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Conserved domains on  [gi|1828885921|ref|WP_167732887|]
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phosphoribosylglycinamide formyltransferase [Staphylococcus schleiferi]

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 ...
 1-188 8.18e-94

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: 271.52  E-value: 8.18e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921   1 MIKIAIFASGSGTNFDNIMTRIREGELqNIEVTALYTDQPEAACIALAQQHGIPVHAFVPKTYENKAAYEADVLKHLKAE 80
Cdd:COG0299     1 MKRIAVLISGRGSNLQALIDAIEAGDL-PAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921  81 QAEWIILAGYMRLIGETLLSAYEGRMLNIHPSLLPKYKGKNAVGQALNSGDDQTGSTVHYVDAGMDTGQIIEQRTCPIYK 160
Cdd:COG0299    80 GPDLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLP 159

                         170       180
                  ....*....|....*....|....*...
gi 1828885921 161 DDTISTLEQRIKSLEYELYPTVIKKIIQ 188
Cdd:COG0299   160 DDTEETLAARILEQEHRLYPEAIRLLAE 187
 
Name Accession Description Interval E-value
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 1-188 8.18e-94

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: 271.52  E-value: 8.18e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921   1 MIKIAIFASGSGTNFDNIMTRIREGELqNIEVTALYTDQPEAACIALAQQHGIPVHAFVPKTYENKAAYEADVLKHLKAE 80
Cdd:COG0299     1 MKRIAVLISGRGSNLQALIDAIEAGDL-PAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921  81 QAEWIILAGYMRLIGETLLSAYEGRMLNIHPSLLPKYKGKNAVGQALNSGDDQTGSTVHYVDAGMDTGQIIEQRTCPIYK 160
Cdd:COG0299    80 GPDLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLP 159

                         170       180
                  ....*....|....*....|....*...
gi 1828885921 161 DDTISTLEQRIKSLEYELYPTVIKKIIQ 188
Cdd:COG0299   160 DDTEETLAARILEQEHRLYPEAIRLLAE 187
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 3-186 2.75e-90

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: 261.55  E-value: 2.75e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921   3 KIAIFASGSGTNFDNIMTRIREGELqNIEVTALYTDQPEAACIALAQQHGIPVHAFVPKTYENKAAYEADVLKHLKAEQA 82
Cdd:cd08645     1 RIAVLASGSGSNLQALIDAIKSGKL-NAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921  83 EWIILAGYMRLIGETLLSAYEGRMLNIHPSLLPKYKGKNAVGQALNSGDDQTGSTVHYVDAGMDTGQIIEQRTCPIYKDD 162
Cdd:cd08645    80 DLIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGD 159

                         170       180
                  ....*....|....*....|....
gi 1828885921 163 TISTLEQRIKSLEYELYPTVIKKI 186
Cdd:cd08645   160 TPETLAERIHALEHRLYPEAIKLL 183
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 3-188 1.55e-73

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: 219.55  E-value: 1.55e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921   3 KIAIFASGSGTNFDNIMTRIREGELqNIEVTALYTDQPEAACIALAQQHGIPVHAFVPKTYENKAAYEADVLKHLKAEQA 82
Cdd:TIGR00639   2 RIVVLISGNGSNLQAIIDACKEGKI-PASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921  83 EWIILAGYMRLIGETLLSAYEGRMLNIHPSLLPKYKGKNAVGQALNSGDDQTGSTVHYVDAGMDTGQIIEQRTCPIYKDD 162
Cdd:TIGR00639  81 DLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPED 160

                         170       180
                  ....*....|....*....|....*.
gi 1828885921 163 TISTLEQRIKSLEYELYPTVIKKIIQ 188
Cdd:TIGR00639 161 TEETLEQRIHKQEHRIYPLAIAWFAQ 186
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 3-183 1.78e-63

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: 193.66  E-value: 1.78e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921   3 KIAIFASGSGTNFDNIMTRIREGElQNIEVTALYTDQPEAACIALAQQHGIPVHAFVPKTYENKAAYEADVLKHLKAEQA 82
Cdd:pfam00551   2 KIAVLISGTGSNLQALIDALRKGG-QDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921  83 EWIILAGYMRLIGETLLSAYEGRMLNIHPSLLPKYKGKNAVGQALNSGDDQTGSTVHYVDAGMDTGQIIEQRTCPIYKDD 162
Cdd:pfam00551  81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160

