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Conserved domains on  [gi|491946580|ref|WP_005685443|]
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phosphoribosylglycinamide formyltransferase [Lacticaseibacillus rhamnosus]

Protein Classification

phosphoribosylglycinamide formyltransferase( domain architecture ID 10171287)

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 Ontology:  GO:0004644|GO:0006189
SCOP:  4000065

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 4-183 1.77e-87

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: 254.62  E-value: 1.77e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580   4 LAVFASGNGTNFEALANAAQAVDSHYQIAVLVCDQMQAPVIQKAAARHIPTLVVNFKDYANKAAAETYILSQL--PPVDA 81
Cdd:cd08645    2 IAVLASGSGSNLQALIDAIKSGKLNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLkeYKVDL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580  82 LILAGYMRIIGPTLLNAFPKRIINLHPALLPSFPGRQGIKDAFDYGVKVTGVTVHYVDAGIDTGEIIAQDPVRVSPGMTL 161
Cdd:cd08645   82 IVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDTP 161

                        170       180
                 ....*....|....*....|..
gi 491946580 162 AQLEAAIHHQEHQTFPATVKQL 183
Cdd:cd08645  162 ETLAERIHALEHRLYPEAIKLL 183
 
Name Accession Description Interval E-value
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 4-183 1.77e-87

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: 254.62  E-value: 1.77e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580   4 LAVFASGNGTNFEALANAAQAVDSHYQIAVLVCDQMQAPVIQKAAARHIPTLVVNFKDYANKAAAETYILSQL--PPVDA 81
Cdd:cd08645    2 IAVLASGSGSNLQALIDAIKSGKLNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLkeYKVDL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580  82 LILAGYMRIIGPTLLNAFPKRIINLHPALLPSFPGRQGIKDAFDYGVKVTGVTVHYVDAGIDTGEIIAQDPVRVSPGMTL 161
Cdd:cd08645   82 IVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDTP 161

                        170       180
                 ....*....|....*....|..
gi 491946580 162 AQLEAAIHHQEHQTFPATVKQL 183
Cdd:cd08645  162 ETLAERIHALEHRLYPEAIKLL 183
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 1-187 1.99e-85

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: 250.34  E-value: 1.99e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580   1 MKSLAVFASGNGTNFEALANAAQAVDSHYQIAVLVCDQMQAPVIQKAAARHIPTLVVNFKDYANKAAAETYILSQLPP-- 78
Cdd:COG0299    1 MKRIAVLISGRGSNLQALIDAIEAGDLPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAyg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580  79 VDALILAGYMRIIGPTLLNAFPKRIINLHPALLPSFPGRQGIKDAFDYGVKVTGVTVHYVDAGIDTGEIIAQDPVRVSPG 158
Cdd:COG0299   81 PDLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPD 160

                        170       180
                 ....*....|....*....|....*....
gi 491946580 159 MTLAQLEAAIHHQEHQTFPATVKQLIEEG 187
Cdd:COG0299  161 DTEETLAARILEQEHRLYPEAIRLLAEGR 189
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 2-189 8.68e-67

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: 202.60  E-value: 8.68e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580    2 KSLAVFASGNGTNFEALANAAQAVDSHYQIAVLVCDQMQAPVIQKAAARHIPTLVVNFKDYANKAAAETYILSQLPP--V 79
Cdd:TIGR00639   1 KRIVVLISGNGSNLQAIIDACKEGKIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAheV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580   80 DALILAGYMRIIGPTLLNAFPKRIINLHPALLPSFPGRQGIKDAFDYGVKVTGVTVHYVDAGIDTGEIIAQDPVRVSPGM 159
Cdd:TIGR00639  81 DLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPED 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 491946580  160 TLAQLEAAIHHQEHQTFPATVKQLIEEGAI 189
Cdd:TIGR00639 161 TEETLEQRIHKQEHRIYPLAIAWFAQGRLK 190
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 2-180 1.22e-52

