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Conserved domains on  [gi|504410142|ref|WP_014597244|]
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MULTISPECIES: phosphoribosylglycinamide formyltransferase [Stutzerimonas]

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 ...
 6-203 5.05e-120

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: 338.93  E-value: 5.05e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142   6 NVVVLISGSGSNLQALIDSQHEGN-PARIRAVIANRADAFGLTRAKGAGIPTAVLDHKAFDGREAFDAALMELIDAHAPD 84
Cdd:COG0299    3 RIAVLISGRGSNLQALIDAIEAGDlPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYGPD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142  85 LVILAGFMRILSPGFVRHYHGRLLNIHPSLLPKYKGLDTHRRALEAGDAEHGCSVHFVTEELDGGPVVLQAALQVKPGDD 164
Cdd:COG0299   83 LVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDDT 162

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 504410142 165 IESLTQRVHVAEHQIYPLAMRWFAEGRLRLAEQGAMLDG 203
Cdd:COG0299  163 EETLAARILEQEHRLYPEAIRLLAEGRLTLDGRRVRLDG 201
 
Name Accession Description Interval E-value
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 6-203 5.05e-120

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: 338.93  E-value: 5.05e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142   6 NVVVLISGSGSNLQALIDSQHEGN-PARIRAVIANRADAFGLTRAKGAGIPTAVLDHKAFDGREAFDAALMELIDAHAPD 84
Cdd:COG0299    3 RIAVLISGRGSNLQALIDAIEAGDlPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYGPD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142  85 LVILAGFMRILSPGFVRHYHGRLLNIHPSLLPKYKGLDTHRRALEAGDAEHGCSVHFVTEELDGGPVVLQAALQVKPGDD 164
Cdd:COG0299   83 LVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDDT 162

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 504410142 165 IESLTQRVHVAEHQIYPLAMRWFAEGRLRLAEQGAMLDG 203
Cdd:COG0299  163 EETLAARILEQEHRLYPEAIRLLAEGRLTLDGRRVRLDG 201
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 6-187 7.11e-105

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: 299.69  E-value: 7.11e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142   6 NVVVLISGSGSNLQALIDSQHEGN-PARIRAVIANRADAFGLTRAKGAGIPTAVLDHKAFDGREAFDAALMELIDAHAPD 84
Cdd:cd08645    1 RIAVLASGSGSNLQALIDAIKSGKlNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142  85 LVILAGFMRILSPGFVRHYHGRLLNIHPSLLPKYKGLDTHRRALEAGDAEHGCSVHFVTEELDGGPVVLQAALQVKPGDD 164
Cdd:cd08645   81 LIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDT 160

                        170       180
                 ....*....|....*....|...
gi 504410142 165 IESLTQRVHVAEHQIYPLAMRWF 187
Cdd:cd08645  161 PETLAERIHALEHRLYPEAIKLL 183
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 6-193 1.74e-98

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: 283.88  E-value: 1.74e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142    6 NVVVLISGSGSNLQALIDSQHEGN-PARIRAVIANRADAFGLTRAKGAGIPTAVLDHKAFDGREAFDAALMELIDAHAPD 84
Cdd:TIGR00639   2 RIVVLISGNGSNLQAIIDACKEGKiPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEVD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142   85 LVILAGFMRILSPGFVRHYHGRLLNIHPSLLPKYKGLDTHRRALEAGDAEHGCSVHFVTEELDGGPVVLQAALQVKPGDD 164
Cdd:TIGR00639  82 LVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPEDT 161

                         170       180
                  ....*....|....*....|....*....
gi 504410142  165 IESLTQRVHVAEHQIYPLAMRWFAEGRLR 193
Cdd:TIGR00639 162 EETLEQRIHKQEHRIYPLAIAWFAQGRLK 190
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 6-183 2.01e-76

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: 227.56  E-value: 2.01e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142    6 NVVVLISGSGSNLQALIDSQHEGN-PARIRAVIANRADAFGLTRAKGAGIPTAVLDHKAFDGREAFDAALMELIDAHAPD 84
Cdd:pfam00551   2 KIAVLISGTGSNLQALIDALRKGGqDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAAD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142   85 LVILAGFMRILSPGFVRHYHGRLLNIHPSLLPKYKGLDTHRRALEAGDAEHGCSVHFVTEELDGGPVVLQAALQVKPGDD 164
Cdd:pfam00551  82 VIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDDT 161

