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Conserved domains on  [gi|1016362974|ref|WP_063032450|]
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phosphoribosylglycinamide formyltransferase [Pseudomonas yamanorum]

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 ...
 7-205 1.70e-120

Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and metabolism]; Folate-dependent phosphoribosylglycinamide formyltransferase PurN is part of the Pathway/BioSystem: Purine biosynthesis


:

Pssm-ID: 440068 [Multi-domain]  Cd Length: 202  Bit Score: 340.09  E-value: 1.70e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974   7 VVVLLSGTGSNLQALIDSTRTGDSPVRIAAVISNRSDAYGLQRARDAGIDTRSLDHKAFEGREAFDSALIELIDAFNPKL 86
Cdd:COG0299     4 IAVLISGRGSNLQALIDAIEAGDLPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYGPDL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974  87 VVLAGFMRILSADFVRHYNGRLLNIHPSLLPKYKGLHTHQRALEAGDTEHGCSVHFVTEELDGGPLVVQAVVPVESEDSA 166
Cdd:COG0299    84 VVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDDTE 163

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1016362974 167 QTLAQRVHTQEHRIYPLAVRWFAEGRLILGDHGALLDGQ 205
Cdd:COG0299   164 ETLAARILEQEHRLYPEAIRLLAEGRLTLDGRRVRLDGE 202
 
Name Accession Description Interval E-value
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 7-205 1.70e-120

Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and metabolism]; Folate-dependent phosphoribosylglycinamide formyltransferase PurN is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440068 [Multi-domain]  Cd Length: 202  Bit Score: 340.09  E-value: 1.70e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974   7 VVVLLSGTGSNLQALIDSTRTGDSPVRIAAVISNRSDAYGLQRARDAGIDTRSLDHKAFEGREAFDSALIELIDAFNPKL 86
Cdd:COG0299     4 IAVLISGRGSNLQALIDAIEAGDLPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYGPDL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974  87 VVLAGFMRILSADFVRHYNGRLLNIHPSLLPKYKGLHTHQRALEAGDTEHGCSVHFVTEELDGGPLVVQAVVPVESEDSA 166
Cdd:COG0299    84 VVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDDTE 163

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1016362974 167 QTLAQRVHTQEHRIYPLAVRWFAEGRLILGDHGALLDGQ 205
Cdd:COG0299   164 ETLAARILEQEHRLYPEAIRLLAEGRLTLDGRRVRLDGE 202
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 7-188 1.95e-106

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: 303.92  E-value: 1.95e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974   7 VVVLLSGTGSNLQALIDSTRTGDSPVRIAAVISNRSDAYGLQRARDAGIDTRSLDHKAFEGREAFDSALIELIDAFNPKL 86
Cdd:cd08645     2 IAVLASGSGSNLQALIDAIKSGKLNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKVDL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974  87 VVLAGFMRILSADFVRHYNGRLLNIHPSLLPKYKGLHTHQRALEAGDTEHGCSVHFVTEELDGGPLVVQAVVPVESEDSA 166
Cdd:cd08645    82 IVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDTP 161

                         170       180
                  ....*....|....*....|..
gi 1016362974 167 QTLAQRVHTQEHRIYPLAVRWF 188
Cdd:cd08645   162 ETLAERIHALEHRLYPEAIKLL 183
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 7-194 3.69e-95

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: 275.40  E-value: 3.69e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974   7 VVVLLSGTGSNLQALIDSTRTGDSPVRIAAVISNRSDAYGLQRARDAGIDTRSLDHKAFEGREAFDSALIELIDAFNPKL 86
Cdd:TIGR00639   3 IVVLISGNGSNLQAIIDACKEGKIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEVDL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974  87 VVLAGFMRILSADFVRHYNGRLLNIHPSLLPKYKGLHTHQRALEAGDTEHGCSVHFVTEELDGGPLVVQAVVPVESEDSA 166
Cdd:TIGR00639  83 VVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPEDTE 162

                         170       180
                  ....*....|....*....|....*...
gi 1016362974 167 QTLAQRVHTQEHRIYPLAVRWFAEGRLI 194
Cdd:TIGR00639 163 ETLEQRIHKQEHRIYPLAIAWFAQGRLK 190
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 7-185 2.01e-80

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: 237.96  E-value: 2.01e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974   7 VVVLLSGTGSNLQALIDSTRTGDSPVRIAAVISNRSDAYGLQRARDAGIDTRSLDHKAFEGREAFDSALIELIDAFNPKL 86
Cdd:pfam00551   3 IAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAADV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974  87 VVLAGFMRILSADFVRHYNGRLLNIHPSLLPKYKGLHTHQRALEAGDTEHGCSVHFVTEELDGGPLVVQAVVPVESEDSA 166
Cdd:pfam00551  83 IVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDDTA 162

