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Conserved domains on  [gi|987450986|gb|AMD86425|]
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phosphoribosylglycinamide formyltransferase [Actinomyces radicidentis]

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 ...
 7-193 3.01e-68

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: 206.81  E-value: 3.01e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987450986   7 ARLVVLVSGTGSNLVALLRACEDPAYGAEVVRVVADKP-CPGVGHALAAGVAASVVAPRDFADRPAWDEALAEEIAGAEP 85
Cdd:COG0299    2 KRIAVLISGRGSNLQALIDAIEAGDLPAEIVLVISNRPdAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYGP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987450986  86 DLVVCAGFMRILGEPVLTRLEGRIINTHPSLLPSFPGAHAVRDALAAGATRAGATLFWVDAGVDTGEHIAQVEVPVLPGD 165
Cdd:COG0299   82 DLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDD 161

                        170       180
                 ....*....|....*....|....*...
gi 987450986 166 TEESLTARVKAAETPQLVEQVGILARER 193
Cdd:COG0299  162 TEETLAARILEQEHRLYPEAIRLLAEGR 189
 
Name Accession Description Interval E-value
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 7-193 3.01e-68

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: 206.81  E-value: 3.01e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987450986   7 ARLVVLVSGTGSNLVALLRACEDPAYGAEVVRVVADKP-CPGVGHALAAGVAASVVAPRDFADRPAWDEALAEEIAGAEP 85
Cdd:COG0299    2 KRIAVLISGRGSNLQALIDAIEAGDLPAEIVLVISNRPdAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYGP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987450986  86 DLVVCAGFMRILGEPVLTRLEGRIINTHPSLLPSFPGAHAVRDALAAGATRAGATLFWVDAGVDTGEHIAQVEVPVLPGD 165
Cdd:COG0299   82 DLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDD 161

                        170       180
                 ....*....|....*....|....*...
gi 987450986 166 TEESLTARVKAAETPQLVEQVGILARER 193
Cdd:COG0299  162 TEETLAARILEQEHRLYPEAIRLLAEGR 189
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 8-178 1.84e-61

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: 189.14  E-value: 1.84e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987450986   8 RLVVLVSGTGSNLVALLRACEDPAYGAEVVRVVADKPC-PGVGHALAAGVAASVVAPRDFADRPAWDEALAEEIAGAEPD 86
Cdd:cd08645    1 RIAVLASGSGSNLQALIDAIKSGKLNAEIVLVISNNPDaYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987450986  87 LVVCAGFMRILGEPVLTRLEGRIINTHPSLLPSFPGAHAVRDALAAGATRAGATLFWVDAGVDTGEHIAQVEVPVLPGDT 166
Cdd:cd08645   81 LIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDT 160

                        170
                 ....*....|..
gi 987450986 167 EESLTARVKAAE 178
Cdd:cd08645  161 PETLAERIHALE 172
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 7-193 1.07e-55

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: 174.48  E-value: 1.07e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987450986    7 ARLVVLVSGTGSNLVALLRACEDPAYGAEVVRVVADKP-CPGVGHALAAGVAASVVAPRDFADRPAWDEALAEEIAGAEP 85
Cdd:TIGR00639   1 KRIVVLISGNGSNLQAIIDACKEGKIPASVVLVISNKPdAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987450986   86 DLVVCAGFMRILGEPVLTRLEGRIINTHPSLLPSFPGAHAVRDALAAGATRAGATLFWVDAGVDTGEHIAQVEVPVLPGD 165
Cdd:TIGR00639  81 DLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPED 160

                         170       180
                  ....*....|....*....|....*...
gi 987450986  166 TEESLTARVKAAETPQLVEQVGILARER 193
Cdd:TIGR00639 161 TEETLEQRIHKQEHRIYPLAIAWFAQGR 188
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 7-184 3.32e-43

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: 142.43  E-value: 3.32e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987450986    7 ARLVVLVSGTGSNLVALLRACEDPAYGAEVVRVVADKP-CPGVGHALAAGVAASVVAPRDFADRPAWDEALAEEIAGAEP 85
Cdd:pfam00551   1 MKIAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDkAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987450986   86 DLVVCAGFMRILGEPVLTRLEGRIINTHPSLLPSFPGAHAVRDALAAGATRAGATLFWVDAGVDTGEHIAQVEVPVLPGD 165
Cdd:pfam00551  81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160

                         170
                  ....*....|....*....
gi 987450986  166 TEESLTARVKAAETPQLVE 184
Cdd:pfam00551 161 TAETLYNRVADLEHKALPR 179
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 8-193 1.60e-22