                         170       180
                  ....*....|....*....|.
gi 1828885921 163 TISTLEQRIKSLEYELYPTVI 183
Cdd:pfam00551 161 TAETLYNRVADLEHKALPRVL 181
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 3-183 1.81e-45

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 148.69  E-value: 1.81e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921   3 KIAIFASGSGTNFDNIMTRIREGELqNIEVTALYTDQPEAACIALAQQHGIPVHAFVPKTYENKAAYEADVLKHLKAEQA 82
Cdd:PLN02331    1 KLAVFVSGGGSNFRAIHDACLDGRV-NGDVVVVVTNKPGCGGAEYARENGIPVLVYPKTKGEPDGLSPDELVDALRGAGV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921  83 EWIILAGYMRLIGETLLSAYEGRMLNIHPSLLPKYKGKNAVGQ-----ALNSGDDQTGSTVHYVDAGMDTGQIIEQRTCP 157
Cdd:PLN02331   80 DFVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFGGKGYYGIkvhkaVIASGARYSGPTVHFVDEHYDTGRILAQRVVP 159

                         170       180
                  ....*....|....*....|....*.
gi 1828885921 158 IYKDDTISTLEQRIKSLEYELYPTVI 183
Cdd:PLN02331  160 VLATDTPEELAARVLHEEHQLYVEVV 185
 
Name Accession Description Interval E-value
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 1-188 8.18e-94

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: 271.52  E-value: 8.18e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921   1 MIKIAIFASGSGTNFDNIMTRIREGELqNIEVTALYTDQPEAACIALAQQHGIPVHAFVPKTYENKAAYEADVLKHLKAE 80
Cdd:COG0299     1 MKRIAVLISGRGSNLQALIDAIEAGDL-PAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921  81 QAEWIILAGYMRLIGETLLSAYEGRMLNIHPSLLPKYKGKNAVGQALNSGDDQTGSTVHYVDAGMDTGQIIEQRTCPIYK 160
Cdd:COG0299    80 GPDLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLP 159

                         170       180
                  ....*....|....*....|....*...
gi 1828885921 161 DDTISTLEQRIKSLEYELYPTVIKKIIQ 188
Cdd:COG0299   160 DDTEETLAARILEQEHRLYPEAIRLLAE 187
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 3-186 2.75e-90

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: 261.55  E-value: 2.75e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921   3 KIAIFASGSGTNFDNIMTRIREGELqNIEVTALYTDQPEAACIALAQQHGIPVHAFVPKTYENKAAYEADVLKHLKAEQA 82
Cdd:cd08645     1 RIAVLASGSGSNLQALIDAIKSGKL-NAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921  83 EWIILAGYMRLIGETLLSAYEGRMLNIHPSLLPKYKGKNAVGQALNSGDDQTGSTVHYVDAGMDTGQIIEQRTCPIYKDD 162
Cdd:cd08645    80 DLIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGD 159

                         170       180
                  ....*....|....*....|....
gi 1828885921 163 TISTLEQRIKSLEYELYPTVIKKI 186
Cdd:cd08645   160 TPETLAERIHALEHRLYPEAIKLL 183
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 3-188 1.55e-73

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: 219.55  E-value: 1.55e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921   3 KIAIFASGSGTNFDNIMTRIREGELqNIEVTALYTDQPEAACIALAQQHGIPVHAFVPKTYENKAAYEADVLKHLKAEQA 82
Cdd:TIGR00639   2 RIVVLISGNGSNLQAIIDACKEGKI-PASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921  83 EWIILAGYMRLIGETLLSAYEGRMLNIHPSLLPKYKGKNAVGQALNSGDDQTGSTVHYVDAGMDTGQIIEQRTCPIYKDD 162
Cdd:TIGR00639  81 DLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPED 160