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: 166.31  E-value: 1.22e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580    2 KSLAVFASGNGTNFEALANAAQAVDSHYQIAVLVCDQMQAPVIQKAAARHIPTLVVNFKDYANKAAAETYILSQLPP--V 79
Cdd:pfam00551   1 MKIAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRAlaA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580   80 DALILAGYMRIIGPTLLNAFPKRIINLHPALLPSFPGRQGIKDAFDYGVKVTGVTVHYVDAGIDTGEIIAQDPVRVSPGM 159
Cdd:pfam00551  81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160

                         170       180
                  ....*....|....*....|.
gi 491946580  160 TLAQLEAAIHHQEHQTFPATV 180
Cdd:pfam00551 161 TAETLYNRVADLEHKALPRVL 181
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 4-186 1.85e-38

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 130.97  E-value: 1.85e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580   4 LAVFASGNGTNFEALANAAQAVDSHYQIAVLVCDQMQAPVIQKAAARHIPTLVVNFKDYANKAAAETYILSQLPP--VDA 81
Cdd:PLN02331   2 LAVFVSGGGSNFRAIHDACLDGRVNGDVVVVVTNKPGCGGAEYARENGIPVLVYPKTKGEPDGLSPDELVDALRGagVDF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580  82 LILAGYMRIIGPTLLNAFPKRIINLHPALLPSFPGR--QGI---KDAFDYGVKVTGVTVHYVDAGIDTGEIIAQDPVRVS 156
Cdd:PLN02331  82 VLLAGYLKLIPVELVRAYPRSILNIHPALLPAFGGKgyYGIkvhKAVIASGARYSGPTVHFVDEHYDTGRILAQRVVPVL 161

                        170       180       190
                 ....*....|....*....|....*....|
gi 491946580 157 PGMTLAQLEAAIHHQEHQTFPATVKQLIEE 186
Cdd:PLN02331 162 ATDTPEELAARVLHEEHQLYVEVVAALCEE 191
 
Name Accession Description Interval E-value
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 4-183 1.77e-87

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: 254.62  E-value: 1.77e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580   4 LAVFASGNGTNFEALANAAQAVDSHYQIAVLVCDQMQAPVIQKAAARHIPTLVVNFKDYANKAAAETYILSQL--PPVDA 81
Cdd:cd08645    2 IAVLASGSGSNLQALIDAIKSGKLNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLkeYKVDL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580  82 LILAGYMRIIGPTLLNAFPKRIINLHPALLPSFPGRQGIKDAFDYGVKVTGVTVHYVDAGIDTGEIIAQDPVRVSPGMTL 161
Cdd:cd08645   82 IVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDTP 161

                        170       180
                 ....*....|....*....|..
gi 491946580 162 AQLEAAIHHQEHQTFPATVKQL 183
Cdd:cd08645  162 ETLAERIHALEHRLYPEAIKLL 183
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 1-187 1.99e-85

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: 250.34  E-value: 1.99e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580   1 MKSLAVFASGNGTNFEALANAAQAVDSHYQIAVLVCDQMQAPVIQKAAARHIPTLVVNFKDYANKAAAETYILSQLPP-- 78
Cdd:COG0299    1 MKRIAVLISGRGSNLQALIDAIEAGDLPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAyg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580  79 VDALILAGYMRIIGPTLLNAFPKRIINLHPALLPSFPGRQGIKDAFDYGVKVTGVTVHYVDAGIDTGEIIAQDPVRVSPG 158
Cdd:COG0299   81 PDLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPD 160

                        170       180
                 ....*....|....*....|....*....
gi 491946580 159 MTLAQLEAAIHHQEHQTFPATVKQLIEEG 187
Cdd:COG0299  161 DTEETLAARILEQEHRLYPEAIRLLAEGR 189
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 2-189 8.68e-67

