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Conserved domains on  [gi|487749730|ref|WP_001831672|]
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MULTISPECIES: phosphoribosylglycinamide formyltransferase [Staphylococcus]

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); ...
 3-186 2.22e-93

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: 269.64  E-value: 2.22e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730   3 NIAIFASGSGSNFENIVKHIQTGQLSGiNVTALYTDNEGVPCIDRAKNLNIPIHINKPKDFSSKSLYEQHLLKLLSSEEV 82
Cdd:cd08645    1 RIAVLASGSGSNLQALIDAIKSGKLNA-EIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730  83 QWIVLAGYMRLVGQDLLQAYEGRILNIHPSLLPKFKGLDAIGQALESGDTVTGSTVHYVDSGMDTGEIIEQQQCDIKPDD 162
Cdd:cd08645   80 DLIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGD 159

                        170       180
                 ....*....|....*....|....
gi 487749730 163 TKEQLEDRVKHLEYELYPRVIAKI 186
Cdd:cd08645  160 TPETLAERIHALEHRLYPEAIKLL 183
 
Name Accession Description Interval E-value
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 3-186 2.22e-93

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: 269.64  E-value: 2.22e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730   3 NIAIFASGSGSNFENIVKHIQTGQLSGiNVTALYTDNEGVPCIDRAKNLNIPIHINKPKDFSSKSLYEQHLLKLLSSEEV 82
Cdd:cd08645    1 RIAVLASGSGSNLQALIDAIKSGKLNA-EIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730  83 QWIVLAGYMRLVGQDLLQAYEGRILNIHPSLLPKFKGLDAIGQALESGDTVTGSTVHYVDSGMDTGEIIEQQQCDIKPDD 162
Cdd:cd08645   80 DLIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGD 159

                        170       180
                 ....*....|....*....|....
gi 487749730 163 TKEQLEDRVKHLEYELYPRVIAKI 186
Cdd:cd08645  160 TPETLAERIHALEHRLYPEAIKLL 183
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 1-188 2.35e-91

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: 264.97  E-value: 2.35e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730   1 MTNIAIFASGSGSNFENIVKHIQTGQLsGINVTALYTDNEGVPCIDRAKNLNIPIHINKPKDFSSKSLYEQHLLKLLSSE 80
Cdd:COG0299    1 MKRIAVLISGRGSNLQALIDAIEAGDL-PAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730  81 EVQWIVLAGYMRLVGQDLLQAYEGRILNIHPSLLPKFKGLDAIGQALESGDTVTGSTVHYVDSGMDTGEIIEQQQCDIKP 160
Cdd:COG0299   80 GPDLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLP 159

                        170       180
                 ....*....|....*....|....*...
gi 487749730 161 DDTKEQLEDRVKHLEYELYPRVIAKIIK 188
Cdd:COG0299  160 DDTEETLAARILEQEHRLYPEAIRLLAE 187
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 3-185 2.95e-71

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: 213.77  E-value: 2.95e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730    3 NIAIFASGSGSNFENIVKHIQTGQLSGiNVTALYTDNEGVPCIDRAKNLNIPIHINKPKDFSSKSLYEQHLLKLLSSEEV 82
Cdd:TIGR00639   2 RIVVLISGNGSNLQAIIDACKEGKIPA-SVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730   83 QWIVLAGYMRLVGQDLLQAYEGRILNIHPSLLPKFKGLDAIGQALESGDTVTGSTVHYVDSGMDTGEIIEQQQCDIKPDD 162
Cdd:TIGR00639  81 DLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPED 160

                         170       180
                  ....*....|....*....|...
gi 487749730  163 TKEQLEDRVKHLEYELYPRVIAK 185
Cdd:TIGR00639 161 TEETLEQRIHKQEHRIYPLAIAW 183
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 3-183 3.26e-66

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: 200.60  E-value: 3.26e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730    3 NIAIFASGSGSNFENIVKHIQTGQLSGiNVTALYTDNEGVPCIDRAKNLNIPIHINKPKDFSSKSLYEQHLLKLLSSEEV 82
Cdd:pfam00551   2 KIAVLISGTGSNLQALIDALRKGGQDA-DVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730   83 QWIVLAGYMRLVGQDLLQAYEGRILNIHPSLLPKFKGLDAIGQALESGDTVTGSTVHYVDSGMDTGEIIEQQQCDIKPDD 162
Cdd:pfam00551  81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160