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 90.14  E-value: 1.60e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987450986   8 RLVVLVSGTGSNLVALLRACEDPAYGAEVVRVVADKP-CPGVGHALAAGVAASVVAPRDFADRPAWDEALAEEIAGAEPD 86
Cdd:PLN02331   1 KLAVFVSGGGSNFRAIHDACLDGRVNGDVVVVVTNKPgCGGAEYARENGIPVLVYPKTKGEPDGLSPDELVDALRGAGVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987450986  87 LVVCAGFMRILGEPVLTRLEGRIINTHPSLLPSFPGA-----HAVRDALAAGATRAGATLFWVDAGVDTGEHIAQVEVPV 161
Cdd:PLN02331  81 FVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFGGKgyygiKVHKAVIASGARYSGPTVHFVDEHYDTGRILAQRVVPV 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 987450986 162 LPGDTEESLTARVKAAETPQLVEQVGILARER 193
Cdd:PLN02331 161 LATDTPEELAARVLHEEHQLYVEVVAALCEER 192
 
Name Accession Description Interval E-value
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 7-193 3.01e-68

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: 206.81  E-value: 3.01e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987450986   7 ARLVVLVSGTGSNLVALLRACEDPAYGAEVVRVVADKP-CPGVGHALAAGVAASVVAPRDFADRPAWDEALAEEIAGAEP 85
Cdd:COG0299    2 KRIAVLISGRGSNLQALIDAIEAGDLPAEIVLVISNRPdAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYGP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987450986  86 DLVVCAGFMRILGEPVLTRLEGRIINTHPSLLPSFPGAHAVRDALAAGATRAGATLFWVDAGVDTGEHIAQVEVPVLPGD 165
Cdd:COG0299   82 DLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDD 161

                        170       180
                 ....*....|....*....|....*...
gi 987450986 166 TEESLTARVKAAETPQLVEQVGILARER 193
Cdd:COG0299  162 TEETLAARILEQEHRLYPEAIRLLAEGR 189
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 8-178 1.84e-61

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: 189.14  E-value: 1.84e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987450986   8 RLVVLVSGTGSNLVALLRACEDPAYGAEVVRVVADKPC-PGVGHALAAGVAASVVAPRDFADRPAWDEALAEEIAGAEPD 86
Cdd:cd08645    1 RIAVLASGSGSNLQALIDAIKSGKLNAEIVLVISNNPDaYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987450986  87 LVVCAGFMRILGEPVLTRLEGRIINTHPSLLPSFPGAHAVRDALAAGATRAGATLFWVDAGVDTGEHIAQVEVPVLPGDT 166
Cdd:cd08645   81 LIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDT 160

                        170
                 ....*....|..
gi 987450986 167 EESLTARVKAAE 178
Cdd:cd08645  161 PETLAERIHALE 172
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 7-193 1.07e-55

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: 174.48  E-value: 1.07e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987450986    7 ARLVVLVSGTGSNLVALLRACEDPAYGAEVVRVVADKP-CPGVGHALAAGVAASVVAPRDFADRPAWDEALAEEIAGAEP 85
Cdd:TIGR00639   1 KRIVVLISGNGSNLQAIIDACKEGKIPASVVLVISNKPdAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987450986   86 DLVVCAGFMRILGEPVLTRLEGRIINTHPSLLPSFPGAHAVRDALAAGATRAGATLFWVDAGVDTGEHIAQVEVPVLPGD 165
Cdd:TIGR00639  81 DLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPED 160

                         170       180
                  ....*....|....*....|....*...
gi 987450986  166 TEESLTARVKAAETPQLVEQVGILARER 193
Cdd:TIGR00639 161 TEETLEQRIHKQEHRIYPLAIAWFAQGR 188
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 7-184 3.32e-43

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: 142.43  E-value: 3.32e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987450986    7 ARLVVLVSGTGSNLVALLRACEDPAYGAEVVRVVADKP-CPGVGHALAAGVAASVVAPRDFADRPAWDEALAEEIAGAEP 85
Cdd:pfam00551   1 MKIAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDkAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987450986   86 DLVVCAGFMRILGEPVLTRLEGRIINTHPSLLPSFPGAHAVRDALAAGATRAGATLFWVDAGVDTGEHIAQVEVPVLPGD 165
Cdd:pfam00551  81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160

