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Conserved domains on  [gi|2544519349|ref|WP_300307743|]
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phosphoribosylglycinamide formyltransferase [Candidatus Thioglobus sp.]

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 ...
 1-199 1.48e-113

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: 321.98  E-value: 1.48e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349   1 MKGVVLISGSGSNLQSIID--NANDINLDIEAVISNKEAAYGLERAKKANITTHTLDHKQFSSREAFDQNLSQLIDQYNP 78
Cdd:COG0299     2 KRIAVLISGRGSNLQALIDaiEAGDLPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYGP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349  79 GVIILAGFMRILTEEFTQKYTGKMLNIHPSLLPKFQGLNTHQRAIDAKETEHGVTIHFVTAELDGGPIIAQSQIKVLEDD 158
Cdd:COG0299    82 DLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDD 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2544519349 159 SAESLAKRVLIEEHKLFPKVIHWFTQNQLKLNDNKVTLDGK 199
Cdd:COG0299   162 TEETLAARILEQEHRLYPEAIRLLAEGRLTLDGRRVRLDGE 202
 
Name Accession Description Interval E-value
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 1-199 1.48e-113

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: 321.98  E-value: 1.48e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349   1 MKGVVLISGSGSNLQSIID--NANDINLDIEAVISNKEAAYGLERAKKANITTHTLDHKQFSSREAFDQNLSQLIDQYNP 78
Cdd:COG0299     2 KRIAVLISGRGSNLQALIDaiEAGDLPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYGP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349  79 GVIILAGFMRILTEEFTQKYTGKMLNIHPSLLPKFQGLNTHQRAIDAKETEHGVTIHFVTAELDGGPIIAQSQIKVLEDD 158
Cdd:COG0299    82 DLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDD 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2544519349 159 SAESLAKRVLIEEHKLFPKVIHWFTQNQLKLNDNKVTLDGK 199
Cdd:COG0299   162 TEETLAARILEQEHRLYPEAIRLLAEGRLTLDGRRVRLDGE 202
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 4-182 5.13e-99

Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); Phosphoribosylglycinamide formyltransferase, also known as GAR transformylase or GART, is an essential enzyme that catalyzes the third step in de novo purine biosynthesis. This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. In prokaryotes, GART is a single domain protein but in most eukaryotes it is the C-terminal portion of a large multifunctional protein which also contains GAR synthetase and aminoimidazole ribonucleotide synthetase activities.


Pssm-ID: 187714 [Multi-domain]  Cd Length: 183  Bit Score: 284.28  E-value: 5.13e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349   4 VVLISGSGSNLQSIID--NANDINLDIEAVISNKEAAYGLERAKKANITTHTLDHKQFSSREAFDQNLSQLIDQYNPGVI 81
Cdd:cd08645     3 AVLASGSGSNLQALIDaiKSGKLNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKVDLI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349  82 ILAGFMRILTEEFTQKYTGKMLNIHPSLLPKFQGLNTHQRAIDAKETEHGVTIHFVTAELDGGPIIAQSQIKVLEDDSAE 161
Cdd:cd08645    83 VLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDTPE 162

                         170       180
                  ....*....|....*....|.
gi 2544519349 162 SLAKRVLIEEHKLFPKVIHWF 182
Cdd:cd08645   163 TLAERIHALEHRLYPEAIKLL 183
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 1-188 2.92e-84

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: 247.28  E-value: 2.92e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349   1 MKGVVLISGSGSNLQSIIDNA--NDINLDIEAVISNKEAAYGLERAKKANITTHTLDHKQFSSREAFDQNLSQLIDQYNP 78
Cdd:TIGR00639   1 KRIVVLISGNGSNLQAIIDACkeGKIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349  79 GVIILAGFMRILTEEFTQKYTGKMLNIHPSLLPKFQGLNTHQRAIDAKETEHGVTIHFVTAELDGGPIIAQSQIKVLEDD 158
Cdd:TIGR00639  81 DLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPED 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 2544519349 159 SAESLAKRVLIEEHKLFPKVIHWFTQNQLK 188
Cdd:TIGR00639 161 TEETLEQRIHKQEHRIYPLAIAWFAQGRLK 190
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 1-179 1.66e-72