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: 202.60  E-value: 8.68e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580    2 KSLAVFASGNGTNFEALANAAQAVDSHYQIAVLVCDQMQAPVIQKAAARHIPTLVVNFKDYANKAAAETYILSQLPP--V 79
Cdd:TIGR00639   1 KRIVVLISGNGSNLQAIIDACKEGKIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAheV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580   80 DALILAGYMRIIGPTLLNAFPKRIINLHPALLPSFPGRQGIKDAFDYGVKVTGVTVHYVDAGIDTGEIIAQDPVRVSPGM 159
Cdd:TIGR00639  81 DLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPED 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 491946580  160 TLAQLEAAIHHQEHQTFPATVKQLIEEGAI 189
Cdd:TIGR00639 161 TEETLEQRIHKQEHRIYPLAIAWFAQGRLK 190
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 2-180 1.22e-52

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: 166.31  E-value: 1.22e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580    2 KSLAVFASGNGTNFEALANAAQAVDSHYQIAVLVCDQMQAPVIQKAAARHIPTLVVNFKDYANKAAAETYILSQLPP--V 79
Cdd:pfam00551   1 MKIAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRAlaA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580   80 DALILAGYMRIIGPTLLNAFPKRIINLHPALLPSFPGRQGIKDAFDYGVKVTGVTVHYVDAGIDTGEIIAQDPVRVSPGM 159
Cdd:pfam00551  81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160

                         170       180
                  ....*....|....*....|.
gi 491946580  160 TLAQLEAAIHHQEHQTFPATV 180
Cdd:pfam00551 161 TAETLYNRVADLEHKALPRVL 181
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 4-186 1.85e-38

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 130.97  E-value: 1.85e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580   4 LAVFASGNGTNFEALANAAQAVDSHYQIAVLVCDQMQAPVIQKAAARHIPTLVVNFKDYANKAAAETYILSQLPP--VDA 81
Cdd:PLN02331   2 LAVFVSGGGSNFRAIHDACLDGRVNGDVVVVVTNKPGCGGAEYARENGIPVLVYPKTKGEPDGLSPDELVDALRGagVDF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580  82 LILAGYMRIIGPTLLNAFPKRIINLHPALLPSFPGR--QGI---KDAFDYGVKVTGVTVHYVDAGIDTGEIIAQDPVRVS 156
Cdd:PLN02331  82 VLLAGYLKLIPVELVRAYPRSILNIHPALLPAFGGKgyYGIkvhKAVIASGARYSGPTVHFVDEHYDTGRILAQRVVPVL 161

                        170       180       190
                 ....*....|....*....|....*....|
gi 491946580 157 PGMTLAQLEAAIHHQEHQTFPATVKQLIEE 186
Cdd:PLN02331 162 ATDTPEELAARVLHEEHQLYVEVVAALCEE 191
FMT_core_Formyl-FH4-Hydrolase_C cd08648
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ...
 51-164 5.54e-29

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: 106.11  E-value: 5.54e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580  51 HIPTlvvnfkDYANKAAAETYILSQLPP--VDALILAGYMRIIGPTLLNAFPKRIINLHPALLPSFPGRQGIKDAFDYGV 128
Cdd:cd08648   53 HIPV------TKDTKAEAEAEQLELLEEygVDLVVLARYMQILSPDFVERYPNRIINIHHSFLPAFKGAKPYHQAFERGV 126

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 491946580 129 KVTGVTVHYVDAGIDTGEIIAQDPVRVSPGMTLAQL 164
Cdd:cd08648  127 KLIGATAHYVTEELDEGPIIEQDVERVSHRDSVEDL 162
PurU COG0788
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ...
 63-164 3.28e-28

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: 106.29  E-value: 3.28e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580  63 ANKAAAETYILSQLPP--VDALILAGYMRIIGPTLLNAFPKRIINLHPALLPSFPGRQGIKDAFDYGVKVTGVTVHYVDA 140
Cdd:COG0788  145 ETKAEAEARLLELLEEydIDLVVLARYMQILSPDFCARLPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTA 224

                         90       100
                 ....*....|....*....|....
gi 491946580 141 GIDTGEIIAQDPVRVSPGMTLAQL 164
Cdd:COG0788  225 DLDEGPIIEQDVERVDHRDTPEDL 248
FMT_core cd08369
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...
 6-182 8.52e-27