                         170
                  ....*....|....*....
gi 1016362974 167 QTLAQRVHTQEHRIYPLAV 185
Cdd:pfam00551 163 ETLYNRVADLEHKALPRVL 181
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 7-199 1.15e-38

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 132.51  E-value: 1.15e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974   7 VVVLLSGTGSNLQALIDSTRTGDSPVRIAAVISNRSDAYGLQRARDAGIDTRSLDHKAFEGREAFDSALIELIDAFNPKL 86
Cdd:PLN02331    2 LAVFVSGGGSNFRAIHDACLDGRVNGDVVVVVTNKPGCGGAEYARENGIPVLVYPKTKGEPDGLSPDELVDALRGAGVDF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974  87 VVLAGFMRILSADFVRHYNGRLLNIHPSLLPK-----YKGLHTHQRALEAGDTEHGCSVHFVTEELDGGPLVVQAVVPVE 161
Cdd:PLN02331   82 VLLAGYLKLIPVELVRAYPRSILNIHPALLPAfggkgYYGIKVHKAVIASGARYSGPTVHFVDEHYDTGRILAQRVVPVL 161

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1016362974 162 SEDSAQTLAQRVHTQEHRIYPLAVRWFAEGRLILGDHG 199
Cdd:PLN02331  162 ATDTPEELAARVLHEEHQLYVEVVAALCEERIVWREDG 199
 
Name Accession Description Interval E-value
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 7-205 1.70e-120

Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and metabolism]; Folate-dependent phosphoribosylglycinamide formyltransferase PurN is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440068 [Multi-domain]  Cd Length: 202  Bit Score: 340.09  E-value: 1.70e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974   7 VVVLLSGTGSNLQALIDSTRTGDSPVRIAAVISNRSDAYGLQRARDAGIDTRSLDHKAFEGREAFDSALIELIDAFNPKL 86
Cdd:COG0299     4 IAVLISGRGSNLQALIDAIEAGDLPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYGPDL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974  87 VVLAGFMRILSADFVRHYNGRLLNIHPSLLPKYKGLHTHQRALEAGDTEHGCSVHFVTEELDGGPLVVQAVVPVESEDSA 166
Cdd:COG0299    84 VVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDDTE 163

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1016362974 167 QTLAQRVHTQEHRIYPLAVRWFAEGRLILGDHGALLDGQ 205
Cdd:COG0299   164 ETLAARILEQEHRLYPEAIRLLAEGRLTLDGRRVRLDGE 202
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 7-188 1.95e-106

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: 303.92  E-value: 1.95e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974   7 VVVLLSGTGSNLQALIDSTRTGDSPVRIAAVISNRSDAYGLQRARDAGIDTRSLDHKAFEGREAFDSALIELIDAFNPKL 86
Cdd:cd08645     2 IAVLASGSGSNLQALIDAIKSGKLNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKVDL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974  87 VVLAGFMRILSADFVRHYNGRLLNIHPSLLPKYKGLHTHQRALEAGDTEHGCSVHFVTEELDGGPLVVQAVVPVESEDSA 166
Cdd:cd08645    82 IVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDTP 161

                         170       180
                  ....*....|....*....|..
gi 1016362974 167 QTLAQRVHTQEHRIYPLAVRWF 188
Cdd:cd08645   162 ETLAERIHALEHRLYPEAIKLL 183
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 7-194 3.69e-95

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: 275.40  E-value: 3.69e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974   7 VVVLLSGTGSNLQALIDSTRTGDSPVRIAAVISNRSDAYGLQRARDAGIDTRSLDHKAFEGREAFDSALIELIDAFNPKL 86
Cdd:TIGR00639   3 IVVLISGNGSNLQAIIDACKEGKIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEVDL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974  87 VVLAGFMRILSADFVRHYNGRLLNIHPSLLPKYKGLHTHQRALEAGDTEHGCSVHFVTEELDGGPLVVQAVVPVESEDSA 166
Cdd:TIGR00639  83 VVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPEDTE 162

                         170       180
                  ....*....|....*....|....*...
gi 1016362974 167 QTLAQRVHTQEHRIYPLAVRWFAEGRLI 194
Cdd:TIGR00639 163 ETLEQRIHKQEHRIYPLAIAWFAQGRLK 190
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 7-185 2.01e-80