                         170
                  ....*....|....*....
gi 504410142  165 IESLTQRVHVAEHQIYPLA 183
Cdd:pfam00551 162 AETLYNRVADLEHKALPRV 180
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 6-198 2.86e-33

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 118.64  E-value: 2.86e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142   6 NVVVLISGSGSNLQALIDSQHEGN-PARIRAVIANRADAFGLTRAKGAGIPTAVLDhKAFDGREAFDAAlmELIDA---H 81
Cdd:PLN02331   1 KLAVFVSGGGSNFRAIHDACLDGRvNGDVVVVVTNKPGCGGAEYARENGIPVLVYP-KTKGEPDGLSPD--ELVDAlrgA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142  82 APDLVILAGFMRILSPGFVRHYHGRLLNIHPSLLPK-----YKGLDTHRRALEAGDAEHGCSVHFVTEELDGGPVVLQAA 156
Cdd:PLN02331  78 GVDFVLLAGYLKLIPVELVRAYPRSILNIHPALLPAfggkgYYGIKVHKAVIASGARYSGPTVHFVDEHYDTGRILAQRV 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 504410142 157 LQVKPGDDIESLTQRVHVAEHQIYPLAMRWFAEGRLRLAEQG 198
Cdd:PLN02331 158 VPVLATDTPEELAARVLHEEHQLYVEVVAALCEERIVWREDG 199
 
Name Accession Description Interval E-value
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 6-203 5.05e-120

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: 338.93  E-value: 5.05e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142   6 NVVVLISGSGSNLQALIDSQHEGN-PARIRAVIANRADAFGLTRAKGAGIPTAVLDHKAFDGREAFDAALMELIDAHAPD 84
Cdd:COG0299    3 RIAVLISGRGSNLQALIDAIEAGDlPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYGPD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142  85 LVILAGFMRILSPGFVRHYHGRLLNIHPSLLPKYKGLDTHRRALEAGDAEHGCSVHFVTEELDGGPVVLQAALQVKPGDD 164
Cdd:COG0299   83 LVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDDT 162

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 504410142 165 IESLTQRVHVAEHQIYPLAMRWFAEGRLRLAEQGAMLDG 203
Cdd:COG0299  163 EETLAARILEQEHRLYPEAIRLLAEGRLTLDGRRVRLDG 201
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 6-187 7.11e-105

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: 299.69  E-value: 7.11e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142   6 NVVVLISGSGSNLQALIDSQHEGN-PARIRAVIANRADAFGLTRAKGAGIPTAVLDHKAFDGREAFDAALMELIDAHAPD 84
Cdd:cd08645    1 RIAVLASGSGSNLQALIDAIKSGKlNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142  85 LVILAGFMRILSPGFVRHYHGRLLNIHPSLLPKYKGLDTHRRALEAGDAEHGCSVHFVTEELDGGPVVLQAALQVKPGDD 164
Cdd:cd08645   81 LIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDT 160

                        170       180
                 ....*....|....*....|...
gi 504410142 165 IESLTQRVHVAEHQIYPLAMRWF 187
Cdd:cd08645  161 PETLAERIHALEHRLYPEAIKLL 183
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 6-193 1.74e-98

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: 283.88  E-value: 1.74e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142    6 NVVVLISGSGSNLQALIDSQHEGN-PARIRAVIANRADAFGLTRAKGAGIPTAVLDHKAFDGREAFDAALMELIDAHAPD 84
Cdd:TIGR00639   2 RIVVLISGNGSNLQAIIDACKEGKiPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEVD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142   85 LVILAGFMRILSPGFVRHYHGRLLNIHPSLLPKYKGLDTHRRALEAGDAEHGCSVHFVTEELDGGPVVLQAALQVKPGDD 164
Cdd:TIGR00639  82 LVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPEDT 161

                         170       180
                  ....*....|....*....|....*....
gi 504410142  165 IESLTQRVHVAEHQIYPLAMRWFAEGRLR 193
Cdd:TIGR00639 162 EETLEQRIHKQEHRIYPLAIAWFAQGRLK 190
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 6-183 2.01e-76