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: 217.16  E-value: 1.66e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349   1 MKGVVLISGSGSNLQSIID--NANDINLDIEAVISNKEAAYGLERAKKANITTHTLDHKQFSSREAFDQNLSQLIDQYNP 78
Cdd:pfam00551   1 MKIAVLISGTGSNLQALIDalRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349  79 GVIILAGFMRILTEEFTQKYTGKMLNIHPSLLPKFQGLNTHQRAIDAKETEHGVTIHFVTAELDGGPIIAQSQIKVLEDD 158
Cdd:pfam00551  81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160

                         170       180
                  ....*....|....*....|.
gi 2544519349 159 SAESLAKRVLIEEHKLFPKVI 179
Cdd:pfam00551 161 TAETLYNRVADLEHKALPRVL 181
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 4-179 3.32e-40

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 135.98  E-value: 3.32e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349   4 VVLISGSGSNLQSIIDNA--NDINLDIEAVISNKEAAYGLERAKKANITTHTLDHKQFSsreafDQNLS--QLIDQ---Y 76
Cdd:PLN02331    3 AVFVSGGGSNFRAIHDACldGRVNGDVVVVVTNKPGCGGAEYARENGIPVLVYPKTKGE-----PDGLSpdELVDAlrgA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349  77 NPGVIILAGFMRILTEEFTQKYTGKMLNIHPSLLPKF-----QGLNTHQRAIDAKETEHGVTIHFVTAELDGGPIIAQSQ 151
Cdd:PLN02331   78 GVDFVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFggkgyYGIKVHKAVIASGARYSGPTVHFVDEHYDTGRILAQRV 157

                         170       180
                  ....*....|....*....|....*...
gi 2544519349 152 IKVLEDDSAESLAKRVLIEEHKLFPKVI 179
Cdd:PLN02331  158 VPVLATDTPEELAARVLHEEHQLYVEVV 185
 
Name Accession Description Interval E-value
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 1-199 1.48e-113

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: 321.98  E-value: 1.48e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349   1 MKGVVLISGSGSNLQSIID--NANDINLDIEAVISNKEAAYGLERAKKANITTHTLDHKQFSSREAFDQNLSQLIDQYNP 78
Cdd:COG0299     2 KRIAVLISGRGSNLQALIDaiEAGDLPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYGP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349  79 GVIILAGFMRILTEEFTQKYTGKMLNIHPSLLPKFQGLNTHQRAIDAKETEHGVTIHFVTAELDGGPIIAQSQIKVLEDD 158
Cdd:COG0299    82 DLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDD 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2544519349 159 SAESLAKRVLIEEHKLFPKVIHWFTQNQLKLNDNKVTLDGK 199
Cdd:COG0299   162 TEETLAARILEQEHRLYPEAIRLLAEGRLTLDGRRVRLDGE 202
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 4-182 5.13e-99

Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); Phosphoribosylglycinamide formyltransferase, also known as GAR transformylase or GART, is an essential enzyme that catalyzes the third step in de novo purine biosynthesis. This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. In prokaryotes, GART is a single domain protein but in most eukaryotes it is the C-terminal portion of a large multifunctional protein which also contains GAR synthetase and aminoimidazole ribonucleotide synthetase activities.


Pssm-ID: 187714 [Multi-domain]  Cd Length: 183  Bit Score: 284.28  E-value: 5.13e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349   4 VVLISGSGSNLQSIID--NANDINLDIEAVISNKEAAYGLERAKKANITTHTLDHKQFSSREAFDQNLSQLIDQYNPGVI 81
Cdd:cd08645     3 AVLASGSGSNLQALIDaiKSGKLNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKVDLI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349  82 ILAGFMRILTEEFTQKYTGKMLNIHPSLLPKFQGLNTHQRAIDAKETEHGVTIHFVTAELDGGPIIAQSQIKVLEDDSAE 161
Cdd:cd08645    83 VLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDTPE 162

                         170       180
                  ....*....|....*....|.
gi 2544519349 162 SLAKRVLIEEHKLFPKVIHWF 182
Cdd:cd08645   163 TLAERIHALEHRLYPEAIKLL 183
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 1-188 2.92e-84

