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Conserved domains on  [gi|663514104|gb|AIF04625|]
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putative Formyl transferase (purN) [uncultured marine thaumarchaeote KM3_175_E11]

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 ...
 1-110 1.91e-66

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: 198.72  E-value: 1.91e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663514104   1 MRILSPEFIKKFKNRILNIHPSILPAFPGLDAQRQAIESGASHSGCTVHFVDEGVDTGPILVQETVKIKNDDTEETLSKR 80
Cdd:COG0299   90 MRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDDTEETLAAR 169

                         90       100       110
                 ....*....|....*....|....*....|
gi 663514104  81 ILAKEHKAYPEAVRLIAEKKISVVGRKVKI 110
Cdd:COG0299  170 ILEQEHRLYPEAIRLLAEGRLTLDGRRVRL 199
 
Name Accession Description Interval E-value
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 1-110 1.91e-66

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: 198.72  E-value: 1.91e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663514104   1 MRILSPEFIKKFKNRILNIHPSILPAFPGLDAQRQAIESGASHSGCTVHFVDEGVDTGPILVQETVKIKNDDTEETLSKR 80
Cdd:COG0299   90 MRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDDTEETLAAR 169

                         90       100       110
                 ....*....|....*....|....*....|
gi 663514104  81 ILAKEHKAYPEAVRLIAEKKISVVGRKVKI 110
Cdd:COG0299  170 ILEQEHRLYPEAIRLLAEGRLTLDGRRVRL 199
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 1-96 4.89e-59

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: 179.12  E-value: 4.89e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663514104   1 MRILSPEFIKKFKNRILNIHPSILPAFPGLDAQRQAIESGASHSGCTVHFVDEGVDTGPILVQETVKIKNDDTEETLSKR 80
Cdd:cd08645   88 MRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDTPETLAER 167

                         90
                 ....*....|....*.
gi 663514104  81 ILAKEHKAYPEAVRLI 96
Cdd:cd08645  168 IHALEHRLYPEAIKLL 183
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 1-98 1.45e-46

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: 147.90  E-value: 1.45e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663514104    1 MRILSPEFIKKFKNRILNIHPSILPAFPGLDAQRQAIESGASHSGCTVHFVDEGVDTGPILVQETVKIKNDDTEETLSKR 80
Cdd:TIGR00639  89 MRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPEDTEETLEQR 168

                          90
                  ....*....|....*...
gi 663514104   81 ILAKEHKAYPEAVRLIAE 98
Cdd:TIGR00639 169 IHKQEHRIYPLAIAWFAQ 186
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 1-93 1.49e-41

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: 135.11  E-value: 1.49e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663514104    1 MRILSPEFIKKFKNRILNIHPSILPAFPGLDAQRQAIESGASHSGCTVHFVDEGVDTGPILVQETVKIKNDDTEETLSKR 80
Cdd:pfam00551  89 MRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDDTAETLYNR 168

                          90
                  ....*....|...
gi 663514104   81 ILAKEHKAYPEAV 93
Cdd:pfam00551 169 VADLEHKALPRVL 181
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 1-101 1.09e-32

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 113.25  E-value: 1.09e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663514104   1 MRILSPEFIKKFKNRILNIHPSILPAFPG-----LDAQRQAIESGASHSGCTVHFVDEGVDTGPILVQETVKIKNDDTEE 75
Cdd:PLN02331  88 LKLIPVELVRAYPRSILNIHPALLPAFGGkgyygIKVHKAVIASGARYSGPTVHFVDEHYDTGRILAQRVVPVLATDTPE 167

                         90       100
                 ....*....|....*....|....*.
gi 663514104  76 TLSKRILAKEHKAYPEAVRLIAEKKI 101
Cdd:PLN02331 168 ELAARVLHEEHQLYVEVVAALCEERI 193
 
Name Accession Description Interval E-value
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 1-110 1.91e-66

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: 198.72  E-value: 1.91e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663514104   1 MRILSPEFIKKFKNRILNIHPSILPAFPGLDAQRQAIESGASHSGCTVHFVDEGVDTGPILVQETVKIKNDDTEETLSKR 80
Cdd:COG0299   90 MRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDDTEETLAAR 169

                         90       100       110
                 ....*....|....*....|....*....|
gi 663514104  81 ILAKEHKAYPEAVRLIAEKKISVVGRKVKI 110
Cdd:COG0299  170 ILEQEHRLYPEAIRLLAEGRLTLDGRRVRL 199
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 1-96 4.89e-59

