 544678888 161 DELDDVIERVYEQEHRCYPLVVQWFCDDRLKLIEGKAYLDNQ 202
Cdd:COG0299  161 DTEETLAARILEQEHRLYPEAIRLLAEGRLTLDGRRVRLDGE 202
 
Name Accession Description Interval E-value
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 1-202 5.54e-115

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: 325.83  E-value: 5.54e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888   1 MKNIVVMISGNGSNLQAIIDAIDTGKINGRICAVISNKATAYGLERAKQAGISTFIFTKKDFSDNLEMDNAIAEQIEALQ 80
Cdd:COG0299    1 MKRIAVLISGRGSNLQALIDAIEAGDLPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888  81 ADLIVLAGYMKILTPEFTARFTGKILNIHPSLLPKYAGLNPHQRAMDAGDTEHGTTIHFVNEEVDGGAIILQAKVPIYPD 160
Cdd:COG0299   81 PDLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPD 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 544678888 161 DELDDVIERVYEQEHRCYPLVVQWFCDDRLKLIEGKAYLDNQ 202
Cdd:COG0299  161 DTEETLAARILEQEHRLYPEAIRLLAEGRLTLDGRRVRLDGE 202
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 3-185 4.14e-103

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: 295.07  E-value: 4.14e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888   3 NIVVMISGNGSNLQAIIDAIDTGKINGRICAVISNKATAYGLERAKQAGISTFIFTKKDFSDNLEMDNAIAEQIEALQAD 82
Cdd:cd08645    1 RIAVLASGSGSNLQALIDAIKSGKLNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888  83 LIVLAGYMKILTPEFTARFTGKILNIHPSLLPKYAGLNPHQRAMDAGDTEHGTTIHFVNEEVDGGAIILQAKVPIYPDDE 162
Cdd:cd08645   81 LIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDT 160

                        170       180
                 ....*....|....*....|...
gi 544678888 163 LDDVIERVYEQEHRCYPLVVQWF 185
Cdd:cd08645  161 PETLAERIHALEHRLYPEAIKLL 183
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 2-191 2.38e-97

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: 281.18  E-value: 2.38e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888    2 KNIVVMISGNGSNLQAIIDAIDTGKINGRICAVISNKATAYGLERAKQAGISTFIFTKKDFSDNLEMDNAIAEQIEALQA 81
Cdd:TIGR00639   1 KRIVVLISGNGSNLQAIIDACKEGKIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888   82 DLIVLAGYMKILTPEFTARFTGKILNIHPSLLPKYAGLNPHQRAMDAGDTEHGTTIHFVNEEVDGGAIILQAKVPIYPDD 161
Cdd:TIGR00639  81 DLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPED 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 544678888  162 ELDDVIERVYEQEHRCYPLVVQWFCDDRLK 191
Cdd:TIGR00639 161 TEETLEQRIHKQEHRIYPLAIAWFAQGRLK 190
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 2-182 4.71e-83

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: 244.51  E-value: 4.71e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888    2 KNIVVMISGNGSNLQAIIDAIDTGKINGRICAVISNKATAYGLERAKQAGISTFIFTKKDFSDNLEMDNAIAEQIEALQA 81
Cdd:pfam00551   1 MKIAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888   82 DLIVLAGYMKILTPEFTARFTGKILNIHPSLLPKYAGLNPHQRAMDAGDTEHGTTIHFVNEEVDGGAIILQAKVPIYPDD 161
Cdd:pfam00551  81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160

                         170       180
                  ....*....|....*....|.
gi 544678888  162 ELDDVIERVYEQEHRCYPLVV 182
Cdd:pfam00551 161 TAETLYNRVADLEHKALPRVL 181
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 3-191 4.88e-53