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: 100.06  E-value: 8.52e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580   6 VFAsGNGTNFEALANAAQAVDSHYQIAVLVcdqmQAPVIQKAAARHIPTLVVNFKDYANKAAAETYILSQLPPVDALILA 85
Cdd:cd08369    2 VIL-GSGNIGQRVLKALLSKEGHEIVGVVT----HPDSPRGTAQLSLELVGGKVYLDSNINTPELLELLKEFAPDLIVSI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580  86 GYMRIIGPTLLNAFPKRIINLHPALLPSFPGRQGIKDAFDYGVKVTGVTVHYVDAGIDTGEIIAQDPVRVSPGMTLAQLE 165
Cdd:cd08369   77 NFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTAGTLY 156

                        170
                 ....*....|....*..
gi 491946580 166 AAIHHQEHQTFPATVKQ 182
Cdd:cd08369  157 QRLIELGPKLLKEALQK 173
purU PRK06027
formyltetrahydrofolate deformylase; Reviewed
 63-164 4.10e-23

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 235676 [Multi-domain]  Cd Length: 286  Bit Score: 92.86  E-value: 4.10e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580  63 ANKAAAETYILSQLPP--VDALILAGYMRIIGPTLLNAFPKRIINLHPALLPSFPGRQGIKDAFDYGVKVTGVTVHYVDA 140
Cdd:PRK06027 148 ETKAEAEARLLELIDEyqPDLVVLARYMQILSPDFVARFPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTA 227

                         90       100
                 ....*....|....*....|....
gi 491946580 141 GIDTGEIIAQDPVRVSPGMTLAQL 164
Cdd:PRK06027 228 DLDEGPIIEQDVIRVDHRDTAEDL 251
PRK13011 PRK13011
formyltetrahydrofolate deformylase; Reviewed
 50-176 1.99e-20

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 237266 [Multi-domain]  Cd Length: 286  Bit Score: 85.80  E-value: 1.99e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580  50 RHIPTlvvnfkDYANKAAAETYILSQLPPVDA--LILAGYMRIIGPTLLNAFPKRIINLHPALLPSFPGRQGIKDAFDYG 127
Cdd:PRK13011 141 HHFPI------TPDTKPQQEAQVLDVVEESGAelVVLARYMQVLSPELCRKLAGRAINIHHSFLPGFKGAKPYHQAYERG 214

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491946580 128 VKVTGVTVHYVDAGIDTGEIIAQDPVRVSPGMTLAQLEA------------AIH-HQEHQTF 176
Cdd:PRK13011 215 VKLIGATAHYVTDDLDEGPIIEQDVERVDHAYSPEDLVAkgrdvecltlarAVKaHIERRVF 276
PLN02828 PLN02828
formyltetrahydrofolate deformylase
 64-156 1.02e-19

formyltetrahydrofolate deformylase


Pssm-ID: 178422  Cd Length: 268  Bit Score: 83.64  E-value: 1.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580  64 NKAAAEtyILSQLPPVDALILAGYMRIIGPTLLNAFPKRIINLHPALLPSFPGRQGIKDAFDYGVKVTGVTVHYVDAGID 143
Cdd:PLN02828 135 NKREDE--ILELVKGTDFLVLARYMQILSGNFLKGYGKDIINIHHGLLPSFKGGNPSKQAFDAGVKLIGATSHFVTEELD 212

                         90
                 ....*....|...
gi 491946580 144 TGEIIAQDPVRVS 156
Cdd:PLN02828 213 AGPIIEQMVERVS 225
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
42-189 1.02e-18

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


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 81.31  E-value: 1.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580  42 PVIQKAAARHIPTL-VVNFKDyankaAAETYILSQLPPvDALILAGYMRIIGPTLLNAFPKRIINLHPALLPSFPGRQGI 120
Cdd:COG0223   47 PVKELALEHGIPVLqPESLKD-----PEFLEELRALNP-DLIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAAPI 120