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: 179.12  E-value: 4.89e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663514104   1 MRILSPEFIKKFKNRILNIHPSILPAFPGLDAQRQAIESGASHSGCTVHFVDEGVDTGPILVQETVKIKNDDTEETLSKR 80
Cdd:cd08645   88 MRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDTPETLAER 167

                         90
                 ....*....|....*.
gi 663514104  81 ILAKEHKAYPEAVRLI 96
Cdd:cd08645  168 IHALEHRLYPEAIKLL 183
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 1-98 1.45e-46

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: 147.90  E-value: 1.45e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663514104    1 MRILSPEFIKKFKNRILNIHPSILPAFPGLDAQRQAIESGASHSGCTVHFVDEGVDTGPILVQETVKIKNDDTEETLSKR 80
Cdd:TIGR00639  89 MRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPEDTEETLEQR 168

                          90
                  ....*....|....*...
gi 663514104   81 ILAKEHKAYPEAVRLIAE 98
Cdd:TIGR00639 169 IHKQEHRIYPLAIAWFAQ 186
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 1-93 1.49e-41

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: 135.11  E-value: 1.49e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663514104    1 MRILSPEFIKKFKNRILNIHPSILPAFPGLDAQRQAIESGASHSGCTVHFVDEGVDTGPILVQETVKIKNDDTEETLSKR 80
Cdd:pfam00551  89 MRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDDTAETLYNR 168

                          90
                  ....*....|...
gi 663514104   81 ILAKEHKAYPEAV 93
Cdd:pfam00551 169 VADLEHKALPRVL 181
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 1-101 1.09e-32

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 113.25  E-value: 1.09e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663514104   1 MRILSPEFIKKFKNRILNIHPSILPAFPG-----LDAQRQAIESGASHSGCTVHFVDEGVDTGPILVQETVKIKNDDTEE 75
Cdd:PLN02331  88 LKLIPVELVRAYPRSILNIHPALLPAFGGkgyygIKVHKAVIASGARYSGPTVHFVDEHYDTGRILAQRVVPVLATDTPE 167

                         90       100
                 ....*....|....*....|....*.
gi 663514104  76 TLSKRILAKEHKAYPEAVRLIAEKKI 101
Cdd:PLN02331 168 ELAARVLHEEHQLYVEVVAALCEERI 193
FMT_core cd08369
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...
 1-95 1.14e-32

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: 112.00  E-value: 1.14e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663514104   1 MRILSPEFIKKFKNRILNIHPSILPAFPGLDAQRQAIESGASHSGCTVHFVDEGVDTGPILVQETVKIKNDDTEETLSKR 80
Cdd:cd08369   79 RQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTAGTLYQR 158

                         90
                 ....*....|....*
gi 663514104  81 ILAKEHKAYPEAVRL 95
Cdd:cd08369  159 LIELGPKLLKEALQK 173
PurU COG0788
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ...
 1-108 1.11e-25

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: 96.66  E-value: 1.11e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663514104   1 MRILSPEFIKKFKNRILNIHPSILPAFPGLDAQRQAIESGASHSGCTVHFVDEGVDTGPILVQETVKIKNDDTEETLS-- 78
Cdd:COG0788  172 MQILSPDFCARLPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVERVDHRDTPEDLVrk 251

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 663514104  79 -----KRILAkehkaypEAVRLIAEKKISVVGRKV 108
Cdd:COG0788  252 grdveKRVLA-------RAVRWHLEDRVLVNGNKT 279
FMT_core_Formyl-FH4-Hydrolase_C cd08648
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ...
 1-111 1.59e-25

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: 94.55  E-value: 1.59e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663514104   1 MRILSPEFIKKFKNRILNIHPSILPAFPGLDAQRQAIESGASHSGCTVHFVDEGVDTGPILVQETVKIKNDDTEETLS-- 78
Cdd:cd08648   86 MQILSPDFVERYPNRIINIHHSFLPAFKGAKPYHQAFERGVKLIGATAHYVTEELDEGPIIEQDVERVSHRDSVEDLVrk 165