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 169.10  E-value: 4.88e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888   3 NIVVMISGNGSNLQAIIDAIDTGKINGRICAVISNKATAYGLERAKQAGISTFIFTKKDFSDNLEMDNAIAEQIEALQAD 82
Cdd:PLN02331   1 KLAVFVSGGGSNFRAIHDACLDGRVNGDVVVVVTNKPGCGGAEYARENGIPVLVYPKTKGEPDGLSPDELVDALRGAGVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888  83 LIVLAGYMKILTPEFTARFTGKILNIHPSLLPK-----YAGLNPHQRAMDAGDTEHGTTIHFVNEEVDGGAIILQAKVPI 157
Cdd:PLN02331  81 FVLLAGYLKLIPVELVRAYPRSILNIHPALLPAfggkgYYGIKVHKAVIASGARYSGPTVHFVDEHYDTGRILAQRVVPV 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 544678888 158 YPDDELDDVIERVYEQEHRCYPLVVQWFCDDRLK 191
Cdd:PLN02331 161 LATDTPEELAARVLHEEHQLYVEVVAALCEERIV 194
 
Name Accession Description Interval E-value
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 1-202 5.54e-115

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: 325.83  E-value: 5.54e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888   1 MKNIVVMISGNGSNLQAIIDAIDTGKINGRICAVISNKATAYGLERAKQAGISTFIFTKKDFSDNLEMDNAIAEQIEALQ 80
Cdd:COG0299    1 MKRIAVLISGRGSNLQALIDAIEAGDLPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888  81 ADLIVLAGYMKILTPEFTARFTGKILNIHPSLLPKYAGLNPHQRAMDAGDTEHGTTIHFVNEEVDGGAIILQAKVPIYPD 160
Cdd:COG0299   81 PDLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPD 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 544678888 161 DELDDVIERVYEQEHRCYPLVVQWFCDDRLKLIEGKAYLDNQ 202
Cdd:COG0299  161 DTEETLAARILEQEHRLYPEAIRLLAEGRLTLDGRRVRLDGE 202
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 3-185 4.14e-103

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: 295.07  E-value: 4.14e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888   3 NIVVMISGNGSNLQAIIDAIDTGKINGRICAVISNKATAYGLERAKQAGISTFIFTKKDFSDNLEMDNAIAEQIEALQAD 82
Cdd:cd08645    1 RIAVLASGSGSNLQALIDAIKSGKLNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888  83 LIVLAGYMKILTPEFTARFTGKILNIHPSLLPKYAGLNPHQRAMDAGDTEHGTTIHFVNEEVDGGAIILQAKVPIYPDDE 162
Cdd:cd08645   81 LIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDT 160

                        170       180
                 ....*....|....*....|...
gi 544678888 163 LDDVIERVYEQEHRCYPLVVQWF 185
Cdd:cd08645  161 PETLAERIHALEHRLYPEAIKLL 183
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 2-191 2.38e-97

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: 281.18  E-value: 2.38e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888    2 KNIVVMISGNGSNLQAIIDAIDTGKINGRICAVISNKATAYGLERAKQAGISTFIFTKKDFSDNLEMDNAIAEQIEALQA 81
Cdd:TIGR00639   1 KRIVVLISGNGSNLQAIIDACKEGKIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888   82 DLIVLAGYMKILTPEFTARFTGKILNIHPSLLPKYAGLNPHQRAMDAGDTEHGTTIHFVNEEVDGGAIILQAKVPIYPDD 161
Cdd:TIGR00639  81 DLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPED 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 544678888  162 ELDDVIERVYEQEHRCYPLVVQWFCDDRLK 191
Cdd:TIGR00639 161 TEETLEQRIHKQEHRIYPLAIAWFAQGRLK 190
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 2-182 4.71e-83

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: 244.51  E-value: 4.71e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888    2 KNIVVMISGNGSNLQAIIDAIDTGKINGRICAVISNKATAYGLERAKQAGISTFIFTKKDFSDNLEMDNAIAEQIEALQA 81
Cdd:pfam00551   1 MKIAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888   82 DLIVLAGYMKILTPEFTARFTGKILNIHPSLLPKYAGLNPHQRAMDAGDTEHGTTIHFVNEEVDGGAIILQAKVPIYPDD 161
Cdd:pfam00551  81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160