                         170       180
                  ....*....|....*....|.
gi 487749730  163 TKEQLEDRVKHLEYELYPRVI 183
Cdd:pfam00551 161 TAETLYNRVADLEHKALPRVL 181
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 3-186 7.07e-44

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 144.84  E-value: 7.07e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730   3 NIAIFASGSGSNFENIVKHIQTGQLSGiNVTALYTDNEGVPCIDRAKNLNIPIHINKPKDFSSKSLYEQHLLKLLSSEEV 82
Cdd:PLN02331   1 KLAVFVSGGGSNFRAIHDACLDGRVNG-DVVVVVTNKPGCGGAEYARENGIPVLVYPKTKGEPDGLSPDELVDALRGAGV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730  83 QWIVLAGYMRLVGQDLLQAYEGRILNIHPSLLPKFKGLDAIGQ-----ALESGDTVTGSTVHYVDSGMDTGEIIEQQQCD 157
Cdd:PLN02331  80 DFVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFGGKGYYGIkvhkaVIASGARYSGPTVHFVDEHYDTGRILAQRVVP 159

                        170       180
                 ....*....|....*....|....*....
gi 487749730 158 IKPDDTKEQLEDRVKHLEYELYPRVIAKI 186
Cdd:PLN02331 160 VLATDTPEELAARVLHEEHQLYVEVVAAL 188
 
Name Accession Description Interval E-value
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 3-186 2.22e-93

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: 269.64  E-value: 2.22e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730   3 NIAIFASGSGSNFENIVKHIQTGQLSGiNVTALYTDNEGVPCIDRAKNLNIPIHINKPKDFSSKSLYEQHLLKLLSSEEV 82
Cdd:cd08645    1 RIAVLASGSGSNLQALIDAIKSGKLNA-EIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730  83 QWIVLAGYMRLVGQDLLQAYEGRILNIHPSLLPKFKGLDAIGQALESGDTVTGSTVHYVDSGMDTGEIIEQQQCDIKPDD 162
Cdd:cd08645   80 DLIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGD 159

                        170       180
                 ....*....|....*....|....
gi 487749730 163 TKEQLEDRVKHLEYELYPRVIAKI 186
Cdd:cd08645  160 TPETLAERIHALEHRLYPEAIKLL 183
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 1-188 2.35e-91

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: 264.97  E-value: 2.35e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730   1 MTNIAIFASGSGSNFENIVKHIQTGQLsGINVTALYTDNEGVPCIDRAKNLNIPIHINKPKDFSSKSLYEQHLLKLLSSE 80
Cdd:COG0299    1 MKRIAVLISGRGSNLQALIDAIEAGDL-PAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730  81 EVQWIVLAGYMRLVGQDLLQAYEGRILNIHPSLLPKFKGLDAIGQALESGDTVTGSTVHYVDSGMDTGEIIEQQQCDIKP 160
Cdd:COG0299   80 GPDLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLP 159

                        170       180
                 ....*....|....*....|....*...
gi 487749730 161 DDTKEQLEDRVKHLEYELYPRVIAKIIK 188
Cdd:COG0299  160 DDTEETLAARILEQEHRLYPEAIRLLAE 187
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 3-185 2.95e-71

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: 213.77  E-value: 2.95e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730    3 NIAIFASGSGSNFENIVKHIQTGQLSGiNVTALYTDNEGVPCIDRAKNLNIPIHINKPKDFSSKSLYEQHLLKLLSSEEV 82
Cdd:TIGR00639   2 RIVVLISGNGSNLQAIIDACKEGKIPA-SVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730   83 QWIVLAGYMRLVGQDLLQAYEGRILNIHPSLLPKFKGLDAIGQALESGDTVTGSTVHYVDSGMDTGEIIEQQQCDIKPDD 162
Cdd:TIGR00639  81 DLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPED 160

                         170       180
                  ....*....|....*....|...
gi 487749730  163 TKEQLEDRVKHLEYELYPRVIAK 185
Cdd:TIGR00639 161 TEETLEQRIHKQEHRIYPLAIAW 183
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 3-183 3.26e-66