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: 227.56  E-value: 2.01e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142    6 NVVVLISGSGSNLQALIDSQHEGN-PARIRAVIANRADAFGLTRAKGAGIPTAVLDHKAFDGREAFDAALMELIDAHAPD 84
Cdd:pfam00551   2 KIAVLISGTGSNLQALIDALRKGGqDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAAD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142   85 LVILAGFMRILSPGFVRHYHGRLLNIHPSLLPKYKGLDTHRRALEAGDAEHGCSVHFVTEELDGGPVVLQAALQVKPGDD 164
Cdd:pfam00551  82 VIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDDT 161

                         170
                  ....*....|....*....
gi 504410142  165 IESLTQRVHVAEHQIYPLA 183
Cdd:pfam00551 162 AETLYNRVADLEHKALPRV 180
FMT_core cd08369
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...
 9-186 2.34e-37

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: 128.17  E-value: 2.34e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142   9 VLISGSGSNLQALIDSQHEGNPARIRAVIANRADAFGLTRAKGAGIPTAVLDHKAfdgreAFDAALMELIDAHAPDLVIL 88
Cdd:cd08369    1 IVILGSGNIGQRVLKALLSKEGHEIVGVVTHPDSPRGTAQLSLELVGGKVYLDSN-----INTPELLELLKEFAPDLIVS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142  89 AGFMRILSPGFVRHYHGRLLNIHPSLLPKYKGLDTHRRALEAGDAEHGCSVHFVTEELDGGPVVLQAALQVKPGDDIESL 168
Cdd:cd08369   76 INFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTAGTL 155

                        170
                 ....*....|....*...
gi 504410142 169 TQRVHVAEHQIYPLAMRW 186
Cdd:cd08369  156 YQRLIELGPKLLKEALQK 173
PurU COG0788
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ...
 6-191 5.35e-35

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: 125.16  E-value: 5.35e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142   6 NVVVLISGSGSNLQALIDSQHEGN-PARIRAVIANRADAFGLtrAKGAGIPTAVLDHKAfDGREAFDAALMELIDAHAPD 84
Cdd:COG0788   88 RVAILVSKEDHCLNDLLYRWRSGElPAEIPAVISNHPDLRPL--AEWFGIPFHHIPVTK-ETKAEAEARLLELLEEYDID 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142  85 LVILAGFMRILSPGFVRHYHGRLLNIHPSLLPKYKGLDTHRRALEAGDAEHGCSVHFVTEELDGGPVVLQAALQVKPGDD 164
Cdd:COG0788  165 LVVLARYMQILSPDFCARLPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVERVDHRDT 244

                        170       180
                 ....*....|....*....|....*..
gi 504410142 165 IESLTQRVHVAEHQIYPLAMRWFAEGR 191
Cdd:COG0788  245 PEDLVRKGRDVEKRVLARAVRWHLEDR 271
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 6-198 2.86e-33

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 118.64  E-value: 2.86e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142   6 NVVVLISGSGSNLQALIDSQHEGN-PARIRAVIANRADAFGLTRAKGAGIPTAVLDhKAFDGREAFDAAlmELIDA---H 81
Cdd:PLN02331   1 KLAVFVSGGGSNFRAIHDACLDGRvNGDVVVVVTNKPGCGGAEYARENGIPVLVYP-KTKGEPDGLSPD--ELVDAlrgA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142  82 APDLVILAGFMRILSPGFVRHYHGRLLNIHPSLLPK-----YKGLDTHRRALEAGDAEHGCSVHFVTEELDGGPVVLQAA 156
Cdd:PLN02331  78 GVDFVLLAGYLKLIPVELVRAYPRSILNIHPALLPAfggkgYYGIKVHKAVIASGARYSGPTVHFVDEHYDTGRILAQRV 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 504410142 157 LQVKPGDDIESLTQRVHVAEHQIYPLAMRWFAEGRLRLAEQG 198
Cdd:PLN02331 158 VPVLATDTPEELAARVLHEEHQLYVEVVAALCEERIVWREDG 199
FMT_core_Formyl-FH4-Hydrolase_C cd08648
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ...
 6-192 6.70e-33

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: 117.28  E-value: 6.70e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142   6 NVVVLISGSGSNLQALIDSQHEGN-PARIRAVIANRADAFGLtrAKGAGIPTAVLDHKAfDGREAFDAALMELIDAHAPD 84
Cdd:cd08648    2 RVAIFVSKEDHCLYDLLHRWREGElPCEIPLVISNHPDLRPL--AERFGIPFHHIPVTK-DTKAEAEAEQLELLEEYGVD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142  85 LVILAGFMRILSPGFVRHYHGRLLNIHPSLLPKYKGLDTHRRALEAGDAEHGCSVHFVTEELDGGPVVLQAALQVKPGDD 164
Cdd:cd08648   79 LVVLARYMQILSPDFVERYPNRIINIHHSFLPAFKGAKPYHQAFERGVKLIGATAHYVTEELDEGPIIEQDVERVSHRDS 158