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491946580 121 KDAFDYGVKVTGVTVHYVDAGIDTGEIIAQDPVRVSPGMTLAQLEAAIHHQEHQTFPATVKQlIEEGAI 189
Cdd:COG0223  121 QWAILNGDTETGVTIMQMDEGLDTGDILLQEEVPIGPDDTAGSLHDKLAELGAELLLETLDA-LEAGTL 188
purU PRK13010
formyltetrahydrofolate deformylase; Reviewed
 63-185 1.50e-17

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 139334 [Multi-domain]  Cd Length: 289  Bit Score: 78.30  E-value: 1.50e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580  63 ANKAAAETYILSQLPPVDA--LILAGYMRIIGPTLLNAFPKRIINLHPALLPSFPGRQGIKDAFDYGVKVTGVTVHYVDA 140
Cdd:PRK13010 152 DTKAQQEAQILDLIETSGAelVVLARYMQVLSDDLSRKLSGRAINIHHSFLPGFKGARPYHQAHARGVKLIGATAHFVTD 231

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 491946580 141 GIDTGEIIAQDPVRVSPGMTLAQLEAAIHHQEHQTFPATVKQLIE 185
Cdd:PRK13010 232 DLDEGPIIEQDVERVDHSYSPEDLVAKGRDVECLTLARAVKAFIE 276
fmt TIGR00460
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ...
 39-185 2.18e-16

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: 75.13  E-value: 2.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580   39 MQAPVIQKAAARHIPtlvvnFKDYANKAaaetyILSQLPPV-----DALILAGYMRIIGPTLLNAFPKRIINLHPALLPS 113
Cdd:TIGR00460  44 TPPPVKVLAEEKGIP-----VFQPEKQR-----QLEELPLVrelkpDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPR 113

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491946580  114 FPGRQGIKDAFDYGVKVTGVTVHYVDAGIDTGEIIAQDPVRVSPGMTLAQLEAAIHHQEHQTFPATVKQLIE 185
Cdd:TIGR00460 114 WRGGAPIQRAILNGDKKTGVTIMQMVPKMDAGDILKQETFPIEEEDNSGTLSDKLSELGAQLLIETLKELPE 185
FMT_core_like_3 cd08653
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 80-161 5.97e-16

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: 71.09  E-value: 5.97e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580  80 DALILAGyMRIIGPTLLNAFPKRIINLHPALLPSFPGRQGIKDAFDYG-VKVTGVTVHYVDAGIDTGEIIAQDPVRVSPG 158
Cdd:cd08653   49 DVVSVYG-CGIIKDALLAIPPLGVLNLHGGILPDYRGVHTGFWALANGdPDNVGVTVHLVDAGIDTGDVLAQARPPLAAG 127


                 ...
gi 491946580 159 MTL 161
Cdd:cd08653  128 DTL 130
FMT_core_Met-tRNA-FMT_N cd08646
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ...
 42-166 3.13e-15

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: 70.55  E-value: 3.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580  42 PVIQKAAARHIPTL-VVNFKDYANKAaaetyILSQLPPvDALILAGYMRIIGPTLLNAFPKRIINLHPALLPSFPGRQGI 120
Cdd:cd08646   47 PVKELALELGLPVLqPEKLKDEEFLE-----ELKALKP-DLIVVVAYGQILPKEILDLPPYGCINVHPSLLPKYRGAAPI 120

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 491946580 121 KDAFDYGVKVTGVTVHYVDAGIDTGEIIAQDPVRVSPGMTLAQLEA 166
Cdd:cd08646  121 QRAILNGDKETGVTIMKMDEGLDTGDILAQEEVPIDPDDTAGELLD 166
PLN02285 PLN02285
methionyl-tRNA formyltransferase
 16-186 9.03e-14

methionyl-tRNA formyltransferase


Pssm-ID: 215159 [Multi-domain]  Cd Length: 334  Bit Score: 68.18  E-value: 9.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580  16 EALANAAQAVDSHYQIAVLVCD----------QMQAPVIQKAAARHIPTLVVNFKDyanKAAAETYI--LSQLPPvDALI 83
Cdd:PLN02285  23 DALLDASQAPDSAFEVAAVVTQpparrgrgrkLMPSPVAQLALDRGFPPDLIFTPE---KAGEEDFLsaLRELQP-DLCI 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580  84 LAGYMRIIGPTLLNAFPKRIINLHPALLPSFPGRQGIKDAFDYGVKVTGVTVHYVDAGIDTGEIIAQDPVRVSPGMTLAQ 163
Cdd:PLN02285  99 TAAYGNILPQKFLDIPKLGTVNIHPSLLPLYRGAAPVQRALQDGVNETGVSVAFTVRALDAGPVIAQERVEVDEDIKAPE 178