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: 200.60  E-value: 3.26e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730    3 NIAIFASGSGSNFENIVKHIQTGQLSGiNVTALYTDNEGVPCIDRAKNLNIPIHINKPKDFSSKSLYEQHLLKLLSSEEV 82
Cdd:pfam00551   2 KIAVLISGTGSNLQALIDALRKGGQDA-DVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730   83 QWIVLAGYMRLVGQDLLQAYEGRILNIHPSLLPKFKGLDAIGQALESGDTVTGSTVHYVDSGMDTGEIIEQQQCDIKPDD 162
Cdd:pfam00551  81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160

                         170       180
                  ....*....|....*....|.
gi 487749730  163 TKEQLEDRVKHLEYELYPRVI 183
Cdd:pfam00551 161 TAETLYNRVADLEHKALPRVL 181
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 3-186 7.07e-44

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 144.84  E-value: 7.07e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730   3 NIAIFASGSGSNFENIVKHIQTGQLSGiNVTALYTDNEGVPCIDRAKNLNIPIHINKPKDFSSKSLYEQHLLKLLSSEEV 82
Cdd:PLN02331   1 KLAVFVSGGGSNFRAIHDACLDGRVNG-DVVVVVTNKPGCGGAEYARENGIPVLVYPKTKGEPDGLSPDELVDALRGAGV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730  83 QWIVLAGYMRLVGQDLLQAYEGRILNIHPSLLPKFKGLDAIGQ-----ALESGDTVTGSTVHYVDSGMDTGEIIEQQQCD 157
Cdd:PLN02331  80 DFVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFGGKGYYGIkvhkaVIASGARYSGPTVHFVDEHYDTGRILAQRVVP 159

                        170       180
                 ....*....|....*....|....*....
gi 487749730 158 IKPDDTKEQLEDRVKHLEYELYPRVIAKI 186
Cdd:PLN02331 160 VLATDTPEELAARVLHEEHQLYVEVVAAL 188
FMT_core cd08369
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...
 4-185 5.16e-36

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: 123.55  E-value: 5.16e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730   4 IAIFasGSGSNFENIVKHIQTGqlSGINVTALYTDNEGVpcIDRAKNLNIPIHINKPKDfssKSLYEQHLLKLLSSEEVQ 83
Cdd:cd08369    1 IVIL--GSGNIGQRVLKALLSK--EGHEIVGVVTHPDSP--RGTAQLSLELVGGKVYLD---SNINTPELLELLKEFAPD 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730  84 WIVLAGYMRLVGQDLLQAYEGRILNIHPSLLPKFKGLDAIGQALESGDTVTGSTVHYVDSGMDTGEIIEQQQCDIKPDDT 163
Cdd:cd08369   72 LIVSINFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDT 151

                        170       180
                 ....*....|....*....|..
gi 487749730 164 KEQLEDRVKHLEYELYPRVIAK 185
Cdd:cd08369  152 AGTLYQRLIELGPKLLKEALQK 173
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
46-188 1.70e-30

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


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 112.89  E-value: 1.70e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730  46 DRAKNLNIPIHinKPKDFSSKSLYEQhllklLSSEEVQWIVLAGYMRLVGQDLLQAYEGRILNIHPSLLPKFKGLDAIGQ 125
Cdd:COG0223   50 ELALEHGIPVL--QPESLKDPEFLEE-----LRALNPDLIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAAPIQW 122

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487749730 126 ALESGDTVTGSTVHYVDSGMDTGEIIEQQQCDIKPDDTKEQLEDRVKHLEYELYPRVIAKIIK 188
Cdd:COG0223  123 AILNGDTETGVTIMQMDEGLDTGDILLQEEVPIGPDDTAGSLHDKLAELGAELLLETLDALEA 185
FMT_core_Met-tRNA-FMT_N cd08646
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ...
 47-188 6.94e-27

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: 100.98  E-value: 6.94e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730  47 RAKNLNIPIHinKPKDFSSKSLYEQhllklLSSEEVQWIVLAGYMRLVGQDLLQAYEGRILNIHPSLLPKFKGLDAIGQA 126
Cdd:cd08646   51 LALELGLPVL--QPEKLKDEEFLEE-----LKALKPDLIVVVAYGQILPKEILDLPPYGCINVHPSLLPKYRGAAPIQRA 123

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487749730 127 LESGDTVTGSTVHYVDSGMDTGEIIEQQQCDIKPDDTKEQLEDRVKHLEYELYPRVIAKIIK 188
Cdd:cd08646  124 ILNGDKETGVTIMKMDEGLDTGDILAQEEVPIDPDDTAGELLDKLAELGADLLLEVLDDIEA 185
PurU TIGR00655
formyltetrahydrofolate deformylase; This model describes formyltetrahydrofolate deformylases. ...
 3-169 2.92e-24