                         170       180
                  ....*....|....*....|....*.
gi 1828885921 163 TISTLEQRIKSLEYELYPTVIKKIIQ 188
Cdd:TIGR00639 161 TEETLEQRIHKQEHRIYPLAIAWFAQ 186
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 3-183 1.78e-63

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: 193.66  E-value: 1.78e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921   3 KIAIFASGSGTNFDNIMTRIREGElQNIEVTALYTDQPEAACIALAQQHGIPVHAFVPKTYENKAAYEADVLKHLKAEQA 82
Cdd:pfam00551   2 KIAVLISGTGSNLQALIDALRKGG-QDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921  83 EWIILAGYMRLIGETLLSAYEGRMLNIHPSLLPKYKGKNAVGQALNSGDDQTGSTVHYVDAGMDTGQIIEQRTCPIYKDD 162
Cdd:pfam00551  81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160

                         170       180
                  ....*....|....*....|.
gi 1828885921 163 TISTLEQRIKSLEYELYPTVI 183
Cdd:pfam00551 161 TAETLYNRVADLEHKALPRVL 181
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 3-183 1.81e-45

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 148.69  E-value: 1.81e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921   3 KIAIFASGSGTNFDNIMTRIREGELqNIEVTALYTDQPEAACIALAQQHGIPVHAFVPKTYENKAAYEADVLKHLKAEQA 82
Cdd:PLN02331    1 KLAVFVSGGGSNFRAIHDACLDGRV-NGDVVVVVTNKPGCGGAEYARENGIPVLVYPKTKGEPDGLSPDELVDALRGAGV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921  83 EWIILAGYMRLIGETLLSAYEGRMLNIHPSLLPKYKGKNAVGQ-----ALNSGDDQTGSTVHYVDAGMDTGQIIEQRTCP 157
Cdd:PLN02331   80 DFVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFGGKGYYGIkvhkaVIASGARYSGPTVHFVDEHYDTGRILAQRVVP 159

                         170       180
                  ....*....|....*....|....*.
gi 1828885921 158 IYKDDTISTLEQRIKSLEYELYPTVI 183
Cdd:PLN02331  160 VLATDTPEELAARVLHEEHQLYVEVV 185
FMT_core cd08369
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...
 4-185 3.76e-41

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: 136.65  E-value: 3.76e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921   4 IAIFasGSGTNFDNIMTRIREGElqNIEVTALYTDQPEAACIALAQqhgipVHAFVPKTYENKAAYEADVLKHLKAEQAE 83
Cdd:cd08369     1 IVIL--GSGNIGQRVLKALLSKE--GHEIVGVVTHPDSPRGTAQLS-----LELVGGKVYLDSNINTPELLELLKEFAPD 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921  84 WIILAGYMRLIGETLLSAYEGRMLNIHPSLLPKYKGKNAVGQALNSGDDQTGSTVHYVDAGMDTGQIIEQRTCPIYKDDT 163
Cdd:cd08369    72 LIVSINFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDT 151

                         170       180
                  ....*....|....*....|..
gi 1828885921 164 ISTLEQRIKSLEYELYPTVIKK 185
Cdd:cd08369   152 AGTLYQRLIELGPKLLKEALQK 173
FMT_core_Formyl-FH4-Hydrolase_C cd08648
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ...
 3-175 1.15e-34

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: 120.74  E-value: 1.15e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921   3 KIAIFASGSGTNFDNIMTRIREGELqNIEVTALYTDQPEAAciALAQQHGIPVHaFVPKTYENKAAYEADVLKHLKAEQA 82
Cdd:cd08648     2 RVAIFVSKEDHCLYDLLHRWREGEL-PCEIPLVISNHPDLR--PLAERFGIPFH-HIPVTKDTKAEAEAEQLELLEEYGV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921  83 EWIILAGYMRLIGETLLSAYEGRMLNIHPSLLPKYKGKNAVGQALNSGDDQTGSTVHYVDAGMDTGQIIEQRTCPIYKDD 162
Cdd:cd08648    78 DLVVLARYMQILSPDFVERYPNRIINIHHSFLPAFKGAKPYHQAFERGVKLIGATAHYVTEELDEGPIIEQDVERVSHRD 157