                        170       180
                 ....*....|....*....|....*...
gi 504410142 165 IESLTQRVHVAEHQIYPLAMRWFAEGRL 192
Cdd:cd08648  159 VEDLVRKGRDIEKQVLARAVKWHLEDRV 186
purU PRK06027
formyltetrahydrofolate deformylase; Reviewed
 7-191 2.10e-28

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 235676 [Multi-domain]  Cd Length: 286  Bit Score: 107.89  E-value: 2.10e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142   7 VVVLISGSGSNLQALIDSQHEGN-PARIRAVIANRADAFGLTRAkgAGIPTAVLDHKAfDGREAFDAALMELIDAHAPDL 85
Cdd:PRK06027  92 VVILVSKEDHCLGDLLWRWRSGElPVEIAAVISNHDDLRSLVER--FGIPFHHVPVTK-ETKAEAEARLLELIDEYQPDL 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142  86 VILAGFMRILSPGFVRHYHGRLLNIHPSLLPKYKGLDTHRRALEAGDAEHGCSVHFVTEELDGGPVVLQAALQVKPGDDI 165
Cdd:PRK06027 169 VVLARYMQILSPDFVARFPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVIRVDHRDTA 248

                        170       180
                 ....*....|....*....|....*.
gi 504410142 166 ESLTQRVHVAEHQIYPLAMRWFAEGR 191
Cdd:PRK06027 249 EDLVRAGRDVEKQVLARAVRWHLEDR 274
PLN02828 PLN02828
formyltetrahydrofolate deformylase
 6-192 7.72e-23

formyltetrahydrofolate deformylase


Pssm-ID: 178422  Cd Length: 268  Bit Score: 92.89  E-value: 7.72e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142   6 NVVVLISGSGSNLQALIDSQHEGN-PARIRAVIAN--RADAFGLTR-AKGAGIPTAVLDHKAFDGREAfdaALMELIdaH 81
Cdd:PLN02828  72 KIAVLASKQDHCLIDLLHRWQDGRlPVDITCVISNheRGPNTHVMRfLERHGIPYHYLPTTKENKRED---EILELV--K 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142  82 APDLVILAGFMRILSPGFVRHYHGRLLNIHPSLLPKYKGLDTHRRALEAGDAEHGCSVHFVTEELDGGPVVLQAALQVKP 161
Cdd:PLN02828 147 GTDFLVLARYMQILSGNFLKGYGKDIINIHHGLLPSFKGGNPSKQAFDAGVKLIGATSHFVTEELDAGPIIEQMVERVSH 226

                        170       180       190
                 ....*....|....*....|....*....|.
gi 504410142 162 GDDIESLTQRVHVAEHQIYPLAMRWFAEGRL 192
Cdd:PLN02828 227 RDNLRSFVQKSENLEKQCLAKAIKSYCELRV 257
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
18-175 2.05e-21

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


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 89.78  E-value: 2.05e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142  18 LQALIDSQHEgnparIRAVIANRADAFGLTR----------AKGAGIPtaVLDHKAFDgreafDAALMELIDAHAPDLVI 87
Cdd:COG0223   16 LEALLAAGHE-----VVAVVTQPDRPAGRGRkltpspvkelALEHGIP--VLQPESLK-----DPEFLEELRALNPDLIV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142  88 LAGFMRILSPGFVRHYHGRLLNIHPSLLPKYKGLDTHRRALEAGDAEHGCSVHFVTEELDGGPVVLQAALQVKPGDDIES 167
Cdd:COG0223   84 VVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDTGDILLQEEVPIGPDDTAGS 163


                 ....*...
gi 504410142 168 LTQRVHVA 175
Cdd:COG0223  164 LHDKLAEL 171
PRK13011 PRK13011
formyltetrahydrofolate deformylase; Reviewed
 7-191 1.32e-19