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: 95.96  E-value: 2.92e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730    3 NIAIFASGSGSNFENIVKHIQTGQLSGiNVTALYTDNEGVPCIdrAKNLNIP-IHINKPKDfsSKSLYEQHLLKLLSSEE 81
Cdd:TIGR00655  86 RVAILVSKEDHCLGDLLWRWYSGELDA-EIALVISNHEDLRSL--VERFGIPfHYIPATKD--NRVEHEKRQLELLKQYQ 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730   82 VQWIVLAGYMRLVGQDLLQAYEGRILNIHPSLLPKFKGLDAIGQALESGDTVTGSTVHYVDSGMDTGEIIEQqqcDIKPD 161
Cdd:TIGR00655 161 VDLVVLAKYMQILSPDFVKRYPNKIINIHHSFLPAFIGANPYQRAYERGVKIIGATAHYVTEELDEGPIIEQ---DVVRV 237


                  ....*...
gi 487749730  162 DTKEQLED 169
Cdd:TIGR00655 238 DHTDNVED 245
FMT_core_Formyl-FH4-Hydrolase_C cd08648
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ...
 3-167 2.10e-23

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: 91.85  E-value: 2.10e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730   3 NIAIFASGSGSNFENIVKHIQTGQLsginvtalytdNEGVPCI----DRAKNL----NIP-IHINKPKDfsSKSLYEQHL 73
Cdd:cd08648    2 RVAIFVSKEDHCLYDLLHRWREGEL-----------PCEIPLVisnhPDLRPLaerfGIPfHHIPVTKD--TKAEAEAEQ 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730  74 LKLLSSEEVQWIVLAGYMRLVGQDLLQAYEGRILNIHPSLLPKFKGLDAIGQALESGDTVTGSTVHYVDSGMDTGEIIEQ 153
Cdd:cd08648   69 LELLEEYGVDLVVLARYMQILSPDFVERYPNRIINIHHSFLPAFKGAKPYHQAFERGVKLIGATAHYVTEELDEGPIIEQ 148

                        170
                 ....*....|....
gi 487749730 154 QQCDIKPDDTKEQL 167
Cdd:cd08648  149 DVERVSHRDSVEDL 162
PurU COG0788
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ...
 48-167 9.23e-23

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: 92.03  E-value: 9.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730  48 AKNLNIP-IHINKPKDfsSKSLYEQHLLKLLSSEEVQWIVLAGYMRLVGQDLLQAYEGRILNIHPSLLPKFKGLDAIGQA 126
Cdd:COG0788  130 AEWFGIPfHHIPVTKE--TKAEAEARLLELLEEYDIDLVVLARYMQILSPDFCARLPGRIINIHHSFLPAFKGAKPYHQA 207

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 487749730 127 LESGDTVTGSTVHYVDSGMDTGEIIEQQQCDIKPDDTKEQL 167
Cdd:COG0788  208 YERGVKLIGATAHYVTADLDEGPIIEQDVERVDHRDTPEDL 248
purU PRK06027
formyltetrahydrofolate deformylase; Reviewed
 48-153 8.00e-21

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 235676 [Multi-domain]  Cd Length: 286  Bit Score: 86.70  E-value: 8.00e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730  48 AKNLNIP-IHINKPKDfsSKSLYEQHLLKLLSSEEVQWIVLAGYMRLVGQDLLQAYEGRILNIHPSLLPKFKGLDAIGQA 126
Cdd:PRK06027 133 VERFGIPfHHVPVTKE--TKAEAEARLLELIDEYQPDLVVLARYMQILSPDFVARFPGRIINIHHSFLPAFKGAKPYHQA 210

                         90       100
                 ....*....|....*....|....*..
gi 487749730 127 LESGDTVTGSTVHYVDSGMDTGEIIEQ 153
Cdd:PRK06027 211 YERGVKLIGATAHYVTADLDEGPIIEQ 237
FMT_core_like_3 cd08653
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 85-186 3.45e-20

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: 82.26  E-value: 3.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730  85 IVLAGYMRLVGQDLLQAYEGRILNIHPSLLPKFKGLDAIGQALESGDTV-TGSTVHYVDSGMDTGEIIEQQQCDIKPDDT 163
Cdd:cd08653   50 VVSVYGCGIIKDALLAIPPLGVLNLHGGILPDYRGVHTGFWALANGDPDnVGVTVHLVDAGIDTGDVLAQARPPLAAGDT 129