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: 247.28  E-value: 2.92e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349   1 MKGVVLISGSGSNLQSIIDNA--NDINLDIEAVISNKEAAYGLERAKKANITTHTLDHKQFSSREAFDQNLSQLIDQYNP 78
Cdd:TIGR00639   1 KRIVVLISGNGSNLQAIIDACkeGKIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349  79 GVIILAGFMRILTEEFTQKYTGKMLNIHPSLLPKFQGLNTHQRAIDAKETEHGVTIHFVTAELDGGPIIAQSQIKVLEDD 158
Cdd:TIGR00639  81 DLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPED 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 2544519349 159 SAESLAKRVLIEEHKLFPKVIHWFTQNQLK 188
Cdd:TIGR00639 161 TEETLEQRIHKQEHRIYPLAIAWFAQGRLK 190
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 1-179 1.66e-72

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: 217.16  E-value: 1.66e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349   1 MKGVVLISGSGSNLQSIID--NANDINLDIEAVISNKEAAYGLERAKKANITTHTLDHKQFSSREAFDQNLSQLIDQYNP 78
Cdd:pfam00551   1 MKIAVLISGTGSNLQALIDalRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349  79 GVIILAGFMRILTEEFTQKYTGKMLNIHPSLLPKFQGLNTHQRAIDAKETEHGVTIHFVTAELDGGPIIAQSQIKVLEDD 158
Cdd:pfam00551  81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160

                         170       180
                  ....*....|....*....|.
gi 2544519349 159 SAESLAKRVLIEEHKLFPKVI 179
Cdd:pfam00551 161 TAETLYNRVADLEHKALPRVL 181
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 4-179 3.32e-40

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 135.98  E-value: 3.32e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349   4 VVLISGSGSNLQSIIDNA--NDINLDIEAVISNKEAAYGLERAKKANITTHTLDHKQFSsreafDQNLS--QLIDQ---Y 76
Cdd:PLN02331    3 AVFVSGGGSNFRAIHDACldGRVNGDVVVVVTNKPGCGGAEYARENGIPVLVYPKTKGE-----PDGLSpdELVDAlrgA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349  77 NPGVIILAGFMRILTEEFTQKYTGKMLNIHPSLLPKF-----QGLNTHQRAIDAKETEHGVTIHFVTAELDGGPIIAQSQ 151
Cdd:PLN02331   78 GVDFVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFggkgyYGIKVHKAVIASGARYSGPTVHFVDEHYDTGRILAQRV 157

                         170       180
                  ....*....|....*....|....*...
gi 2544519349 152 IKVLEDDSAESLAKRVLIEEHKLFPKVI 179
Cdd:PLN02331  158 VPVLATDTPEELAARVLHEEHQLYVEVV 185
FMT_core cd08369
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...
 5-179 1.61e-38

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: 130.49  E-value: 1.61e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349   5 VLISGSGSNLQSIIDNANDINL-DIEAVISNKEAAYGLERAKKANITthtldHKQFSSREAFDQNLSQLIDQYNPGVIIL 83
Cdd:cd08369     1 IVILGSGNIGQRVLKALLSKEGhEIVGVVTHPDSPRGTAQLSLELVG-----GKVYLDSNINTPELLELLKEFAPDLIVS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349  84 AGFMRILTEEFTQKYTGKMLNIHPSLLPKFQGLNTHQRAIDAKETEHGVTIHFVTAELDGGPIIAQSQIKVLEDDSAESL 163
Cdd:cd08369    76 INFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTAGTL 155

                         170
                  ....*....|....*.
gi 2544519349 164 AKRVLIEEHKLFPKVI 179
Cdd:cd08369   156 YQRLIELGPKLLKEAL 171
PurU COG0788
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ...
 21-194 1.48e-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: 125.93  E-value: 1.48e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349  21 ANDINLDIEAVISNKEAAYGLerAKKANITTHTLDHKQfSSREAFDQNLSQLIDQYNPGVIILAGFMRILTEEFTQKYTG 100
Cdd:COG0788   109 SGELPAEIPAVISNHPDLRPL--AEWFGIPFHHIPVTK-ETKAEAEARLLELLEEYDIDLVVLARYMQILSPDFCARLPG 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349 101 KMLNIHPSLLPKFQGLNTHQRAIdaketEHGV-----TIHFVTAELDGGPIIAQSQIKVLEDDSAESLA-------KRVL 168
Cdd:COG0788   186 RIINIHHSFLPAFKGAKPYHQAY-----ERGVkligaTAHYVTADLDEGPIIEQDVERVDHRDTPEDLVrkgrdveKRVL 260