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 237266 [Multi-domain]  Cd Length: 286  Bit Score: 84.26  E-value: 1.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142   7 VVVLISGSGSNLQALIDSQHEGN-PARIRAVIANRADAFGLtrAKGAGIP------TAvldhkafDGREAFDAALMELID 79
Cdd:PRK13011  92 VLIMVSKFDHCLNDLLYRWRIGElPMDIVGVVSNHPDLEPL--AAWHGIPfhhfpiTP-------DTKPQQEAQVLDVVE 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142  80 AHAPDLVILAGFMRILSPGFVRHYHGRLLNIHPSLLPKYKGLDTHRRALEAGDAEHGCSVHFVTEELDGGPVVLQAALQV 159
Cdd:PRK13011 163 ESGAELVVLARYMQVLSPELCRKLAGRAINIHHSFLPGFKGAKPYHQAYERGVKLIGATAHYVTDDLDEGPIIEQDVERV 242

                        170       180       190
                 ....*....|....*....|....*....|..
gi 504410142 160 KPGDDIESLTQRVHVAEHQIYPLAMRWFAEGR 191
Cdd:PRK13011 243 DHAYSPEDLVAKGRDVECLTLARAVKAHIERR 274
FMT_core_like_3 cd08653
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 71-172 2.38e-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: 80.72  E-value: 2.38e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142  71 DAALMELIDAHAPDLVILAGfMRILSPGFVRHYHGRLLNIHPSLLPKYKGLDTHRRALEAGDAEH-GCSVHFVTEELDGG 149
Cdd:cd08653   36 GPEVVAALRALAPDVVSVYG-CGIIKDALLAIPPLGVLNLHGGILPDYRGVHTGFWALANGDPDNvGVTVHLVDAGIDTG 114

                         90       100
                 ....*....|....*....|...
gi 504410142 150 PVVLQAALQVKPGDDIESLTQRV 172
Cdd:cd08653  115 DVLAQARPPLAAGDTLLSLYLRL 137
purU PRK13010
formyltetrahydrofolate deformylase; Reviewed
 7-192 8.35e-18

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 139334 [Multi-domain]  Cd Length: 289  Bit Score: 79.45  E-value: 8.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142   7 VVVLISGSGSNLQALIDSQHEGN-PARIRAVIANRADAFGLtrAKGAGIPTAVLDhKAFDGREAFDAALMELIDAHAPDL 85
Cdd:PRK13010  96 VVIMVSKFDHCLNDLLYRWRMGElDMDIVGIISNHPDLQPL--AVQHDIPFHHLP-VTPDTKAQQEAQILDLIETSGAEL 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142  86 VILAGFMRILSPGFVRHYHGRLLNIHPSLLPKYKGLDTHRRALEAGDAEHGCSVHFVTEELDGGPVVLQAALQVKPGDDI 165
Cdd:PRK13010 173 VVLARYMQVLSDDLSRKLSGRAINIHHSFLPGFKGARPYHQAHARGVKLIGATAHFVTDDLDEGPIIEQDVERVDHSYSP 252

                        170       180
                 ....*....|....*....|....*..
gi 504410142 166 ESLTQRVHVAEHQIYPLAMRWFAEGRL 192
Cdd:PRK13010 253 EDLVAKGRDVECLTLARAVKAFIEHRV 279
FMT_core_Met-tRNA-FMT_N cd08646
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ...
 18-171 3.94e-17

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: 76.33  E-value: 3.94e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142  18 LQALIDSQHEgnparIRAVIANRADAFG----LT------RAKGAGIPtaVLDHKAFDGREAFdaalmELIDAHAPDLVI 87
Cdd:cd08646   16 LEALLKSGHE-----VVAVVTQPDKPRGrgkkLTpspvkeLALELGLP--VLQPEKLKDEEFL-----EELKALKPDLIV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142  88 LAGFMRILSPGFVRHYHGRLLNIHPSLLPKYKG---LdthRRALEAGDAEHGCSVHFVTEELDGGPVVLQAALQVKPGDD 164
Cdd:cd08646   84 VVAYGQILPKEILDLPPYGCINVHPSLLPKYRGaapI---QRAILNGDKETGVTIMKMDEGLDTGDILAQEEVPIDPDDT 160