                         170       180
                  ....*....|....*....|.
gi 544678888  162 ELDDVIERVYEQEHRCYPLVV 182
Cdd:pfam00551 161 TAETLYNRVADLEHKALPRVL 181
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 3-191 4.88e-53

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 169.10  E-value: 4.88e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888   3 NIVVMISGNGSNLQAIIDAIDTGKINGRICAVISNKATAYGLERAKQAGISTFIFTKKDFSDNLEMDNAIAEQIEALQAD 82
Cdd:PLN02331   1 KLAVFVSGGGSNFRAIHDACLDGRVNGDVVVVVTNKPGCGGAEYARENGIPVLVYPKTKGEPDGLSPDELVDALRGAGVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888  83 LIVLAGYMKILTPEFTARFTGKILNIHPSLLPK-----YAGLNPHQRAMDAGDTEHGTTIHFVNEEVDGGAIILQAKVPI 157
Cdd:PLN02331  81 FVLLAGYLKLIPVELVRAYPRSILNIHPALLPAfggkgYYGIKVHKAVIASGARYSGPTVHFVDEHYDTGRILAQRVVPV 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 544678888 158 YPDDELDDVIERVYEQEHRCYPLVVQWFCDDRLK 191
Cdd:PLN02331 161 LATDTPEELAARVLHEEHQLYVEVVAALCEERIV 194
FMT_core cd08369
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...
 6-184 1.62e-39

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: 133.57  E-value: 1.62e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888   6 VMISGNGSNLQAIIDAIdTGKINGRICAVISNKATAYGLERakqagISTFIFTKKDFSDNLEMDNAIAEQIEALQADLIV 85
Cdd:cd08369    1 IVILGSGNIGQRVLKAL-LSKEGHEIVGVVTHPDSPRGTAQ-----LSLELVGGKVYLDSNINTPELLELLKEFAPDLIV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888  86 LAGYMKILTPEFTARFTGKILNIHPSLLPKYAGLNPHQRAMDAGDTEHGTTIHFVNEEVDGGAIILQAKVPIYPDDELDD 165
Cdd:cd08369   75 SINFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTAGT 154

                        170
                 ....*....|....*....
gi 544678888 166 VIERVYEQEHRCYPLVVQW 184
Cdd:cd08369  155 LYQRLIELGPKLLKEALQK 173
FMT_core_Formyl-FH4-Hydrolase_C cd08648
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ...
 2-196 9.31e-38

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: 129.60  E-value: 9.31e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888   2 KNIVVMISGNGSNLQAIIDAIDTGKINGRICAVISNKATAYGLerAKQAGISTFIF-TKKDfsDNLEMDNAIAEQIEALQ 80
Cdd:cd08648    1 KRVAIFVSKEDHCLYDLLHRWREGELPCEIPLVISNHPDLRPL--AERFGIPFHHIpVTKD--TKAEAEAEQLELLEEYG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888  81 ADLIVLAGYMKILTPEFTARFTGKILNIHPSLLPKYAGLNPHQRAMDAGDTEHGTTIHFVNEEVDGGAIILQAKVPIYPD 160
Cdd:cd08648   77 VDLVVLARYMQILSPDFVERYPNRIINIHHSFLPAFKGAKPYHQAFERGVKLIGATAHYVTEELDEGPIIEQDVERVSHR 156

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 544678888 161 DELDDVIERVYEQEHRCYPLVVQWFCDDRLKLIEGK 196
Cdd:cd08648  157 DSVEDLVRKGRDIEKQVLARAVKWHLEDRVLVYGNK 192
PurU COG0788
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ...
 2-189 2.89e-32