                         170
                  ....*....|...
gi 1828885921 163 TISTLEQRIKSLE 175
Cdd:cd08648   158 SVEDLVRKGRDIE 170
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
28-188 3.39e-31

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


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 114.82  E-value: 3.39e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921  28 QNIEVTALYTdQPEAAC-----------IALAQQHGIPVhaFVPKTYENKAAYEAdvlkhLKAEQAEWIILAGYMRLIGE 96
Cdd:COG0223    22 AGHEVVAVVT-QPDRPAgrgrkltpspvKELALEHGIPV--LQPESLKDPEFLEE-----LRALNPDLIVVVAYGQILPK 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921  97 TLLSAYEGRMLNIHPSLLPKYKGKNAVGQALNSGDDQTGSTVHYVDAGMDTGQIIEQRTCPIYKDDTISTLEQRIKSLEY 176
Cdd:COG0223    94 EVLDIPRLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDTGDILLQEEVPIGPDDTAGSLHDKLAELGA 173

                         170
                  ....*....|..
gi 1828885921 177 ELYPTVIKKIIQ 188
Cdd:COG0223   174 ELLLETLDALEA 185
PurU TIGR00655
formyltetrahydrofolate deformylase; This model describes formyltetrahydrofolate deformylases. ...
 3-175 4.08e-30

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


Pssm-ID: 273199 [Multi-domain]  Cd Length: 280  Bit Score: 111.37  E-value: 4.08e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921   3 KIAIFASGSGTNFDNIMTRIREGELqNIEVTALYTDQPEAAciALAQQHGIPVHaFVPKTYENKAAYEADVLKHLKAEQA 82
Cdd:TIGR00655  86 RVAILVSKEDHCLGDLLWRWYSGEL-DAEIALVISNHEDLR--SLVERFGIPFH-YIPATKDNRVEHEKRQLELLKQYQV 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921  83 EWIILAGYMRLIGETLLSAYEGRMLNIHPSLLPKYKGKNAVGQALNSGDDQTGSTVHYVDAGMDTGQIIEQRTCPIYKDD 162
Cdd:TIGR00655 162 DLVVLAKYMQILSPDFVKRYPNKIINIHHSFLPAFIGANPYQRAYERGVKIIGATAHYVTEELDEGPIIEQDVVRVDHTD 241

                         170
                  ....*....|...
gi 1828885921 163 TISTLEQRIKSLE 175
Cdd:TIGR00655 242 NVEDLIRAGRDIE 254
PurU COG0788
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ...
 3-167 4.92e-30

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: 110.91  E-value: 4.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921   3 KIAIFASGSGTNFDNIMTRIREGELqNIEVTALYTDQPEAAciALAQQHGIPVHaFVPKTYENKAAYEADVLKHLKAEQA 82
Cdd:COG0788    88 RVAILVSKEDHCLNDLLYRWRSGEL-PAEIPAVISNHPDLR--PLAEWFGIPFH-HIPVTKETKAEAEARLLELLEEYDI 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921  83 EWIILAGYMRLIGETLLSAYEGRMLNIHPSLLPKYKGKNAVGQALNSGDDQTGSTVHYVDAGMDTGQIIEQRTCPIYKDD 162
Cdd:COG0788   164 DLVVLARYMQILSPDFCARLPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVERVDHRD 243


                  ....*
gi 1828885921 163 TISTL 167
Cdd:COG0788   244 TPEDL 248
PRK13011 PRK13011
formyltetrahydrofolate deformylase; Reviewed
 3-166 1.12e-29

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 237266 [Multi-domain]  Cd Length: 286  Bit Score: 110.46  E-value: 1.12e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921   3 KIAIFASGSGTNFDNIMTRIREGELqNIEVTALYTDQPEAAciALAQQHGIPVHAFvPKTYENKAAYEADVLKHLKAEQA 82
Cdd:PRK13011   91 KVLIMVSKFDHCLNDLLYRWRIGEL-PMDIVGVVSNHPDLE--PLAAWHGIPFHHF-PITPDTKPQQEAQVLDVVEESGA 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921  83 EWIILAGYMRLIGETLLSAYEGRMLNIHPSLLPKYKGKNAVGQALNSGDDQTGSTVHYVDAGMDTGQIIEQRTCPI---- 158
Cdd:PRK13011  167 ELVVLARYMQVLSPELCRKLAGRAINIHHSFLPGFKGAKPYHQAYERGVKLIGATAHYVTDDLDEGPIIEQDVERVdhay 246