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 663514104  79 -----KRILAKehkaypeAVRLIAEKKISVVGRKVKIL 111
Cdd:cd08648  166 grdieKQVLAR-------AVKWHLEDRVLVYGNKTVVF 196
PurU TIGR00655
formyltetrahydrofolate deformylase; This model describes formyltetrahydrofolate deformylases. ...
 1-111 5.98e-24

formyltetrahydrofolate deformylase; This model describes formyltetrahydrofolate deformylases. The enzyme is a homohexamer. Sequences from a related enzyme formyl tetrahydrofolate-specific enzyme, phosphoribosylglycinamide formyltransferase, serve as an outgroup for phylogenetic analysis. Putative members of this family, scoring below the trusted cutoff, include a sequence from Rhodobacter capsulatus that lacks an otherwise conserved C-terminal region. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273199 [Multi-domain]  Cd Length: 280  Bit Score: 92.11  E-value: 5.98e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663514104    1 MRILSPEFIKKFKNRILNIHPSILPAFPGLDAQRQAIESGASHSGCTVHFVDEGVDTGPILVQETVKIKNDDTEETLSKR 80
Cdd:TIGR00655 170 MQILSPDFVKRYPNKIINIHHSFLPAFIGANPYQRAYERGVKIIGATAHYVTEELDEGPIIEQDVVRVDHTDNVEDLIRA 249

                          90       100       110
                  ....*....|....*....|....*....|.
gi 663514104   81 ILAKEHKAYPEAVRLIAEKKISVVGRKVKIL 111
Cdd:TIGR00655 250 GRDIEKVVLARAVKLHLEDRVFVYENKTVVF 280
purU PRK06027
formyltetrahydrofolate deformylase; Reviewed
 1-107 5.72e-20

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 235676 [Multi-domain]  Cd Length: 286  Bit Score: 81.69  E-value: 5.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663514104   1 MRILSPEFIKKFKNRILNIHPSILPAFPGLDAQRQAIESGASHSGCTVHFVDEGVDTGPILVQETVKIKNDDTEETL--- 77
Cdd:PRK06027 175 MQILSPDFVARFPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVIRVDHRDTAEDLvra 254

                         90       100       110
                 ....*....|....*....|....*....|....
gi 663514104  78 ----SKRILAKehkaypeAVRLIAEKKISVVGRK 107
Cdd:PRK06027 255 grdvEKQVLAR-------AVRWHLEDRVLVYGNK 281
FMT_core_Met-tRNA-FMT_N cd08646
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ...
 2-84 1.63e-19

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: 79.02  E-value: 1.63e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663514104   2 RILSPEFIKKFKNRILNIHPSILPAFPGldA---QRqAIESGASHSGCTVHFVDEGVDTGPILVQETVKIKNDDTEETLS 78
Cdd:cd08646   89 QILPKEILDLPPYGCINVHPSLLPKYRG--AapiQR-AILNGDKETGVTIMKMDEGLDTGDILAQEEVPIDPDDTAGELL 165


                 ....*.
gi 663514104  79 KRiLAK 84
Cdd:cd08646  166 DK-LAE 170
FMT_core_like_3 cd08653
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 1-94 3.62e-19

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: 76.87  E-value: 3.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663514104   1 MRILSPEFIKKFKNRILNIHPSILPAFPGLDAQRQAIESG-ASHSGCTVHFVDEGVDTGPILVQETVKIKNDDTEETLSK 79
Cdd:cd08653   56 CGIIKDALLAIPPLGVLNLHGGILPDYRGVHTGFWALANGdPDNVGVTVHLVDAGIDTGDVLAQARPPLAAGDTLLSLYL 135

                         90
                 ....*....|....*
gi 663514104  80 RILAKEHKAYPEAVR 94
Cdd:cd08653  136 RLYRAGVELMVEAIA 150
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
2-101 3.80e-19

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


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 79.76  E-value: 3.80e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663514104   2 RILSPEFIKKFKNRILNIHPSILPAFPGLDA-QRqAIESGASHSGCTVHFVDEGVDTGPILVQETVKIKNDDTEETLSKR 80
Cdd:COG0223   89 QILPKEVLDIPRLGCINLHASLLPRYRGAAPiQW-AILNGDTETGVTIMQMDEGLDTGDILLQEEVPIGPDDTAGSLHDK 167

                         90       100
                 ....*....|....*....|.
gi 663514104  81 ILAKEHKAYPEAVRLIAEKKI 101
Cdd:COG0223  168 LAELGAELLLETLDALEAGTL 188
PLN02828 PLN02828
formyltetrahydrofolate deformylase
 1-104 2.75e-18

formyltetrahydrofolate deformylase


Pssm-ID: 178422  Cd Length: 268  Bit Score: 77.09  E-value: 2.75e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663514104   1 MRILSPEFIKKFKNRILNIHPSILPAFPGLDAQRQAIESGASHSGCTVHFVDEGVDTGPILVQETVKIKNDDT------- 73
Cdd:PLN02828 157 MQILSGNFLKGYGKDIINIHHGLLPSFKGGNPSKQAFDAGVKLIGATSHFVTEELDAGPIIEQMVERVSHRDNlrsfvqk 236