                         170
                  ....*....|....*....
gi 987450986  166 TEESLTARVKAAETPQLVE 184
Cdd:pfam00551 161 TAETLYNRVADLEHKALPR 179
FMT_core cd08369
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...
 11-186 5.03e-26

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: 98.13  E-value: 5.03e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987450986  11 VLVSGTGSNLVALLRACEDPAyGAEVVRVVADKPcpgVGHALAAGVAASVVAPRDFADRPAWDEaLAEEIAGAEPDLVVC 90
Cdd:cd08369    1 IVILGSGNIGQRVLKALLSKE-GHEIVGVVTHPD---SPRGTAQLSLELVGGKVYLDSNINTPE-LLELLKEFAPDLIVS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987450986  91 AGFMRILGEPVLTRLEGRIINTHPSLLPSFPGAHAVRDALAAGATRAGATLFWVDAGVDTGEHIAQVEVPVLPGDTEESL 170
Cdd:cd08369   76 INFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTAGTL 155

                        170
                 ....*....|....*.
gi 987450986 171 TARVKAAEtPQLVEQV 186
Cdd:cd08369  156 YQRLIELG-PKLLKEA 170
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 8-193 1.60e-22

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 90.14  E-value: 1.60e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987450986   8 RLVVLVSGTGSNLVALLRACEDPAYGAEVVRVVADKP-CPGVGHALAAGVAASVVAPRDFADRPAWDEALAEEIAGAEPD 86
Cdd:PLN02331   1 KLAVFVSGGGSNFRAIHDACLDGRVNGDVVVVVTNKPgCGGAEYARENGIPVLVYPKTKGEPDGLSPDELVDALRGAGVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987450986  87 LVVCAGFMRILGEPVLTRLEGRIINTHPSLLPSFPGA-----HAVRDALAAGATRAGATLFWVDAGVDTGEHIAQVEVPV 161
Cdd:PLN02331  81 FVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFGGKgyygiKVHKAVIASGARYSGPTVHFVDEHYDTGRILAQRVVPV 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 987450986 162 LPGDTEESLTARVKAAETPQLVEQVGILARER 193
Cdd:PLN02331 161 LATDTPEELAARVLHEEHQLYVEVVAALCEER 192
FMT_core_like_3 cd08653
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 73-187 4.61e-15

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: 68.78  E-value: 4.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987450986  73 DEALAEEIAGAEPDLVVCAGfMRILGEPVLTRLEGRIINTHPSLLPSFPGAHAV-RDALAAGATRAGATLFWVDAGVDTG 151
Cdd:cd08653   36 GPEVVAALRALAPDVVSVYG-CGIIKDALLAIPPLGVLNLHGGILPDYRGVHTGfWALANGDPDNVGVTVHLVDAGIDTG 114

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 987450986 152 EHIAQVEVPVLPGDTEESLTARVKAAETPQLVEQVG 187
Cdd:cd08653  115 DVLAQARPPLAAGDTLLSLYLRLYRAGVELMVEAIA 150
FMT_core_like_4 cd08651
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 73-184 2.59e-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: 187720 [Multi-domain]  Cd Length: 180  Bit Score: 67.68  E-value: 2.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987450986  73 DEALAEEIAGAEPDLVVCAGFMRILGEPVLTRLEGRIINTHPSLLPSFPGAHAVRDALAAGATRAGATLFWVDAGVDTGE 152
Cdd:cd08651   64 DEEIIEWIKEANPDIIFVFGWSQLLKPEILAIPRLGVIGFHPTKLPKNRGRAPIPWAILLGLKETASTFFWMDEGADSGD 143

                         90       100       110
                 ....*....|....*....|....*....|..
gi 987450986 153 HIAQVEVPVLPGDTEESLTARVKAAETPQLVE 184
Cdd:cd08651  144 ILSQEPFPIDKDDTANSLYDKIMEAAKQQIDK 175
PurU COG0788
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ...
 67-123 1.59e-13

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: 67.00  E-value: 1.59e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 987450986  67 ADRPAWDEALAEEIAGAEPDLVVCAGFMRILGEPVLTRLEGRIINTHPSLLPSFPGA 123
Cdd:COG0788  145 ETKAEAEARLLELLEEYDIDLVVLARYMQILSPDFCARLPGRIINIHHSFLPAFKGA 201
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
73-184 2.53e-13

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


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 66.67  E-value: 2.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987450986  73 DEALAEEIAGAEPDLVVCAGFMRILGEPVLTRLEGRIINTHPSLLPSFPGA----HAVRDalaagatragatLFWVDAGV 148
Cdd:COG0223   67 DPEFLEELRALNPDLIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAapiqWAILNgdte----tgvtIMQMDEGL 142