                  ....*...
gi 1828885921 159 YKDDTIST 166
Cdd:PRK13011  247 SPEDLVAK 254
FMT_core_Met-tRNA-FMT_N cd08646
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ...
 29-188 5.33e-28

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: 103.68  E-value: 5.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921  29 NIEVTALYTdQPEAACI-----------ALAQQHGIPVHAfvPKTYENKAAYEAdvlkhLKAEQAEWIILAGYMRLIGET 97
Cdd:cd08646    23 GHEVVAVVT-QPDKPRGrgkkltpspvkELALELGLPVLQ--PEKLKDEEFLEE-----LKALKPDLIVVVAYGQILPKE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921  98 LLSAYEGRMLNIHPSLLPKYKGKNAVGQALNSGDDQTGSTVHYVDAGMDTGQIIEQRTCPIYKDDTISTLEQRIKSLEYE 177
Cdd:cd08646    95 ILDLPPYGCINVHPSLLPKYRGAAPIQRAILNGDKETGVTIMKMDEGLDTGDILAQEEVPIDPDDTAGELLDKLAELGAD 174

                         170
                  ....*....|.
gi 1828885921 178 LYPTVIKKIIQ 188
Cdd:cd08646   175 LLLEVLDDIEA 185
purU PRK13010
formyltetrahydrofolate deformylase; Reviewed
 3-155 1.82e-27

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 139334 [Multi-domain]  Cd Length: 289  Bit Score: 104.49  E-value: 1.82e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921   3 KIAIFASGSGTNFDNIMTRIREGELqNIEVTALYTDQPEAAciALAQQHGIPVHAFvPKTYENKAAYEADVLKHLKAEQA 82
Cdd:PRK13010   95 KVVIMVSKFDHCLNDLLYRWRMGEL-DMDIVGIISNHPDLQ--PLAVQHDIPFHHL-PVTPDTKAQQEAQILDLIETSGA 170

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828885921  83 EWIILAGYMRLIGETLLSAYEGRMLNIHPSLLPKYKGKNAVGQALNSGDDQTGSTVHYVDAGMDTGQIIEQRT 155
Cdd:PRK13010  171 ELVVLARYMQVLSDDLSRKLSGRAINIHHSFLPGFKGARPYHQAHARGVKLIGATAHFVTDDLDEGPIIEQDV 243
purU PRK06027
formyltetrahydrofolate deformylase; Reviewed
 3-153 9.08e-26

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 235676 [Multi-domain]  Cd Length: 286  Bit Score: 99.80  E-value: 9.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921   3 KIAIFASGSGTNFDNIMTRIREGELqNIEVTALYTDQPEAAciALAQQHGIPVHaFVPKTYENKAAYEADVLKHLKAEQA 82
Cdd:PRK06027   91 RVVILVSKEDHCLGDLLWRWRSGEL-PVEIAAVISNHDDLR--SLVERFGIPFH-HVPVTKETKAEAEARLLELIDEYQP 166

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1828885921  83 EWIILAGYMRLIGETLLSAYEGRMLNIHPSLLPKYKGKNAVGQALNSGDDQTGSTVHYVDAGMDTGQIIEQ 153
Cdd:PRK06027  167 DLVVLARYMQILSPDFVARFPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQ 237
PLN02828 PLN02828
formyltetrahydrofolate deformylase
 3-184 6.81e-25

formyltetrahydrofolate deformylase


Pssm-ID: 178422  Cd Length: 268  Bit Score: 97.51  E-value: 6.81e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921   3 KIAIFASGSGTNFDNIMTRIREGELQnIEVTALYTDQ---PEAACIALAQQHGIPVHaFVPKTYENKAayEADVLKHLKA 79
Cdd:PLN02828   72 KIAVLASKQDHCLIDLLHRWQDGRLP-VDITCVISNHergPNTHVMRFLERHGIPYH-YLPTTKENKR--EDEILELVKG 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921  80 eqAEWIILAGYMRLIGETLLSAYEGRMLNIHPSLLPKYKGKNAVGQALNSGDDQTGSTVHYVDAGMDTGQIIEQRTCPIY 159
Cdd:PLN02828  148 --TDFLVLARYMQILSGNFLKGYGKDIINIHHGLLPSFKGGNPSKQAFDAGVKLIGATSHFVTEELDAGPIIEQMVERVS 225