                         170       180
                  ....*....|....*....|....*.
gi 2544519349 169 IEehklfpkVIHWFTQNQLKLNDNKV 194
Cdd:COG0788   261 AR-------AVRWHLEDRVLVNGNKT 279
purU PRK06027
formyltetrahydrofolate deformylase; Reviewed
 21-193 2.15e-31

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 235676 [Multi-domain]  Cd Length: 286  Bit Score: 115.20  E-value: 2.15e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349  21 ANDINLDIEAVISNKEAAYGLerAKKANITTHTLDHKQFSSREAFDQnLSQLIDQYNPGVIILAGFMRILTEEFTQKYTG 100
Cdd:PRK06027  112 SGELPVEIAAVISNHDDLRSL--VERFGIPFHHVPVTKETKAEAEAR-LLELIDEYQPDLVVLARYMQILSPDFVARFPG 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349 101 KMLNIHPSLLPKFQGLNTHQRAidakeTEHGV-----TIHFVTAELDGGPIIAQSQIKVLEDDSAESLA-------KRVL 168
Cdd:PRK06027  189 RIINIHHSFLPAFKGAKPYHQA-----YERGVkligaTAHYVTADLDEGPIIEQDVIRVDHRDTAEDLVragrdveKQVL 263

                         170       180
                  ....*....|....*....|....*
gi 2544519349 169 ieehklfPKVIHWFTQNQLKLNDNK 193
Cdd:PRK06027  264 -------ARAVRWHLEDRVLVYGNK 281
FMT_core_Formyl-FH4-Hydrolase_C cd08648
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ...
 20-195 8.45e-31

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: 111.50  E-value: 8.45e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349  20 NANDINLDIEAVISNKEAAYGLerAKKANITTHTLDHKQFSSREAFDQNLsQLIDQYNPGVIILAGFMRILTEEFTQKYT 99
Cdd:cd08648    22 REGELPCEIPLVISNHPDLRPL--AERFGIPFHHIPVTKDTKAEAEAEQL-ELLEEYGVDLVVLARYMQILSPDFVERYP 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349 100 GKMLNIHPSLLPKFQGLNTHQRAIDAKETEHGVTIHFVTAELDGGPIIAQSQIKVLEDDSAESLA-------KRVLIeeh 172
Cdd:cd08648    99 NRIINIHHSFLPAFKGAKPYHQAFERGVKLIGATAHYVTEELDEGPIIEQDVERVSHRDSVEDLVrkgrdieKQVLA--- 175

                         170       180
                  ....*....|....*....|...
gi 2544519349 173 klfpKVIHWFTQNQLKLNDNKVT 195
Cdd:cd08648   176 ----RAVKWHLEDRVLVYGNKTV 194
purU PRK13010
formyltetrahydrofolate deformylase; Reviewed
 23-193 1.19e-21

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 139334 [Multi-domain]  Cd Length: 289  Bit Score: 89.47  E-value: 1.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349  23 DINLDIEAVISNKEAAygLERAKKANITTH----TLDHKqfSSREAfdqNLSQLIDQYNPGVIILAGFMRILTEEFTQKY 98
Cdd:PRK13010  118 ELDMDIVGIISNHPDL--QPLAVQHDIPFHhlpvTPDTK--AQQEA---QILDLIETSGAELVVLARYMQVLSDDLSRKL 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349  99 TGKMLNIHPSLLPKFQGLNTHQRAIDAKETEHGVTIHFVTAELDGGPIIAQSQIKVLEDDSAESLAKRVLIEEHKLFPKV 178
Cdd:PRK13010  191 SGRAINIHHSFLPGFKGARPYHQAHARGVKLIGATAHFVTDDLDEGPIIEQDVERVDHSYSPEDLVAKGRDVECLTLARA 270

                         170
                  ....*....|....*
gi 2544519349 179 IHWFTQNQLKLNDNK 193
Cdd:PRK13010  271 VKAFIEHRVFINGDR 285
PRK13011 PRK13011
formyltetrahydrofolate deformylase; Reviewed
 23-194 1.27e-21