                        170       180
                 ....*....|....*....|...
gi 491946580 164 LEAaihhqehQTFPATVKQLIEE 186
Cdd:PLN02285 179 LLP-------LLFELGTKLLLRE 194
FMT_core_like_4 cd08651
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 80-157 1.43e-12

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


Pssm-ID: 187720 [Multi-domain]  Cd Length: 180  Bit Score: 62.67  E-value: 1.43e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491946580  80 DALILAGYMRIIGPTLLNAFPKRIINLHPALLPSFPGRQGIKDAFDYGVKVTGVTVHYVDAGIDTGEIIAQDPVRVSP 157
Cdd:cd08651   77 DIIFVFGWSQLLKPEILAIPRLGVIGFHPTKLPKNRGRAPIPWAILLGLKETASTFFWMDEGADSGDILSQEPFPIDK 154
FMT_core_like_2 cd08822
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 15-164 6.07e-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: 187724 [Multi-domain]  Cd Length: 192  Bit Score: 58.63  E-value: 6.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580  15 FEALANAAQAVDShyqIAVLVCDQMQAPVIQKAAARHIPTLVVNFkdyankAAAETYIlsqlPPVDALILAGYMRIIGPT 94
Cdd:cd08822   16 LEALRARGIALLG---VAAPEEGDRLAAAARTAGSRGLPRAGVAV------LPADAIP----PGTDLIVAAHCHAFISAK 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580  95 LLNAFPKRIINLHPALLPSFPGRQGIKDAFDYGVKVTGVTVHYVDAGIDTGEIIAQDPVRVSPGMTLAQL 164
Cdd:cd08822   83 TRARARLGAIGYHPSLLPRHRGRDAVEWTIRMRDPITGGTVYHLDDGVDGGPIAAQDWCHVRPGDTAAEL 152
FMT_core_ArnA_N cd08644
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ...
 43-157 1.66e-10

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: 57.74  E-value: 1.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580  43 VIQKAAARHIPtlVVNFKDYANKAAAETyiLSQLPPvdALILAGYMRIIGPTLLNAFPKR-IINLHPALLPSFPGRQGIK 121
Cdd:cd08644   45 VAQLAREHGIP--VFTPDDINHPEWVER--LRALKP--DLIFSFYYRHMISEDILEIARLgAFNLHGSLLPKYRGRAPLN 118

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 491946580 122 DAFDYGVKVTGVTVHYVDAGIDTGEIIAQDPVRVSP 157
Cdd:cd08644  119 WALINGETETGVTLHRMTKKPDAGAIVDQEKVPILP 154
FMT_core_like_5 cd08823
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 80-165 3.50e-10

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


Pssm-ID: 187725 [Multi-domain]  Cd Length: 177  Bit Score: 56.30  E-value: 3.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580  80 DALILAGYMRIIGPTLLNAFPKRIINLHPALLPSFPGRQGIKDAFDYGVKVTGVTVHYVDAGIDTGEIIAQDPVRVSPGM 159
Cdd:cd08823   73 DTVVVFTFPYRIPQHILDLPPLGFYNLHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMTAEIDRGPIVLEQFTPIHPDD 152


                 ....*.
gi 491946580 160 TLAQLE 165
Cdd:cd08823  153 TYGLLC 158
PRK06988 PRK06988
formyltransferase;
82-163 1.19e-07

formyltransferase;