                         170       180
                  ....*....|....*....|....*
gi 1828885921 160 KDDTISTLEQRIKSLEYELYPTVIK 184
Cdd:PLN02828  226 HRDNLRSFVQKSENLEKQCLAKAIK 250
FMT_core_like_3 cd08653
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 70-183 2.86e-22

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: 87.65  E-value: 2.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921  70 EADVLKHLKAEQAEWIILAGyMRLIGETLLSAYEGRMLNIHPSLLPKYKGKNAVGQALNSGDDQ-TGSTVHYVDAGMDTG 148
Cdd:cd08653    36 GPEVVAALRALAPDVVSVYG-CGIIKDALLAIPPLGVLNLHGGILPDYRGVHTGFWALANGDPDnVGVTVHLVDAGIDTG 114

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1828885921 149 QIIEQRTCPIYKDDTISTLEQRIKSLEYELYPTVI 183
Cdd:cd08653   115 DVLAQARPPLAAGDTLLSLYLRLYRAGVELMVEAI 149
FMT_core_like_4 cd08651
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 45-186 3.31e-21

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: 85.78  E-value: 3.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921  45 IALAQQHGIPVHAFvpkTYENkaayEADVLKHLKAEQAEWIILAGYMRLIGETLLSAYEGRMLNIHPSLLPKYKGKNAVG 124
Cdd:cd08651    46 DSFARKNGIPYYKF---TDIN----DEEIIEWIKEANPDIIFVFGWSQLLKPEILAIPRLGVIGFHPTKLPKNRGRAPIP 118

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828885921 125 QALNSGDDQTGSTVHYVDAGMDTGQIIEQRTCPIYKDDTISTLEQRIKSLEYELYPTVIKKI 186
Cdd:cd08651   119 WAILLGLKETASTFFWMDEGADSGDILSQEPFPIDKDDTANSLYDKIMEAAKQQIDKFLPRL 180
fmt TIGR00460
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ...
 47-187 2.78e-19

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: 83.22  E-value: 2.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921  47 LAQQHGIPVhaFVPKTYEnkaayEADVLKHLKAEQAEWIILAGYMRLIGETLLSAYEGRMLNIHPSLLPKYKGKNAVGQA 126
Cdd:TIGR00460  51 LAEEKGIPV--FQPEKQR-----QLEELPLVRELKPDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRA 123

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1828885921 127 LNSGDDQTGSTVHYVDAGMDTGQIIEQRTCPIYKDDTISTLEQRIKSLEYELYPTVIKKII 187
Cdd:TIGR00460 124 ILNGDKKTGVTIMQMVPKMDAGDILKQETFPIEEEDNSGTLSDKLSELGAQLLIETLKELP 184
FMT_core_FDH_N cd08647
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ...
 48-188 5.08e-18

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: 77.87  E-value: 5.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921  48 AQQHGIPVhaFVPKTYENKAAYEADVLKHLKAEQAEWIILAGYMRLIGETLLSAYEGRMLNIHPSLLPKYKGKNAVGQAL 127
Cdd:cd08647    46 AEKDGVPV--FKFPRWRAKGQAIPEVVAKYKALGAELNVLPFCSQFIPMEVIDAPKHGSIIYHPSILPRHRGASAINWTL 123

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1828885921 128 NSGDDQTGSTVHYVDAGMDTGQIIEQRTCPIYKDDTISTLEQRIksleyeLYPTVIKKIIQ 188
Cdd:cd08647   124 IHGDKKAGFTIFWADDGLDTGPILLQKECDVLPNDTVDTLYNRF------LYPEGIKAMVE 178
FMT_core_ArnA_N cd08644
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ...
 3-167 8.62e-17