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 987450986 149 DTGEHIAQVEVPVLPGDTEESLTARVKAAETPQLVE 184
Cdd:COG0223  143 DTGDILLQEEVPIGPDDTAGSLHDKLAELGAELLLE 178
FMT_core_Met-tRNA-FMT_N cd08646
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ...
 73-173 5.57e-11

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: 58.99  E-value: 5.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987450986  73 DEALAEEIAGAEPDLVVCAGFMRILGEPVLTRLEGRIINTHPSLLPSFPGA----HA---------Vrdalaagatraga 139
Cdd:cd08646   67 DEEFLEELKALKPDLIVVVAYGQILPKEILDLPPYGCINVHPSLLPKYRGAapiqRAilngdketgV------------- 133

                         90       100       110
                 ....*....|....*....|....*....|....
gi 987450986 140 TLFWVDAGVDTGEHIAQVEVPVLPGDTEESLTAR 173
Cdd:cd08646  134 TIMKMDEGLDTGDILAQEEVPIDPDDTAGELLDK 167
FMT_core_Formyl-FH4-Hydrolase_C cd08648
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ...
 63-123 6.10e-11

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: 58.73  E-value: 6.10e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 987450986  63 PRDFADRPAWDEALAEEIAGAEPDLVVCAGFMRILGEPVLTRLEGRIINTHPSLLPSFPGA 123
Cdd:cd08648   55 PVTKDTKAEAEAEQLELLEEYGVDLVVLARYMQILSPDFVERYPNRIINIHHSFLPAFKGA 115
purU PRK06027
formyltetrahydrofolate deformylase; Reviewed
 67-123 6.27e-11

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 235676 [Multi-domain]  Cd Length: 286  Bit Score: 59.74  E-value: 6.27e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 987450986  67 ADRPAWDEALAEEIAGAEPDLVVCAGFMRILGEPVLTRLEGRIINTHPSLLPSFPGA 123
Cdd:PRK06027 148 ETKAEAEARLLELIDEYQPDLVVLARYMQILSPDFVARFPGRIINIHHSFLPAFKGA 204
fmt TIGR00460
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ...
 84-186 4.76e-08

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: 51.63  E-value: 4.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987450986   84 EPDLVVCAGFMRILGEPVLTRLEGRIINTHPSLLPSFPGAHAVRDALAAGATRAGATLFWVDAGVDTGEHIAQVEVPVLP 163
Cdd:TIGR00460  78 KPDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVPKMDAGDILKQETFPIEE 157

                          90       100
                  ....*....|....*....|...
gi 987450986  164 GDTEESLTARVkAAETPQLVEQV 186
Cdd:TIGR00460 158 EDNSGTLSDKL-SELGAQLLIET 179
purU PRK13010
formyltetrahydrofolate deformylase; Reviewed
 86-172 4.80e-07

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 139334 [Multi-domain]  Cd Length: 289  Bit Score: 48.64  E-value: 4.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987450986  86 DLVVCAGFMRILGEPVLTRLEGRIINTHPSLLPSFPGAHAVRDALAAGATRAGATLFWVDAGVDTGEHIAQVEVPVLPGD 165
Cdd:PRK13010 171 ELVVLARYMQVLSDDLSRKLSGRAINIHHSFLPGFKGARPYHQAHARGVKLIGATAHFVTDDLDEGPIIEQDVERVDHSY 250


                 ....*..
gi 987450986 166 TEESLTA 172
Cdd:PRK13010 251 SPEDLVA 257
PRK13011 PRK13011
formyltetrahydrofolate deformylase; Reviewed
 79-123 4.87e-07

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 237266 [Multi-domain]  Cd Length: 286  Bit Score: 48.83  E-value: 4.87e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 987450986  79 EIAGAEpdLVVCAGFMRILGEPVLTRLEGRIINTHPSLLPSFPGA 123
Cdd:PRK13011 162 EESGAE--LVVLARYMQVLSPELCRKLAGRAINIHHSFLPGFKGA 204
FMT_core_FDH_N cd08647
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ...
 70-173 5.99e-06

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: 45.13  E-value: 5.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987450986  70 PAW---DEALAEEIA-----GAEPD-LVVCAGF--MRILGEPVltrlEGRIInTHPSLLPSFPGAHAVRDALAAGATRAG 138
Cdd:cd08647   57 PRWrakGQAIPEVVAkykalGAELNvLPFCSQFipMEVIDAPK----HGSII-YHPSILPRHRGASAINWTLIHGDKKAG 131