                         90       100
                 ....*....|....*....|...
gi 487749730 164 KEQLEDRVKHLEYELYPRVIAKI 186
Cdd:cd08653  130 LLSLYLRLYRAGVELMVEAIADL 152
fmt TIGR00460
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ...
 43-174 3.65e-20

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: 85.53  E-value: 3.65e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730   43 PCIDRAKNLNIPIhinkpkdFSSKSLYEQHLLKLLSSEEVQWIVLAGYMRLVGQDLLQAYEGRILNIHPSLLPKFKGLDA 122
Cdd:TIGR00460  47 PVKVLAEEKGIPV-------FQPEKQRQLEELPLVRELKPDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAP 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 487749730  123 IGQALESGDTVTGSTVHYVDSGMDTGEIIEQQQCDIKPDDTKEQLEDRVKHL 174
Cdd:TIGR00460 120 IQRAILNGDKKTGVTIMQMVPKMDAGDILKQETFPIEEEDNSGTLSDKLSEL 171
PRK13011 PRK13011
formyltetrahydrofolate deformylase; Reviewed
 48-153 1.72e-19

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 237266 [Multi-domain]  Cd Length: 286  Bit Score: 83.11  E-value: 1.72e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730  48 AKNLNIPIHiNKPKDFSSKSLYEQHLLKLLSSEEVQWIVLAGYMRLVGQDLLQAYEGRILNIHPSLLPKFKGLDAIGQAL 127
Cdd:PRK13011 133 AAWHGIPFH-HFPITPDTKPQQEAQVLDVVEESGAELVVLARYMQVLSPELCRKLAGRAINIHHSFLPGFKGAKPYHQAY 211

                         90       100
                 ....*....|....*....|....*.
gi 487749730 128 ESGDTVTGSTVHYVDSGMDTGEIIEQ 153
Cdd:PRK13011 212 ERGVKLIGATAHYVTDDLDEGPIIEQ 237
purU PRK13010
formyltetrahydrofolate deformylase; Reviewed
 48-153 1.28e-17

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 139334 [Multi-domain]  Cd Length: 289  Bit Score: 78.30  E-value: 1.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730  48 AKNLNIPIHiNKPKDFSSKSLYEQHLLKLLSSEEVQWIVLAGYMRLVGQDLLQAYEGRILNIHPSLLPKFKGLDAIGQAL 127
Cdd:PRK13010 137 AVQHDIPFH-HLPVTPDTKAQQEAQILDLIETSGAELVVLARYMQVLSDDLSRKLSGRAINIHHSFLPGFKGARPYHQAH 215

                         90       100
                 ....*....|....*....|....*.
gi 487749730 128 ESGDTVTGSTVHYVDSGMDTGEIIEQ 153
Cdd:PRK13010 216 ARGVKLIGATAHFVTDDLDEGPIIEQ 241
PLN02828 PLN02828
formyltetrahydrofolate deformylase
 70-183 3.03e-16

formyltetrahydrofolate deformylase


Pssm-ID: 178422  Cd Length: 268  Bit Score: 74.40  E-value: 3.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730  70 EQHLLKLLSSEEvqWIVLAGYMRLVGQDLLQAYEGRILNIHPSLLPKFKGLDAIGQALESGDTVTGSTVHYVDSGMDTGE 149
Cdd:PLN02828 138 EDEILELVKGTD--FLVLARYMQILSGNFLKGYGKDIINIHHGLLPSFKGGNPSKQAFDAGVKLIGATSHFVTEELDAGP 215

                         90       100       110
                 ....*....|....*....|....*....|....
gi 487749730 150 IIEQQQCDIKPDDTKEQLEDRVKHLEYELYPRVI 183
Cdd:PLN02828 216 IIEQMVERVSHRDNLRSFVQKSENLEKQCLAKAI 249
FMT_core_like_4 cd08651
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 71-186 1.07e-14

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


Pssm-ID: 187720 [Multi-domain]  Cd Length: 180  Bit Score: 68.45  E-value: 1.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730  71 QHLLKLLSSEEVQWIVLAGYMRLVGQDLLQAYEGRILNIHPSLLPKFKGLDAIGQALESGDTVTGSTVHYVDSGMDTGEI 150
Cdd:cd08651   65 EEIIEWIKEANPDIIFVFGWSQLLKPEILAIPRLGVIGFHPTKLPKNRGRAPIPWAILLGLKETASTFFWMDEGADSGDI 144