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: 74.69  E-value: 8.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921   3 KIAIFAsgsgtnFDNIMTRIREGEL-QNIEVTALYT--DQPE-----AACIALAQQHGIPVhaFVPKTYENKAAYEAdvL 74
Cdd:cd08644     2 KAVVFA------YHEVGYRCLEALLaAGFEVVAVFThtDNPGeniwfGSVAQLAREHGIPV--FTPDDINHPEWVER--L 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921  75 KHLKAEqaewIILAGYMR-LIGETLLSAYEGRMLNIHPSLLPKYKGKNAVGQALNSGDDQTGSTVHYVDAGMDTGQIIEQ 153
Cdd:cd08644    72 RALKPD----LIFSFYYRhMISEDILEIARLGAFNLHGSLLPKYRGRAPLNWALINGETETGVTLHRMTKKPDAGAIVDQ 147

                         170
                  ....*....|....
gi 1828885921 154 RTCPIYKDDTISTL 167
Cdd:cd08644   148 EKVPILPDDTAKSL 161
PRK06988 PRK06988
formyltransferase;
46-163 2.66e-16

formyltransferase;


Pssm-ID: 235902 [Multi-domain]  Cd Length: 312  Bit Score: 75.12  E-value: 2.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921  46 ALAQQHGIPVhafvpKTYENKAayEADVLKHLKAEQAEWIILAGYMRLIGETLLSAYEGRMLNIHPSLLPKYKGKNAVGQ 125
Cdd:PRK06988   49 AVAAEHGIPV-----ITPADPN--DPELRAAVAAAAPDFIFSFYYRHMIPVDLLALAPRGAYNMHGSLLPKYRGRVPVNW 121

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1828885921 126 ALNSGDDQTGSTVHYVDAGMDTGQIIEQRTCPIYKDDT 163
Cdd:PRK06988  122 AVLNGETETGATLHEMVAKPDAGAIVDQTAVPILPDDT 159
PLN02285 PLN02285
methionyl-tRNA formyltransferase
 46-174 3.63e-16

methionyl-tRNA formyltransferase


Pssm-ID: 215159 [Multi-domain]  Cd Length: 334  Bit Score: 74.73  E-value: 3.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921  46 ALAQQHGIPVHA-FVPKTyenkaAYEADVLKHLKAEQAEWIILAGYMRLIGETLLSAYEGRMLNIHPSLLPKYKGKNAVG 124
Cdd:PLN02285   62 QLALDRGFPPDLiFTPEK-----AGEEDFLSALRELQPDLCITAAYGNILPQKFLDIPKLGTVNIHPSLLPLYRGAAPVQ 136

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1828885921 125 QALNSGDDQTGSTVHYVDAGMDTGQIIEQRTCPIYKDDTISTLEQRIKSL 174
Cdd:PLN02285  137 RALQDGVNETGVSVAFTVRALDAGPVIAQERVEVDEDIKAPELLPLLFEL 186
FMT_core_like_5 cd08823
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 4-186 3.34e-14

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


Pssm-ID: 187725 [Multi-domain]  Cd Length: 177  Bit Score: 67.09  E-value: 3.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921   4 IAIFASGSgTNFDNIMTRIREGELQNIEVTALYTDQPEA----ACIALAQQHGIPVHAFvpktyENKAAYEAdvlkhLKA 79
Cdd:cd08823     1 IVILCNTS-MAAPLLGQLLSEGRLAGIAVPAHNASYFPQifvfTGIRRLVSKQRVDTAN-----LKEQLAEW-----LRA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921  80 EQAEWIILAGYMRLIGETLLSAYEGRMLNIHPSLLPKYKGKNAVGQALNSGDDQTGSTVHYVDAGMDTGQIIEQRTCPIY 159
Cdd:cd08823    70 LAADTVVVFTFPYRIPQHILDLPPLGFYNLHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMTAEIDRGPIVLEQFTPIH 149

                         170       180
                  ....*....|....*....|....*..
gi 1828885921 160 KDDTISTLEQRIKSLEYELYPTVIKKI 186
Cdd:cd08823   150 PDDTYGLLCSRLAMLAVGLLEELYQNL 176
FMT_core_NRPS_like cd08649
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ...
 40-167 1.65e-13