                         90       100       110
                 ....*....|....*....|....*....|.
gi 663514104  74 EETLSKRILAKEHKAYPEAVRLIAEKKISVV 104
Cdd:PLN02828 237 SENLEKQCLAKAIKSYCELRVLPYGTNKTVV 267
FMT_core_FDH_N cd08647
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ...
 20-100 3.77e-16

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: 70.17  E-value: 3.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663514104  20 HPSILPAFPGLDAQRQAIESGASHSGCTVHFVDEGVDTGPILVQETVKIKNDDTEETLSKRILAKEH-KAYPEAVRLIAE 98
Cdd:cd08647  106 HPSILPRHRGASAINWTLIHGDKKAGFTIFWADDGLDTGPILLQKECDVLPNDTVDTLYNRFLYPEGiKAMVEAVRLIAE 185


                 ..
gi 663514104  99 KK 100
Cdd:cd08647  186 GK 187
purU PRK13010
formyltetrahydrofolate deformylase; Reviewed
 1-107 2.78e-15

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 139334 [Multi-domain]  Cd Length: 289  Bit Score: 69.44  E-value: 2.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663514104   1 MRILSPEFIKKFKNRILNIHPSILPAFPGLDAQRQAIESGASHSGCTVHFVDEGVDTGPILVQETVKIKNDDTEETLSKR 80
Cdd:PRK13010 179 MQVLSDDLSRKLSGRAINIHHSFLPGFKGARPYHQAHARGVKLIGATAHFVTDDLDEGPIIEQDVERVDHSYSPEDLVAK 258

                         90       100
                 ....*....|....*....|....*..
gi 663514104  81 ILAKEHKAYPEAVRLIAEKKISVVGRK 107
Cdd:PRK13010 259 GRDVECLTLARAVKAFIEHRVFINGDR 285
PRK13011 PRK13011
formyltetrahydrofolate deformylase; Reviewed
 1-77 2.26e-14

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 237266 [Multi-domain]  Cd Length: 286  Bit Score: 66.54  E-value: 2.26e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663514104   1 MRILSPEFIKKFKNRILNIHPSILPAFPGLDAQRQAIESGASHSGCTVHFVDEGVDTGPILVQETVKIKNDDTEETL 77
Cdd:PRK13011 175 MQVLSPELCRKLAGRAINIHHSFLPGFKGAKPYHQAYERGVKLIGATAHYVTDDLDEGPIIEQDVERVDHAYSPEDL 251
FMT_core_like_4 cd08651
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 3-81 7.29e-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: 61.13  E-value: 7.29e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663514104   3 ILSPEFIKKFKNRILNIHPSILPAFPGLDAQRQAIESGASHSGCTVHFVDEGVDTGPILVQETVKIKNDDTEETLSKRI 81
Cdd:cd08651   87 LLKPEILAIPRLGVIGFHPTKLPKNRGRAPIPWAILLGLKETASTFFWMDEGADSGDILSQEPFPIDKDDTANSLYDKI 165
FMT_core_like_2 cd08822
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 4-98 1.55e-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: 60.55  E-value: 1.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663514104   4 LSPEFIKKFKNRILNIHPSILPAFPGLDAQRQAIESGASHSGCTVHFVDEGVDTGPILVQETVKIKNDDTEETLSKRILA 83
Cdd:cd08822   79 ISAKTRARARLGAIGYHPSLLPRHRGRDAVEWTIRMRDPITGGTVYHLDDGVDGGPIAAQDWCHVRPGDTAAELWRRALA 158

                         90
                 ....*....|....*
gi 663514104  84 kehkayPEAVRLIAE 98
Cdd:cd08822  159 ------PMGVKLLTQ 167
FMT_core_NRPS_like cd08649
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ...
 2-77 3.72e-12