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 987450986 139 ATLFWVDAGVDTGEHIAQVEVPVLPGDTEESLTAR 173
Cdd:cd08647  132 FTIFWADDGLDTGPILLQKECDVLPNDTVDTLYNR 166
FMT_core_like_5 cd08823
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 72-190 7.88e-06

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: 44.36  E-value: 7.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987450986  72 WDEALAEEIAGAEPDLVVCAGFMRILGEPVLTRLEGRIINTHPSLLPSFPGAHAVRDALAAGATRAGATLFWVDAGVDTG 151
Cdd:cd08823   59 LKEQLAEWLRALAADTVVVFTFPYRIPQHILDLPPLGFYNLHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMTAEIDRG 138

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 987450986 152 EHIAQVEVPVLPGDTEESLTARVKAAETPQLVEQVGILA 190
Cdd:cd08823  139 PIVLEQFTPIHPDDTYGLLCSRLAMLAVGLLEELYQNLA 177
PLN02285 PLN02285
methionyl-tRNA formyltransferase
 2-173 1.90e-05

methionyl-tRNA formyltransferase


Pssm-ID: 215159 [Multi-domain]  Cd Length: 334  Bit Score: 43.91  E-value: 1.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987450986   2 TGAGAARLVVLvsGT----GSNLVALLRACEDPAYGAEVVRVVADKPCP-GVGHALAAGVAASVVAPRDFADRP------ 70
Cdd:PLN02285   2 GSGRKKRLVFL--GTpevaATVLDALLDASQAPDSAFEVAAVVTQPPARrGRGRKLMPSPVAQLALDRGFPPDLiftpek 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987450986  71 AWDEALAEEIAGAEPDLVVCAGFMRILGEPVLTRLEGRIINTHPSLLPSFPGAHAV-RDALAAGATRAGATLFWVDAgVD 149
Cdd:PLN02285  80 AGEEDFLSALRELQPDLCITAAYGNILPQKFLDIPKLGTVNIHPSLLPLYRGAAPVqRALQDGVNETGVSVAFTVRA-LD 158

                        170       180
                 ....*....|....*....|....
gi 987450986 150 TGEHIAQVEVPVLPGDTEESLTAR 173
Cdd:PLN02285 159 AGPVIAQERVEVDEDIKAPELLPL 182
FMT_core_like_2 cd08822
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 86-186 2.23e-05

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: 43.22  E-value: 2.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987450986  86 DLVVCAGFMRILGEPVLTRLEGRIINTHPSLLPSFPGAHAVRDALAAGATRAGATLFWVDAGVDTGEHIAQVEVPVLPGD 165
Cdd:cd08822   68 DLIVAAHCHAFISAKTRARARLGAIGYHPSLLPRHRGRDAVEWTIRMRDPITGGTVYHLDDGVDGGPIAAQDWCHVRPGD 147

                         90       100
                 ....*....|....*....|.
gi 987450986 166 TEESLTARVKAAETPQLVEQV 186
Cdd:cd08822  148 TAAELWRRALAPMGVKLLTQV 168
PLN02828 PLN02828
formyltetrahydrofolate deformylase
 86-127 3.29e-05

formyltetrahydrofolate deformylase


Pssm-ID: 178422  Cd Length: 268  Bit Score: 43.20  E-value: 3.29e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 987450986  86 DLVVCAGFMRILGEPVLTRLEGRIINTHPSLLPSFPGAHAVR 127
Cdd:PLN02828 149 DFLVLARYMQILSGNFLKGYGKDIINIHHGLLPSFKGGNPSK 190
FMT_core_ArnA_N cd08644
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ...
 70-174 2.18e-03

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: 37.33  E-value: 2.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987450986  70 PAWDEALAEeiagAEPDLVVCAGFMRILGEPVLTRLEGRIINTHPSLLPSFPGAHAVRDALAAGATRAGATLFWVDAGVD 149
Cdd:cd08644   65 PEWVERLRA----LKPDLIFSFYYRHMISEDILEIARLGAFNLHGSLLPKYRGRAPLNWALINGETETGVTLHRMTKKPD 140

                         90       100
                 ....*....|....*....|....*
gi 987450986 150 TGEHIAQVEVPVLPGDTEESLTARV 174
Cdd:cd08644  141 AGAIVDQEKVPILPDDTAKSLFHKL 165
 
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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