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: 64.97  E-value: 1.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921  40 PEAACIALAQQHGIPVHAFVPKTYENkaayeadvlkhLKAEQAEWIILAGYMRLIGETLLSAYEGRMLNIHPSLLPKYKG 119
Cdd:cd08649    31 TDPAIRAWAAAEGIAVLEPGEALEEL-----------LSDEPFDWLFSIVNLRILPSEVLALPRKGAINFHDGPLPRYAG 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1828885921 120 KNAVGQALNSGDDQTGSTVHYVDAGMDTGQIIEQRTCPIYKDDTISTL 167
Cdd:cd08649   100 LNATSWALLAGETRHGVTWHRIEEGVDAGDILVQRPFDIAPDDTALSL 147
PRK08125 PRK08125
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ...
 47-188 2.18e-13

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


Pssm-ID: 236156 [Multi-domain]  Cd Length: 660  Bit Score: 67.32  E-value: 2.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921  47 LAQQHGIPVHAfvPKtyenkaayeaDVlKHLK-----AEQAEWIILAGYMR-LIGETLLSAYEGRMLNIHPSLLPKYKGK 120
Cdd:PRK08125   48 LAAELGIPVYA--PE----------DV-NHPLwveriRELAPDVIFSFYYRnLLSDEILQLAPAGAFNLHGSLLPKYRGR 114

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1828885921 121 NAVGQALNSGDDQTGSTVHYVDAGMDTGQIIEQRTCPIYKDDTISTLEQRIKSLEYELYPTVIKKIIQ 188
Cdd:PRK08125  115 APLNWVLVNGETETGVTLHRMVKRADAGAIVAQQRVAIAPDDTALTLHHKLCHAARQLLEQTLPAIKH 182
FMT_core_like_2 cd08822
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 85-188 2.78e-13

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


Pssm-ID: 187724 [Multi-domain]  Cd Length: 192  Bit Score: 64.79  E-value: 2.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921  85 IILAGYMRLIG-ETLLSAYEGrMLNIHPSLLPKYKGKNAVGQALNSGDDQTGSTVHYVDAGMDTGQIIEQRTCPIYKDDT 163
Cdd:cd08822    70 IVAAHCHAFISaKTRARARLG-AIGYHPSLLPRHRGRDAVEWTIRMRDPITGGTVYHLDDGVDGGPIAAQDWCHVRPGDT 148

                          90       100
                  ....*....|....*....|....*
gi 1828885921 164 ISTLEQRiksleyELYPTVIKKIIQ 188
Cdd:cd08822   149 AAELWRR------ALAPMGVKLLTQ 167
FMT_core_like_6 cd08820
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 77-167 1.27e-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: 60.15  E-value: 1.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921  77 LKAEQAEWIILAGYMRLIGETLLSAYEGRMLNIHPSLLPKYKGKNAVGQALNSGDDQTGSTVHYVDAGMDTGQIIEQRTC 156
Cdd:cd08820    65 LENKGVDILISVQYHWILPGSILEKAKEIAFNLHNAPLPEYRGCNQFSHAILNGDDQFGTTIHWMAEGIDSGDIIFEKRF 144

                          90
                  ....*....|.
gi 1828885921 157 PIYKDDTISTL 167
Cdd:cd08820   145 PIPSDCTVISL 155
PRK07579 PRK07579
dTDP-4-amino-4,6-dideoxyglucose formyltransferase;
105-186 9.31e-07

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


Pssm-ID: 236058 [Multi-domain]  Cd Length: 245  Bit Score: 47.59  E-value: 9.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828885921 105 RMLNIHPSLLPKYKG-KNAVGQALNsgDDQTGSTVHYVDAGMDTGQIIEQRTCPIYKDDTISTLEQRIKSLEYELYPTVI 183
Cdd:PRK07579   87 RCINIHPGFNPYNRGwFPQVFSIIN--GLKIGATIHEMDEQLDHGPIIAQREVEIESWDSSGSVYARVMDIERELVLEHF 164


                  ...
gi 1828885921 184 KKI 186
Cdd:PRK07579  165 DAI 167
 
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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