Pssm-ID: 235902 [Multi-domain]  Cd Length: 312  Bit Score: 50.46  E-value: 1.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580  82 LILAGYMR-IIGPTLLNAFPKRIINLHPALLPSFPGRQGIKDAFDYGVKVTGVTVHYVDAGIDTGEIIAQDPVRVSPGMT 160
Cdd:PRK06988  80 FIFSFYYRhMIPVDLLALAPRGAYNMHGSLLPKYRGRVPVNWAVLNGETETGATLHEMVAKPDAGAIVDQTAVPILPDDT 159


                 ...
gi 491946580 161 LAQ 163
Cdd:PRK06988 160 AAQ 162
PRK08125 PRK08125
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ...
 73-157 1.71e-07

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


Pssm-ID: 236156 [Multi-domain]  Cd Length: 660  Bit Score: 50.37  E-value: 1.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580  73 LSQLPPvDALILAGYMRIIGPTLLNAFPKRIINLHPALLPSFPGRQGIKDAFDYGVKVTGVTVHYVDAGIDTGEIIAQDP 152
Cdd:PRK08125  71 IRELAP-DVIFSFYYRNLLSDEILQLAPAGAFNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQQR 149


                 ....*
gi 491946580 153 VRVSP 157
Cdd:PRK08125 150 VAIAP 154
FMT_core_NRPS_like cd08649
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ...
 21-183 3.14e-06

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: 45.33  E-value: 3.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580  21 AAQAVDSHYQIAVLVCdqmQAPVIQK-AAARHIPtlvvnfkdYANKAAAETYILSQLPpVDALILAGYMRIIGPTLLNAF 99
Cdd:cd08649   15 AEQLLAAGHRIAAVVS---TDPAIRAwAAAEGIA--------VLEPGEALEELLSDEP-FDWLFSIVNLRILPSEVLALP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580 100 PKRIINLHPALLPSFPGRQGIKDAFDYGVKVTGVTVHYVDAGIDTGEIIAQDPVRVSPGMTLAQLEAAIHHQEHQTFPAT 179
Cdd:cd08649   83 RKGAINFHDGPLPRYAGLNATSWALLAGETRHGVTWHRIEEGVDAGDILVQRPFDIAPDDTALSLNLKCYEAGIEGFGEL 162


                 ....
gi 491946580 180 VKQL 183
Cdd:cd08649  163 IDEL 166
FMT_core_like_6 cd08820
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 76-150 2.13e-05

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


Pssm-ID: 187722 [Multi-domain]  Cd Length: 173  Bit Score: 42.81  E-value: 2.13e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491946580  76 LPPVDALILAGYMRIIGPTLLNAFPKRIINLHPALLPSFPGRQGIKDAFDYGVKVTGVTVHYVDAGIDTGEIIAQ 150
Cdd:cd08820   67 NKGVDILISVQYHWILPGSILEKAKEIAFNLHNAPLPEYRGCNQFSHAILNGDDQFGTTIHWMAEGIDSGDIIFE 141
FMT_core_FDH_N cd08647
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ...
 104-187 1.55e-04

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: 40.89  E-value: 1.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491946580 104 INLHPALLPSFPGRQGIKDAFDYGVKVTGVTVHYVDAGIDTGEIIAQDPVRVSPGMTLAQLEAAIHHQEHQTFPATVKQL 183
Cdd:cd08647  103 IIYHPSILPRHRGASAINWTLIHGDKKAGFTIFWADDGLDTGPILLQKECDVLPNDTVDTLYNRFLYPEGIKAMVEAVRL 182


                 ....
gi 491946580 184 IEEG 187
Cdd:cd08647  183 IAEG 186
PRK07579 PRK07579
dTDP-4-amino-4,6-dideoxyglucose formyltransferase;
102-155 7.00e-03

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


Pssm-ID: 236058 [Multi-domain]  Cd Length: 245  Bit Score: 36.03  E-value: 7.00e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491946580 102 RIINLHPALLPS----FPGRQGIKDafdyGVKVtGVTVHYVDAGIDTGEIIAQDPVRV 155
Cdd:PRK07579  87 RCINIHPGFNPYnrgwFPQVFSIIN----GLKI-GATIHEMDEQLDHGPIIAQREVEI 139
 
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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