                 ....*..
gi 504410142 165 IESLTQR 171
Cdd:cd08646  161 AGELLDK 167
PLN02285 PLN02285
methionyl-tRNA formyltransferase
 20-161 1.07e-16

methionyl-tRNA formyltransferase


Pssm-ID: 215159 [Multi-domain]  Cd Length: 334  Bit Score: 77.04  E-value: 1.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142  20 ALIDSQHEGNPARIRAVIANRADAFGLTRakgaGIPTAVLDHKAFDGREAFDAALMELidahAPDLVILAGFMRILSPGF 99
Cdd:PLN02285  39 AAVVTQPPARRGRGRKLMPSPVAQLALDR----GFPPDLIFTPEKAGEEDFLSALREL----QPDLCITAAYGNILPQKF 110

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504410142 100 VRHYHGRLLNIHPSLLPKYKGLDTHRRALEAGDAEHGCSVHFVTEELDGGPVVLQAALQVKP 161
Cdd:PLN02285 111 LDIPKLGTVNIHPSLLPLYRGAAPVQRALQDGVNETGVSVAFTVRALDAGPVIAQERVEVDE 172
fmt TIGR00460
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ...
 83-199 1.02e-12

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: 65.50  E-value: 1.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142   83 PDLVILAGFMRILSPGFVRHYHGRLLNIHPSLLPKYKGLDTHRRALEAGDAEHGCSVHFVTEELDGGPVVLQAALQVKPG 162
Cdd:TIGR00460  79 PDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVPKMDAGDILKQETFPIEEE 158

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 504410142  163 DDIESLTQRVHVAEHQIYPLAMRWFAEGRLRLAEQGA 199
Cdd:TIGR00460 159 DNSGTLSDKLSELGAQLLIETLKELPEGKNKPEPQDA 195
FMT_core_like_5 cd08823
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 74-172 7.98e-11

Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.


Pssm-ID: 187725 [Multi-domain]  Cd Length: 177  Bit Score: 58.61  E-value: 7.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142  74 LMELIDAHAPDLVILAGFMRILsPGFVRHYHGR-LLNIHPSLLPKYKGLDTHRRALEAGDAEHGCSVHFVTEELDGGPVV 152
Cdd:cd08823   63 LAEWLRALAADTVVVFTFPYRI-PQHILDLPPLgFYNLHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMTAEIDRGPIV 141

                         90       100
                 ....*....|....*....|
gi 504410142 153 LQAALQVKPGDDIESLTQRV 172
Cdd:cd08823  142 LEQFTPIHPDDTYGLLCSRL 161
FMT_core_FDH_N cd08647
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ...
 48-204 1.11e-08

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: 53.22  E-value: 1.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142  48 RAKGAGIPTAVLDHKAFdGRE----AFDAAL--MELIDAHApdlvilagfmrilspgfvrhyHGRLLnIHPSLLPKYKGL 121
Cdd:cd08647   60 RAKGQAIPEVVAKYKAL-GAElnvlPFCSQFipMEVIDAPK---------------------HGSII-YHPSILPRHRGA 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142 122 DTHRRALEAGDAEHGCSVHFVTEELDGGPVVLQAALQVKPGDDIESLTQRVhvaehqIYP-------LAMRWFAEG---R 191
Cdd:cd08647  117 SAINWTLIHGDKKAGFTIFWADDGLDTGPILLQKECDVLPNDTVDTLYNRF------LYPegikamvEAVRLIAEGkapR 190

                        170
                 ....*....|...
gi 504410142 192 LRLAEQGAMLDGV 204
Cdd:cd08647  191 IPQPEEGATYEGI 203
FMT_core_ArnA_N cd08644
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ...
 108-179 6.21e-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: 50.81  E-value: 6.21e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504410142 108 LNIHPSLLPKYKGLDTHRRALEAGDAEHGCSVHFVTEELDGGPVVLQAALQVKPGDDIESLTQRVHVAEHQI 179
Cdd:cd08644  101 FNLHGSLLPKYRGRAPLNWALINGETETGVTLHRMTKKPDAGAIVDQEKVPILPDDTAKSLFHKLCVAARRL 172
FMT_core_NRPS_like cd08649
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ...
 10-169 3.71e-07

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: 48.02  E-value: 3.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142  10 LISGSGSNL----QALIDSQHegnpaRIRAVIAnrADAFGLTRAKGAGIPtavldhkAFDGREAFDAALMElidaHAPDL 85
Cdd:cd08649    3 VIIGGGTLLiqcaEQLLAAGH-----RIAAVVS--TDPAIRAWAAAEGIA-------VLEPGEALEELLSD----EPFDW 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142  86 VILAGFMRILSPGFVRHYHGRLLNIHPSLLPKYKGLDTHRRALEAGDAEHGCSVHFVTEELDGGPVVLQAALQVKPGDDI 165
Cdd:cd08649   65 LFSIVNLRILPSEVLALPRKGAINFHDGPLPRYAGLNATSWALLAGETRHGVTWHRIEEGVDAGDILVQRPFDIAPDDTA 144