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: 117.84  E-value: 2.89e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888   2 KNIVVMISGNGSNLQAIIDAIDTGKINGRICAVISNKATAYGLerAKQAGIsTFIFTKKDFSDNLEMDNAIAEQIEALQA 81
Cdd:COG0788   87 KRVAILVSKEDHCLNDLLYRWRSGELPAEIPAVISNHPDLRPL--AEWFGI-PFHHIPVTKETKAEAEARLLELLEEYDI 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888  82 DLIVLAGYMKILTPEFTARFTGKILNIHPSLLPKYAGLNPHQRAMDAGDTEHGTTIHFVNEEVDGGAIILQAKVPIYPDD 161
Cdd:COG0788  164 DLVVLARYMQILSPDFCARLPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVERVDHRD 243

                        170       180       190
                 ....*....|....*....|....*....|
gi 544678888 162 ELDDVIERVYEQEHRCypLV--VQWFCDDR 189
Cdd:COG0788  244 TPEDLVRKGRDVEKRV--LAraVRWHLEDR 271
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
45-170 1.59e-30

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


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 113.66  E-value: 1.59e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888  45 ERAKQAGIStfIFTKKDFSDNlemdnAIAEQIEALQADLIVLAGYMKILTPEFTARFTGKILNIHPSLLPKYAGLNPHQR 124
Cdd:COG0223   50 ELALEHGIP--VLQPESLKDP-----EFLEELRALNPDLIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAAPIQW 122

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 544678888 125 AMDAGDTEHGTTIHFVNEEVDGGAIILQAKVPIYPDDELDDVIERV 170
Cdd:COG0223  123 AILNGDTETGVTIMQMDEGLDTGDILLQEEVPIGPDDTAGSLHDKL 168
purU PRK06027
formyltetrahydrofolate deformylase; Reviewed
 2-189 1.56e-26

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 235676 [Multi-domain]  Cd Length: 286  Bit Score: 102.88  E-value: 1.56e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888   2 KNIVVMISGNGSNLQAIIDAIDTGKINGRICAVISNKATAYGLerAKQAGIStFIFTKKDFSDNLEMDNAIAEQIEALQA 81
Cdd:PRK06027  90 KRVVILVSKEDHCLGDLLWRWRSGELPVEIAAVISNHDDLRSL--VERFGIP-FHHVPVTKETKAEAEARLLELIDEYQP 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888  82 DLIVLAGYMKILTPEFTARFTGKILNIHPSLLPKYAGLNPHQRAMDAGDTEHGTTIHFVNEEVDGGAIILQAKVPIYPDD 161
Cdd:PRK06027 167 DLVVLARYMQILSPDFVARFPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVIRVDHRD 246

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 544678888 162 ELDDV------IERVyeqehrcyplV----VQWFCDDR 189
Cdd:PRK06027 247 TAEDLvragrdVEKQ----------VlaraVRWHLEDR 274
FMT_core_Met-tRNA-FMT_N cd08646
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ...
 45-169 2.07e-24

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: 95.20  E-value: 2.07e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888  45 ERAKQAGIStfIFTkkdfSDNLEMDNAIaEQIEALQADLIVLAGYMKILTPEFTARFTGKILNIHPSLLPKYAGLNPHQR 124
Cdd:cd08646   50 ELALELGLP--VLQ----PEKLKDEEFL-EELKALKPDLIVVVAYGQILPKEILDLPPYGCINVHPSLLPKYRGAAPIQR 122

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 544678888 125 AMDAGDTEHGTTIHFVNEEVDGGAIILQAKVPIYPDDELDDVIER 169
Cdd:cd08646  123 AILNGDKETGVTIMKMDEGLDTGDILAQEEVPIDPDDTAGELLDK 167
fmt TIGR00460
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ...
 66-169 1.48e-22

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: 92.85  E-value: 1.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888   66 LEMDNAIAEqIEALQADLIVLAGYMKILTPEFTARFTGKILNIHPSLLPKYAGLNPHQRAMDAGDTEHGTTIHFVNEEVD 145
Cdd:TIGR00460  65 QRQLEELPL-VRELKPDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVPKMD 143

                          90       100
                  ....*....|....*....|....*..
gi 544678888  146 GGAIILQAKVPIYPDD---ELDDVIER 169
Cdd:TIGR00460 144 AGDILKQETFPIEEEDnsgTLSDKLSE 170
FMT_core_like_3 cd08653
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 76-172 4.09e-22