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 237266 [Multi-domain]  Cd Length: 286  Bit Score: 89.27  E-value: 1.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349  23 DINLDIEAVISNKEAAYGLerAKKANITTH----TLDHKqfSSREAfdqNLSQLIDQYNPGVIILAGFMRILTEEFTQKY 98
Cdd:PRK13011  114 ELPMDIVGVVSNHPDLEPL--AAWHGIPFHhfpiTPDTK--PQQEA---QVLDVVEESGAELVVLARYMQVLSPELCRKL 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349  99 TGKMLNIHPSLLPKFQGLNTHQRAIDAKETEHGVTIHFVTAELDGGPIIAQSQIKVLEDDSAESL-AKRVLIEEHKLFpK 177
Cdd:PRK13011  187 AGRAINIHHSFLPGFKGAKPYHQAYERGVKLIGATAHYVTDDLDEGPIIEQDVERVDHAYSPEDLvAKGRDVECLTLA-R 265

                         170
                  ....*....|....*..
gi 2544519349 178 VIHWFTQNQLKLNDNKV 194
Cdd:PRK13011  266 AVKAHIERRVFLNGNRT 282
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
42-167 5.55e-21

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


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 87.85  E-value: 5.55e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349  42 ERAKKANITTHTldHKQFSSREAFDQnlsqlIDQYNPGVIILAGFMRILTEEFTQKYTGKMLNIHPSLLPKFQGLNTHQR 121
Cdd:COG0223    50 ELALEHGIPVLQ--PESLKDPEFLEE-----LRALNPDLIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAAPIQW 122

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2544519349 122 AIDAKETEHGVTIHFVTAELDGGPIIAQSQIKVLEDDSAESLAKRV 167
Cdd:COG0223   123 AILNGDTETGVTIMQMDEGLDTGDILLQEEVPIGPDDTAGSLHDKL 168
FMT_core_like_3 cd08653
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 71-180 2.17e-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: 80.33  E-value: 2.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349  71 QLIDQYNPGVIILAGfMRILTEEFTQKYTGKMLNIHPSLLPKFQGLNTHQRAIDAKETEH-GVTIHFVTAELDGGPIIAQ 149
Cdd:cd08653    41 AALRALAPDVVSVYG-CGIIKDALLAIPPLGVLNLHGGILPDYRGVHTGFWALANGDPDNvGVTVHLVDAGIDTGDVLAQ 119

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2544519349 150 SQIKVLEDDSAESLAKRVLIEEHKLFPKVIH 180
Cdd:cd08653   120 ARPPLAAGDTLLSLYLRLYRAGVELMVEAIA 150
FMT_core_Met-tRNA-FMT_N cd08646
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ...
 42-166 3.68e-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: 81.34  E-value: 3.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349  42 ERAKKANITTHTLDhkqfSSReafDQNLSQLIDQYNPGVIILAGFMRILTEEFTQKYTGKMLNIHPSLLPKFQGLNTHQR 121
Cdd:cd08646    50 ELALELGLPVLQPE----KLK---DEEFLEELKALKPDLIVVVAYGQILPKEILDLPPYGCINVHPSLLPKYRGAAPIQR 122

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2544519349 122 AIDAKETEHGVTIHFVTAELDGGPIIAQSQIKVLEDDSAESLAKR 166
Cdd:cd08646   123 AILNGDKETGVTIMKMDEGLDTGDILAQEEVPIDPDDTAGELLDK 167
PLN02828 PLN02828
formyltetrahydrofolate deformylase
 26-179 4.51e-19

formyltetrahydrofolate deformylase


Pssm-ID: 178422  Cd Length: 268  Bit Score: 82.10  E-value: 4.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349  26 LDIEAVISNKEAAYG------LERAkkaNITTHTLDHKQFSSREAFDQNLSQLIDqynpgVIILAGFMRILTEEFTQKYT 99
Cdd:PLN02828   98 VDITCVISNHERGPNthvmrfLERH---GIPYHYLPTTKENKREDEILELVKGTD-----FLVLARYMQILSGNFLKGYG 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349 100 GKMLNIHPSLLPKFQGLNTHQRAIDAKETEHGVTIHFVTAELDGGPIIAQSQIKVLEDDSAESLAKRVLIEEHKLFPKVI 179
Cdd:PLN02828  170 KDIINIHHGLLPSFKGGNPSKQAFDAGVKLIGATSHFVTEELDAGPIIEQMVERVSHRDNLRSFVQKSENLEKQCLAKAI 249
fmt TIGR00460
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ...
 67-167 4.69e-18

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: 80.14  E-value: 4.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349  67 QNLSQLIDQYNPGVIILAGFMRILTEEFTQKYTGKMLNIHPSLLPKFQGLNTHQRAIDAKETEHGVTIHFVTAELDGGPI 146
Cdd:TIGR00460  68 LEELPLVRELKPDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVPKMDAGDI 147