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: 59.19  E-value: 3.72e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663514104   2 RILSPEFIKKFKNRILNIHPSILPAFPGLDAQRQAIESGASHSGCTVHFVDEGVDTGPILVQETVKIKNDDTEETL 77
Cdd:cd08649   72 RILPSEVLALPRKGAINFHDGPLPRYAGLNATSWALLAGETRHGVTWHRIEEGVDAGDILVQRPFDIAPDDTALSL 147
PLN02285 PLN02285
methionyl-tRNA formyltransferase
 3-81 4.20e-10

methionyl-tRNA formyltransferase


Pssm-ID: 215159 [Multi-domain]  Cd Length: 334  Bit Score: 55.08  E-value: 4.20e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663514104   3 ILSPEFIKKFKNRILNIHPSILPAFPGLDAQRQAIESGASHSGCTVHFVDEGVDTGPILVQETVKIKNDDTEETLSKRI 81
Cdd:PLN02285 105 ILPQKFLDIPKLGTVNIHPSLLPLYRGAAPVQRALQDGVNETGVSVAFTVRALDAGPVIAQERVEVDEDIKAPELLPLL 183
FMT_core_like_5 cd08823
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 7-98 5.74e-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: 187725 [Multi-domain]  Cd Length: 177  Bit Score: 53.60  E-value: 5.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663514104   7 EFIKKFKNRILNIHPSILPAFPGLDAQRQAIESGASHSGCTVHFVDEGVDTGPILVQETVKIKNDDTEETLSKRIlakeh 86
Cdd:cd08823   87 HILDLPPLGFYNLHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMTAEIDRGPIVLEQFTPIHPDDTYGLLCSRL----- 161

                         90
                 ....*....|..
gi 663514104  87 kAYpEAVRLIAE 98
Cdd:cd08823  162 -AM-LAVGLLEE 171
FMT_core_like_6 cd08820
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 3-77 1.55e-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: 187722 [Multi-domain]  Cd Length: 173  Bit Score: 49.75  E-value: 1.55e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663514104   3 ILSPEFIKKFKNRILNIHPSILPAFPGLDAQRQAIESGASHSGCTVHFVDEGVDTGPILVQETVKIKNDDTEETL 77
Cdd:cd08820   81 ILPGSILEKAKEIAFNLHNAPLPEYRGCNQFSHAILNGDDQFGTTIHWMAEGIDSGDIIFEKRFPIPSDCTVISL 155
FMT_core_ArnA_N cd08644
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ...
 1-82 3.42e-08

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: 49.27  E-value: 3.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663514104   1 MRILSPEFIKKFKNR------IL--------NIHPSILPAFPGLDAQRQAIESGASHSGCTVHFVDEGVDTGPILVQETV 66
Cdd:cd08644   71 LRALKPDLIFSFYYRhmisedILeiarlgafNLHGSLLPKYRGRAPLNWALINGETETGVTLHRMTKKPDAGAIVDQEKV 150

                         90
                 ....*....|....*.
gi 663514104  67 KIKNDDTEETLSKRIL 82
Cdd:cd08644  151 PILPDDTAKSLFHKLC 166
PRK08125 PRK08125
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ...
 2-81 3.22e-07

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


Pssm-ID: 236156 [Multi-domain]  Cd Length: 660  Bit Score: 46.90  E-value: 3.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663514104   2 RILSPEFIKKFKNR------IL--------NIHPSILPAFPGLDAQRQAIESGASHSGCTVHFVDEGVDTGPILVQETVK 67
Cdd:PRK08125  72 RELAPDVIFSFYYRnllsdeILqlapagafNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQQRVA 151

                         90
                 ....*....|....
gi 663514104  68 IKNDDTEETLSKRI 81
Cdd:PRK08125 152 IAPDDTALTLHHKL 165
PRK07579 PRK07579
dTDP-4-amino-4,6-dideoxyglucose formyltransferase;
15-85 3.17e-06

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


Pssm-ID: 236058 [Multi-domain]  Cd Length: 245  Bit Score: 44.12  E-value: 3.17e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663514104  15 RILNIHPSILPAFPGLDAQRQAIESGAShSGCTVHFVDEGVDTGPILVQETVKIKNDDTEETLSKRILAKE 85
Cdd:PRK07579  87 RCINIHPGFNPYNRGWFPQVFSIINGLK-IGATIHEMDEQLDHGPIIAQREVEIESWDSSGSVYARVMDIE 156
PRK06988 PRK06988
formyltransferase;
2-73 8.29e-06

formyltransferase;


Pssm-ID: 235902 [Multi-domain]  Cd Length: 312  Bit Score: 42.76  E-value: 8.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663514104   2 RILSPEFIKKFKNR--------------ILNIHPSILPAFPGLDAQRQAIESGASHSGCTVHFVDEGVDTGPILVQETVK 67
Cdd:PRK06988  74 AAAAPDFIFSFYYRhmipvdllalaprgAYNMHGSLLPKYRGRVPVNWAVLNGETETGATLHEMVAKPDAGAIVDQTAVP 153


                 ....*.
gi 663514104  68 IKNDDT 73
Cdd:PRK06988 154 ILPDDT 159
 
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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