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: 88.04  E-value: 4.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888  76 IEALQADLIVLAGyMKILTPEFTARFTGKILNIHPSLLPKYAGLNPHQRAMDAGDTEH-GTTIHFVNEEVDGGAIILQAK 154
Cdd:cd08653   43 LRALAPDVVSVYG-CGIIKDALLAIPPLGVLNLHGGILPDYRGVHTGFWALANGDPDNvGVTVHLVDAGIDTGDVLAQAR 121

                         90
                 ....*....|....*...
gi 544678888 155 VPIYPDDELDDVIERVYE 172
Cdd:cd08653  122 PPLAAGDTLLSLYLRLYR 139
PRK13011 PRK13011
formyltetrahydrofolate deformylase; Reviewed
 24-161 6.11e-22

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 237266 [Multi-domain]  Cd Length: 286  Bit Score: 90.81  E-value: 6.11e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888  24 TGKINGRICAVISNKATAYGLerAKQAGIStFIFTKKDFSDNLEMDNAIAEQIEALQADLIVLAGYMKILTPEFTARFTG 103
Cdd:PRK13011 112 IGELPMDIVGVVSNHPDLEPL--AAWHGIP-FHHFPITPDTKPQQEAQVLDVVEESGAELVVLARYMQVLSPELCRKLAG 188

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544678888 104 KILNIHPSLLPKYAGLNPHQRAMDAGDTEHGTTIHFVNEEVDGGAIILQAKVPI----YPDD 161
Cdd:PRK13011 189 RAINIHHSFLPGFKGAKPYHQAYERGVKLIGATAHYVTDDLDEGPIIEQDVERVdhaySPED 250
PLN02828 PLN02828
formyltetrahydrofolate deformylase
 82-190 1.77e-19

formyltetrahydrofolate deformylase


Pssm-ID: 178422  Cd Length: 268  Bit Score: 83.64  E-value: 1.77e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888  82 DLIVLAGYMKILTPEFTARFTGKILNIHPSLLPKYAGLNPHQRAMDAGDTEHGTTIHFVNEEVDGGAIILQAKVPIYPDD 161
Cdd:PLN02828 149 DFLVLARYMQILSGNFLKGYGKDIINIHHGLLPSFKGGNPSKQAFDAGVKLIGATSHFVTEELDAGPIIEQMVERVSHRD 228

                         90       100
                 ....*....|....*....|....*....
gi 544678888 162 ELDDVIERVYEQEHRCYPLVVQWFCDDRL 190
Cdd:PLN02828 229 NLRSFVQKSENLEKQCLAKAIKSYCELRV 257
purU PRK13010
formyltetrahydrofolate deformylase; Reviewed
 2-152 1.09e-18

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 139334 [Multi-domain]  Cd Length: 289  Bit Score: 81.77  E-value: 1.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888   2 KNIVVMISGNGSNLQAIIDAIDTGKINGRICAVISNKATAygLERAKQAGIStFIFTKKDFSDNLEMDNAIAEQIEALQA 81
Cdd:PRK13010  94 PKVVIMVSKFDHCLNDLLYRWRMGELDMDIVGIISNHPDL--QPLAVQHDIP-FHHLPVTPDTKAQQEAQILDLIETSGA 170

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544678888  82 DLIVLAGYMKILTPEFTARFTGKILNIHPSLLPKYAGLNPHQRAMDAGDTEHGTTIHFVNEEVDGGAIILQ 152
Cdd:PRK13010 171 ELVVLARYMQVLSDDLSRKLSGRAINIHHSFLPGFKGARPYHQAHARGVKLIGATAHFVTDDLDEGPIIEQ 241
PRK06988 PRK06988
formyltransferase;
69-170 2.73e-18

formyltransferase;