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 487749730 151 IEQQQCDIKPDDTKEQLEDRVKHLEYELYPRVIAKI 186
Cdd:cd08651  145 LSQEPFPIDKDDTANSLYDKIMEAAKQQIDKFLPRL 180
FMT_core_like_2 cd08822
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 85-171 1.33e-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: 187724 [Multi-domain]  Cd Length: 192  Bit Score: 68.64  E-value: 1.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730  85 IVLAGYMRLVGQDLLQAYEGRILNIHPSLLPKFKGLDAIGQALESGDTVTGSTVHYVDSGMDTGEIIEQQQCDIKPDDTK 164
Cdd:cd08822   70 IVAAHCHAFISAKTRARARLGAIGYHPSLLPRHRGRDAVEWTIRMRDPITGGTVYHLDDGVDGGPIAAQDWCHVRPGDTA 149


                 ....*..
gi 487749730 165 EQLEDRV 171
Cdd:cd08822  150 AELWRRA 156
FMT_core_FDH_N cd08647
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ...
 110-184 1.43e-14

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: 68.63  E-value: 1.43e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487749730 110 HPSLLPKFKGLDAIGQALESGDTVTGSTVHYVDSGMDTGEIIEQQQCDIKPDDTKEQLEDRVkhleyeLYPRVIA 184
Cdd:cd08647  106 HPSILPRHRGASAINWTLIHGDKKAGFTIFWADDGLDTGPILLQKECDVLPNDTVDTLYNRF------LYPEGIK 174
PLN02285 PLN02285
methionyl-tRNA formyltransferase
 70-170 5.84e-14

methionyl-tRNA formyltransferase


Pssm-ID: 215159 [Multi-domain]  Cd Length: 334  Bit Score: 68.57  E-value: 5.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730  70 EQHLLKLLSSEEVQWIVLAGYMRLVGQDLLQAYEGRILNIHPSLLPKFKGLDAIGQALESGDTVTGSTVHYVDSGMDTGE 149
Cdd:PLN02285  82 EEDFLSALRELQPDLCITAAYGNILPQKFLDIPKLGTVNIHPSLLPLYRGAAPVQRALQDGVNETGVSVAFTVRALDAGP 161

                         90       100
                 ....*....|....*....|.
gi 487749730 150 IIEQQQCDIKPDDTKEQLEDR 170
Cdd:PLN02285 162 VIAQERVEVDEDIKAPELLPL 182
FMT_core_ArnA_N cd08644
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ...
 29-188 9.34e-14

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: 66.60  E-value: 9.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730  29 GINVTALYT--DNEG----VPCIDR-AKNLNIPIHInkPKDFSSKSLYEQhlLKLLSSEevqwIVLAGYMR-LVGQDLLQ 100
Cdd:cd08644   23 GFEVVAVFThtDNPGeniwFGSVAQlAREHGIPVFT--PDDINHPEWVER--LRALKPD----LIFSFYYRhMISEDILE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730 101 AYEGRILNIHPSLLPKFKGLDAIGQALESGDTVTGSTVHYVDSGMDTGEIIEQQQCDIKPDDTKEQLEDRVKHLEYELYP 180
Cdd:cd08644   95 IARLGAFNLHGSLLPKYRGRAPLNWALINGETETGVTLHRMTKKPDAGAIVDQEKVPILPDDTAKSLFHKLCVAARRLLA 174


                 ....*...
gi 487749730 181 RVIAKIIK 188
Cdd:cd08644  175 RTLPALKA 182
FMT_core_NRPS_like cd08649
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ...
 22-163 3.31e-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: 64.20  E-value: 3.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730  22 IQTGQL---SGINVTALYTDNEGVpcIDRAKNLNIPIHINkpkdfsskslyEQHLLKLLSSEEVQWIVLAGYMRLVGQDL 98
Cdd:cd08649   12 IQCAEQllaAGHRIAAVVSTDPAI--RAWAAAEGIAVLEP-----------GEALEELLSDEPFDWLFSIVNLRILPSEV 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487749730  99 LQAYEGRILNIHPSLLPKFKGLDAIGQALESGDTVTGSTVHYVDSGMDTGEIIEQQQCDIKPDDT 163
Cdd:cd08649   79 LALPRKGAINFHDGPLPRYAGLNATSWALLAGETRHGVTWHRIEEGVDAGDILVQRPFDIAPDDT 143
PRK06988 PRK06988
formyltransferase;
90-171 1.43e-12

formyltransferase;