                          90       100
                  ....*....|....*....|.
gi 2544519349 147 IAQSQIKVLEDDSAESLAKRV 167
Cdd:TIGR00460 148 LKQETFPIEEEDNSGTLSDKL 168
PLN02285 PLN02285
methionyl-tRNA formyltransferase
 63-163 5.44e-13

methionyl-tRNA formyltransferase


Pssm-ID: 215159 [Multi-domain]  Cd Length: 334  Bit Score: 66.26  E-value: 5.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349  63 EAFDQNLSQLidqyNPGVIILAGFMRILTEEFTQKYTGKMLNIHPSLLPKFQGLNTHQRAIDAKETEHGVTIHFVTAELD 142
Cdd:PLN02285   83 EDFLSALREL----QPDLCITAAYGNILPQKFLDIPKLGTVNIHPSLLPLYRGAAPVQRALQDGVNETGVSVAFTVRALD 158

                          90       100
                  ....*....|....*....|.
gi 2544519349 143 GGPIIAQSQIKVLEDDSAESL 163
Cdd:PLN02285  159 AGPVIAQERVEVDEDIKAPEL 179
FMT_core_ArnA_N cd08644
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ...
 103-174 9.69e-13

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: 63.90  E-value: 9.69e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2544519349 103 LNIHPSLLPKFQGLNTHQRAIDAKETEHGVTIHFVTAELDGGPIIAQSQIKVLEDDSAESLAKRVLIEEHKL 174
Cdd:cd08644   101 FNLHGSLLPKYRGRAPLNWALINGETETGVTLHRMTKKPDAGAIVDQEKVPILPDDTAKSLFHKLCVAARRL 172
PRK08125 PRK08125
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ...
 73-167 3.03e-11

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


Pssm-ID: 236156 [Multi-domain]  Cd Length: 660  Bit Score: 61.54  E-value: 3.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349  73 IDQYNPGVIILAGFMRILTEEFTQKYTGKMLNIHPSLLPKFQGLNTHQRAIDAKETEHGVTIHFVTAELDGGPIIAQSQI 152
Cdd:PRK08125   71 IRELAPDVIFSFYYRNLLSDEILQLAPAGAFNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQQRV 150

                          90
                  ....*....|....*
gi 2544519349 153 KVLEDDSAESLAKRV 167
Cdd:PRK08125  151 AIAPDDTALTLHHKL 165
FMT_core_like_6 cd08820
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 14-179 4.04e-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: 187722 [Multi-domain]  Cd Length: 173  Bit Score: 58.99  E-value: 4.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349  14 LQSIIDNANDINLDIEAVISNKEAAYGLERAKKANITTHTLdhkqfssreafdQNLSQL---IDQYNPGVIILAGFMRIL 90
Cdd:cd08820    15 LRTLLRLQDRGSFEIIAVLTNTSPADVWEGSEPLYDIGSTE------------RNLHKLleiLENKGVDILISVQYHWIL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349  91 TEEFTQKYTGKMLNIHPSLLPKFQGLNTHQRAIDAKETEHGVTIHFVTAELDGGPIIAQSQIKVLEDDSAESLAKRVLIE 170
Cdd:cd08820    83 PGSILEKAKEIAFNLHNAPLPEYRGCNQFSHAILNGDDQFGTTIHWMAEGIDSGDIIFEKRFPIPSDCTVISLYILAHYA 162


                  ....*....
gi 2544519349 171 EHKLFPKVI 179
Cdd:cd08820   163 AIALFGEHI 171
FMT_core_like_4 cd08651
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 14-180 3.27e-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: 187720 [Multi-domain]  Cd Length: 180  Bit Score: 56.51  E-value: 3.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349  14 LQSIIDNANDINLdieaVISNKEAAYG--------LERAKKANITTHTLDHKQfssreafDQNLSQLIDQYNPGVIILAG 85
Cdd:cd08651    15 LEAILEAGGEVVG----VITLDDSSSNndsdyldlDSFARKNGIPYYKFTDIN-------DEEIIEWIKEANPDIIFVFG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349  86 FMRILTEEFTQKYTGKMLNIHPSLLPKFQGLNTHQRAIDAKETEHGVTIHFVTAELDGGPIIAQSQIKVLEDDSAESLAK 165
Cdd:cd08651    84 WSQLLKPEILAIPRLGVIGFHPTKLPKNRGRAPIPWAILLGLKETASTFFWMDEGADSGDILSQEPFPIDKDDTANSLYD 163