Pssm-ID: 235902 [Multi-domain]  Cd Length: 312  Bit Score: 81.28  E-value: 2.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888  69 DNAIAEQIEALQADLIVLAGYMKILTPEFTARFTGKILNIHPSLLPKYAGLNPHQRAMDAGDTEHGTTIHFVNEEVDGGA 148
Cdd:PRK06988  66 DPELRAAVAAAAPDFIFSFYYRHMIPVDLLALAPRGAYNMHGSLLPKYRGRVPVNWAVLNGETETGATLHEMVAKPDAGA 145

                         90       100
                 ....*....|....*....|..
gi 544678888 149 IILQAKVPIYPDDELDDVIERV 170
Cdd:PRK06988 146 IVDQTAVPILPDDTAAQVFDKV 167
PLN02285 PLN02285
methionyl-tRNA formyltransferase
 76-173 1.17e-17

methionyl-tRNA formyltransferase


Pssm-ID: 215159 [Multi-domain]  Cd Length: 334  Bit Score: 79.74  E-value: 1.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888  76 IEALQADLIVLAGYMKILTPEFTARFTGKILNIHPSLLPKYAGLNPHQRAMDAGDTEHGTTIHFVNEEVDGGAIILQAKV 155
Cdd:PLN02285  89 LRELQPDLCITAAYGNILPQKFLDIPKLGTVNIHPSLLPLYRGAAPVQRALQDGVNETGVSVAFTVRALDAGPVIAQERV 168

                         90
                 ....*....|....*...
gi 544678888 156 PIYPDDELDDVIERVYEQ 173
Cdd:PLN02285 169 EVDEDIKAPELLPLLFEL 186
FMT_core_ArnA_N cd08644
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ...
 73-176 2.58e-16

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: 73.92  E-value: 2.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888  73 AEQIEALQADLIVLAGYMKILTPEFTARFTGKILNIHPSLLPKYAGLNPHQRAMDAGDTEHGTTIHFVNEEVDGGAIILQ 152
Cdd:cd08644   68 VERLRALKPDLIFSFYYRHMISEDILEIARLGAFNLHGSLLPKYRGRAPLNWALINGETETGVTLHRMTKKPDAGAIVDQ 147

                         90       100
                 ....*....|....*....|....
gi 544678888 153 AKVPIYPDDELDDVIERVYEQEHR 176
Cdd:cd08644  148 EKVPILPDDTAKSLFHKLCVAARR 171
FMT_core_NRPS_like cd08649
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ...
 66-161 7.09e-15

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: 69.21  E-value: 7.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888  66 LEMDNAIAEQIEALQADLIVLAGYMKILTPEFTARFTGKILNIHPSLLPKYAGLNPHQRAMDAGDTEHGTTIHFVNEEVD 145
Cdd:cd08649   47 LEPGEALEELLSDEPFDWLFSIVNLRILPSEVLALPRKGAINFHDGPLPRYAGLNATSWALLAGETRHGVTWHRIEEGVD 126

                         90
                 ....*....|....*.
gi 544678888 146 GGAIILQAKVPIYPDD 161
Cdd:cd08649  127 AGDILVQRPFDIAPDD 142
FMT_core_like_5 cd08823
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 60-161 6.72e-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: 67.09  E-value: 6.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888  60 KDFSDNLEMDNAIAEQIEALQADLIVLAGYMKILTPEFTARFTGKILNIHPSLLPKYAGLNPHQRAMDAGDTEHGTTIHF 139
Cdd:cd08823   51 KQRVDTANLKEQLAEWLRALAADTVVVFTFPYRIPQHILDLPPLGFYNLHPGLLPAYRGPDPLFWQIRNQEQETAITVHK 130