Pssm-ID: 235902 [Multi-domain]  Cd Length: 312  Bit Score: 64.33  E-value: 1.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730  90 YMRLVGQDLLQAYEGRILNIHPSLLPKFKGLDAIGQALESGDTVTGSTVHYVDSGMDTGEIIEQQQCDIKPDDTKEQLED 169
Cdd:PRK06988  86 YRHMIPVDLLALAPRGAYNMHGSLLPKYRGRVPVNWAVLNGETETGATLHEMVAKPDAGAIVDQTAVPILPDDTAAQVFD 165


                 ..
gi 487749730 170 RV 171
Cdd:PRK06988 166 KV 167
FMT_core_like_5 cd08823
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 86-186 6.89e-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: 187725 [Multi-domain]  Cd Length: 177  Bit Score: 60.92  E-value: 6.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730  86 VLAGYMRLVGQDLLQAYEGRILNIHPSLLPKFKGLDAIGQALESGDTVTGSTVHYVDSGMDTGEIIEQQQCDIKPDDTKE 165
Cdd:cd08823   76 VVFTFPYRIPQHILDLPPLGFYNLHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMTAEIDRGPIVLEQFTPIHPDDTYG 155

                         90       100
                 ....*....|....*....|.
gi 487749730 166 QLEDRVKHLEYELYPRVIAKI 186
Cdd:cd08823  156 LLCSRLAMLAVGLLEELYQNL 176
PRK08125 PRK08125
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ...
 90-186 4.75e-11

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


Pssm-ID: 236156 [Multi-domain]  Cd Length: 660  Bit Score: 60.77  E-value: 4.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730  90 YMRLVGQDLLQAYEGRILNIHPSLLPKFKGLDAIGQALESGDTVTGSTVHYVDSGMDTGEIIEQQQCDIKPDDTKEQLED 169
Cdd:PRK08125  84 YRNLLSDEILQLAPAGAFNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQQRVAIAPDDTALTLHH 163

                         90
                 ....*....|....*..
gi 487749730 170 RVKHLEYELYPRVIAKI 186
Cdd:PRK08125 164 KLCHAARQLLEQTLPAI 180
FMT_core_like_6 cd08820
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 73-167 2.12e-09

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


Pssm-ID: 187722 [Multi-domain]  Cd Length: 173  Bit Score: 53.98  E-value: 2.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730  73 LLKLLSSEEVQWIVLAGYMRLVGQDLLQAYEGRILNIHPSLLPKFKGLDAIGQALESGDTVTGSTVHYVDSGMDTGEIIE 152
Cdd:cd08820   61 LLEILENKGVDILISVQYHWILPGSILEKAKEIAFNLHNAPLPEYRGCNQFSHAILNGDDQFGTTIHWMAEGIDSGDIIF 140

                         90
                 ....*....|....*
gi 487749730 153 QQQCDIKPDDTKEQL 167
Cdd:cd08820  141 EKRFPIPSDCTVISL 155
PRK07579 PRK07579
dTDP-4-amino-4,6-dideoxyglucose formyltransferase;
45-186 1.69e-06

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


Pssm-ID: 236058 [Multi-domain]  Cd Length: 245  Bit Score: 46.82  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749730  45 IDRAKNLNIPI-HINKPKDFSSKSLYEQHLLKLLSSEEVQWIVlAGYMRLVGQDLLQAYEG------RILNIHPSLLPKF 117
Cdd:PRK07579  21 IARKNDMDVDYfCSFKSQTSFAKEIYQSPIKQLDVAERVAEIV-ERYDLVLSFHCKQRFPAklvngvRCINIHPGFNPYN 99

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 487749730 118 KGLDAIGQALESGDTVtGSTVHYVDSGMDTGEIIEQQQCDIKPDDTKEQLEDRVKHLEYELYPRVIAKI 186
Cdd:PRK07579 100 RGWFPQVFSIINGLKI-GATIHEMDEQLDHGPIIAQREVEIESWDSSGSVYARVMDIERELVLEHFDAI 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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