                 ....
gi 504410142 166 ESLT 169
Cdd:cd08649  145 LSLN 148
FMT_core_like_4 cd08651
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 71-172 5.21e-07

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: 48.03  E-value: 5.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142  71 DAALMELIDAHAPDLVILAGFMRILSPGFVRHYHGRLLNIHPSLLPKYKGldthrRA-----LEAGDAEHGCSVHFVTEE 145
Cdd:cd08651   64 DEEIIEWIKEANPDIIFVFGWSQLLKPEILAIPRLGVIGFHPTKLPKNRG-----RApipwaILLGLKETASTFFWMDEG 138

                         90       100
                 ....*....|....*....|....*..
gi 504410142 146 LDGGPVVLQAALQVKPGDDIESLTQRV 172
Cdd:cd08651  139 ADSGDILSQEPFPIDKDDTANSLYDKI 165
FMT_core_like_2 cd08822
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 79-200 1.32e-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: 187724 [Multi-domain]  Cd Length: 192  Bit Score: 47.07  E-value: 1.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142  79 DAHAP--DLVILAGFMRILSPGFVRHYHGRLLNIHPSLLPKYKGLDTHRRALEAGDAEHGCSVHFVTEELDGGPVVLQAA 156
Cdd:cd08822   61 DAIPPgtDLIVAAHCHAFISAKTRARARLGAIGYHPSLLPRHRGRDAVEWTIRMRDPITGGTVYHLDDGVDGGPIAAQDW 140

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 504410142 157 LQVKPGDDIESLTQRVhvaehqIYPLAMRWFAEGRLRLAEQGAM 200
Cdd:cd08822  141 CHVRPGDTAAELWRRA------LAPMGVKLLTQVIDALLRGGNL 178
PRK08125 PRK08125
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ...
 108-197 5.20e-06

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


Pssm-ID: 236156 [Multi-domain]  Cd Length: 660  Bit Score: 46.51  E-value: 5.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142 108 LNIHPSLLPKYKGLDTHRRALEAGDAEHGCSVHFVTEELDGGPVVLQAALQVKPGDDIESLTQRVHVAEHQIYPLAMRWF 187
Cdd:PRK08125 101 FNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQQRVAIAPDDTALTLHHKLCHAARQLLEQTLPAI 180

                         90
                 ....*....|
gi 504410142 188 AEGRLRLAEQ 197
Cdd:PRK08125 181 KHGNIPEIPQ 190
PRK06988 PRK06988
formyltransferase;
71-179 8.31e-06

formyltransferase;


Pssm-ID: 235902 [Multi-domain]  Cd Length: 312  Bit Score: 45.45  E-value: 8.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142  71 DAALMELIDAHAPDlVILAGFMR-ILSPGFVRHYHGRLLNIHPSLLPKYKGLDTHRRALEAGDAEHGCSVHFVTEELDGG 149
Cdd:PRK06988  66 DPELRAAVAAAAPD-FIFSFYYRhMIPVDLLALAPRGAYNMHGSLLPKYRGRVPVNWAVLNGETETGATLHEMVAKPDAG 144

                         90       100       110
                 ....*....|....*....|....*....|
gi 504410142 150 PVVLQAALQVKPGDDIESLTQRVHVAEHQI 179
Cdd:PRK06988 145 AIVDQTAVPILPDDTAAQVFDKVTVAAEQT 174
FMT_core_like_6 cd08820
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 74-175 1.19e-04

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: 41.27  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410142  74 LMELIDAHAPDLVILAGFMRILSPGFVRHYHGRLLNIHPSLLPKYKGLDTHRRALEAGDAEHGCSVHFVTEELDGGPVVL 153
Cdd:cd08820   61 LLEILENKGVDILISVQYHWILPGSILEKAKEIAFNLHNAPLPEYRGCNQFSHAILNGDDQFGTTIHWMAEGIDSGDIIF 140

                         90       100
                 ....*....|....*....|..
gi 504410142 154 QAALQVKPGDDIESLTQRVHVA 175
Cdd:cd08820  141 EKRFPIPSDCTVISLYILAHYA 162
 
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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