                         90       100
                 ....*....|....*....|..
gi 544678888 140 VNEEVDGGAIILQAKVPIYPDD 161
Cdd:cd08823  131 MTAEIDRGPIVLEQFTPIHPDD 152
FMT_core_like_4 cd08651
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 15-170 6.47e-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: 187720 [Multi-domain]  Cd Length: 180  Bit Score: 64.21  E-value: 6.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888  15 LQAIIDAidtgkiNGRICAVISNKATAYG--------LERAKQAGISTFIFTKKDfsdnlemDNAIAEQIEALQADLIVL 86
Cdd:cd08651   15 LEAILEA------GGEVVGVITLDDSSSNndsdyldlDSFARKNGIPYYKFTDIN-------DEEIIEWIKEANPDIIFV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888  87 AGYMKILTPEFTARFTGKILNIHPSLLPKYAGLNPHQRAMDAGDTEHGTTIHFVNEEVDGGAIILQAKVPIYPDDELDDV 166
Cdd:cd08651   82 FGWSQLLKPEILAIPRLGVIGFHPTKLPKNRGRAPIPWAILLGLKETASTFFWMDEGADSGDILSQEPFPIDKDDTANSL 161


                 ....
gi 544678888 167 IERV 170
Cdd:cd08651  162 YDKI 165
PRK08125 PRK08125
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ...
 74-161 9.06e-11

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


Pssm-ID: 236156 [Multi-domain]  Cd Length: 660  Bit Score: 60.38  E-value: 9.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888  74 EQIEALQADLIVLAGYMKILTPEFTARFTGKILNIHPSLLPKYAGLNPHQRAMDAGDTEHGTTIHFVNEEVDGGAIILQA 153
Cdd:PRK08125  69 ERIRELAPDVIFSFYYRNLLSDEILQLAPAGAFNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQQ 148


                 ....*...
gi 544678888 154 KVPIYPDD 161
Cdd:PRK08125 149 RVAIAPDD 156
FMT_core_like_6 cd08820
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 72-171 1.32e-10

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: 57.84  E-value: 1.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888  72 IAEQIEALQADLIVLAGYMKILTPEFTARFTGKILNIHPSLLPKYAGLNPHQRAMDAGDTEHGTTIHFVNEEVDGGAIIL 151
Cdd:cd08820   61 LLEILENKGVDILISVQYHWILPGSILEKAKEIAFNLHNAPLPEYRGCNQFSHAILNGDDQFGTTIHWMAEGIDSGDIIF 140

                         90       100
                 ....*....|....*....|
gi 544678888 152 QAKVPIYPDDELDDVIERVY 171
Cdd:cd08820  141 EKRFPIPSDCTVISLYILAH 160
FMT_core_like_2 cd08822
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 82-170 9.65e-08

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: 50.15  E-value: 9.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544678888  82 DLIVLAGYMKILTPEFTARFTGKILNIHPSLLPKYAGLNPHQRAMDAGDTEHGTTIHFVNEEVDGGAIILQAKVPIYPDD 161
Cdd:cd08822   68 DLIVAAHCHAFISAKTRARARLGAIGYHPSLLPRHRGRDAVEWTIRMRDPITGGTVYHLDDGVDGGPIAAQDWCHVRPGD 147


                 ....*....
gi 544678888 162 ELDDVIERV 170
Cdd:cd08822  148 TAAELWRRA 156
FMT_core_FDH_N cd08647
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ...
 109-169 6.66e-07

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: 47.83  E-value: 6.66e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544678888 109 HPSLLPKYAGLNPHQRAMDAGDTEHGTTIHFVNEEVDGGAIILQAKVPIYPDDELDDVIER 169
Cdd:cd08647  106 HPSILPRHRGASAINWTLIHGDKKAGFTIFWADDGLDTGPILLQKECDVLPNDTVDTLYNR 166
PRK07579 PRK07579
dTDP-4-amino-4,6-dideoxyglucose formyltransferase;
106-174 1.56e-03

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


Pssm-ID: 236058 [Multi-domain]  Cd Length: 245  Bit Score: 38.35  E-value: 1.56e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544678888 106 LNIHPSLLPKYAGLNPHQRAMdAGDTEHGTTIHFVNEEVDGGAIILQAKVPIYPDDELDDVIERVYEQE 174
Cdd:PRK07579  89 INIHPGFNPYNRGWFPQVFSI-INGLKIGATIHEMDEQLDHGPIIAQREVEIESWDSSGSVYARVMDIE 156
 
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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