                         170
                  ....*....|....*
gi 2544519349 166 RVLIEEHKLFPKVIH 180
Cdd:cd08651   164 KIMEAAKQQIDKFLP 178
FMT_core_NRPS_like cd08649
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ...
 88-163 1.83e-09

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: 54.19  E-value: 1.83e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2544519349  88 RILTEEFTQKYTGKMLNIHPSLLPKFQGLNTHQRAIDAKETEHGVTIHFVTAELDGGPIIAQSQIKVLEDDSAESL 163
Cdd:cd08649    72 RILPSEVLALPRKGAINFHDGPLPRYAGLNATSWALLAGETRHGVTWHRIEEGVDAGDILVQRPFDIAPDDTALSL 147
FMT_core_like_5 cd08823
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 104-167 2.18e-09

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: 54.37  E-value: 2.18e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2544519349 104 NIHPSLLPKFQGLNTHQRAIDAKETEHGVTIHFVTAELDGGPIIAQSQIKVLEDDSAESLAKRV 167
Cdd:cd08823    98 NLHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMTAEIDRGPIVLEQFTPIHPDDTYGLLCSRL 161
PRK06988 PRK06988
formyltransferase;
103-161 2.34e-08

formyltransferase;


Pssm-ID: 235902 [Multi-domain]  Cd Length: 312  Bit Score: 52.77  E-value: 2.34e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2544519349 103 LNIHPSLLPKFQGLNTHQRAIDAKETEHGVTIHFVTAELDGGPIIAQSQIKVLEDDSAE 161
Cdd:PRK06988  103 YNMHGSLLPKYRGRVPVNWAVLNGETETGATLHEMVAKPDAGAIVDQTAVPILPDDTAA 161
FMT_core_like_2 cd08822
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 106-182 5.49e-08

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


Pssm-ID: 187724 [Multi-domain]  Cd Length: 192  Bit Score: 50.92  E-value: 5.49e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2544519349 106 HPSLLPKFQGLNTHQRAIDAKETEHGVTIHFVTAELDGGPIIAQSQIKVLEDDSAESLAKRVLIEEH-KLFPKVIHWF 182
Cdd:cd08822    95 HPSLLPRHRGRDAVEWTIRMRDPITGGTVYHLDDGVDGGPIAAQDWCHVRPGDTAAELWRRALAPMGvKLLTQVIDAL 172
FMT_core_FDH_N cd08647
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ...
 106-171 2.57e-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: 46.29  E-value: 2.57e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2544519349 106 HPSLLPKFQGLNTHQRAIDAKETEHGVTIHFVTAELDGGPIIAQSQIKVLEDDSAESLAKRVLIEE 171
Cdd:cd08647   106 HPSILPRHRGASAINWTLIHGDKKAGFTIFWADDGLDTGPILLQKECDVLPNDTVDTLYNRFLYPE 171
PRK07579 PRK07579
dTDP-4-amino-4,6-dideoxyglucose formyltransferase;
12-179 2.86e-06

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


Pssm-ID: 236058 [Multi-domain]  Cd Length: 245  Bit Score: 46.44  E-value: 2.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349  12 SNLQSIIDNANDINLDIEAvisnkeaayglerakkANITTHTLDHKQFssreafdQNLSQLIDQYNPGVIILAGFMRILT 91
Cdd:PRK07579   15 ALAVDLIARKNDMDVDYFC----------------SFKSQTSFAKEIY-------QSPIKQLDVAERVAEIVERYDLVLS 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519349  92 EEFTQKYTGKM------LNIHPSLLPKFQGLNTHQRAIDAKEtEHGVTIHFVTAELDGGPIIAQSQIKVLEDDSAESLAK 165
Cdd:PRK07579   72 FHCKQRFPAKLvngvrcINIHPGFNPYNRGWFPQVFSIINGL-KIGATIHEMDEQLDHGPIIAQREVEIESWDSSGSVYA 150

                         170
                  ....*....|....
gi 2544519349 166 RVLIEEHKLFPKVI 179
Cdd:PRK07579  151 RVMDIERELVLEHF 164
 
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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