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: 237.96  E-value: 2.01e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974   7 VVVLLSGTGSNLQALIDSTRTGDSPVRIAAVISNRSDAYGLQRARDAGIDTRSLDHKAFEGREAFDSALIELIDAFNPKL 86
Cdd:pfam00551   3 IAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAADV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974  87 VVLAGFMRILSADFVRHYNGRLLNIHPSLLPKYKGLHTHQRALEAGDTEHGCSVHFVTEELDGGPLVVQAVVPVESEDSA 166
Cdd:pfam00551  83 IVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDDTA 162

                         170
                  ....*....|....*....
gi 1016362974 167 QTLAQRVHTQEHRIYPLAV 185
Cdd:pfam00551 163 ETLYNRVADLEHKALPRVL 181
PurU COG0788
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ...
 7-195 4.32e-39

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: 135.56  E-value: 4.32e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974   7 VVVLLSGTGSNLQALIDSTRTGDSPVRIAAVISNRSDAYGLqrARDAGIDTRSLDHKAfEGREAFDSALIELIDAFNPKL 86
Cdd:COG0788    89 VAILVSKEDHCLNDLLYRWRSGELPAEIPAVISNHPDLRPL--AEWFGIPFHHIPVTK-ETKAEAEARLLELLEEYDIDL 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974  87 VVLAGFMRILSADFVRHYNGRLLNIHPSLLPKYKGLHTHQRALEAGDTEHGCSVHFVTEELDGGPLVVQAVVPVESEDSA 166
Cdd:COG0788   166 VVLARYMQILSPDFCARLPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVERVDHRDTP 245

                         170       180
                  ....*....|....*....|....*....
gi 1016362974 167 QTLAQRVHTQEHRIYPLAVRWFAEGRLIL 195
Cdd:COG0788   246 EDLVRKGRDVEKRVLARAVRWHLEDRVLV 274
FMT_core cd08369
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...
 9-187 4.53e-39

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: 132.41  E-value: 4.53e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974   9 VLLSGTGSNLQALIDSTRTGDSPVrIAAVISNRSDAYGlqrarDAGIDTRSLDHKAFEGREAFDSALIELIDAFNPKLVV 88
Cdd:cd08369     1 IVILGSGNIGQRVLKALLSKEGHE-IVGVVTHPDSPRG-----TAQLSLELVGGKVYLDSNINTPELLELLKEFAPDLIV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974  89 LAGFMRILSADFVRHYNGRLLNIHPSLLPKYKGLHTHQRALEAGDTEHGCSVHFVTEELDGGPLVVQAVVPVESEDSAQT 168
Cdd:cd08369    75 SINFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTAGT 154

                         170
                  ....*....|....*....
gi 1016362974 169 LAQRVHTQEHRIYPLAVRW 187
Cdd:cd08369   155 LYQRLIELGPKLLKEALQK 173
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 7-199 1.15e-38

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 132.51  E-value: 1.15e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974   7 VVVLLSGTGSNLQALIDSTRTGDSPVRIAAVISNRSDAYGLQRARDAGIDTRSLDHKAFEGREAFDSALIELIDAFNPKL 86
Cdd:PLN02331    2 LAVFVSGGGSNFRAIHDACLDGRVNGDVVVVVTNKPGCGGAEYARENGIPVLVYPKTKGEPDGLSPDELVDALRGAGVDF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974  87 VVLAGFMRILSADFVRHYNGRLLNIHPSLLPK-----YKGLHTHQRALEAGDTEHGCSVHFVTEELDGGPLVVQAVVPVE 161
Cdd:PLN02331   82 VLLAGYLKLIPVELVRAYPRSILNIHPALLPAfggkgYYGIKVHKAVIASGARYSGPTVHFVDEHYDTGRILAQRVVPVL 161

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1016362974 162 SEDSAQTLAQRVHTQEHRIYPLAVRWFAEGRLILGDHG 199
Cdd:PLN02331  162 ATDTPEELAARVLHEEHQLYVEVVAALCEERIVWREDG 199
FMT_core_Formyl-FH4-Hydrolase_C cd08648
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ...
 7-195 2.15e-35

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: 123.83  E-value: 2.15e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974   7 VVVLLSGTGSNLQALIDSTRTGDSPVRIAAVISNRSDAYGLqrARDAGIDTRSLDHKAfEGREAFDSALIELIDAFNPKL 86
Cdd:cd08648     3 VAIFVSKEDHCLYDLLHRWREGELPCEIPLVISNHPDLRPL--AERFGIPFHHIPVTK-DTKAEAEAEQLELLEEYGVDL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974  87 VVLAGFMRILSADFVRHYNGRLLNIHPSLLPKYKGLHTHQRALEAGDTEHGCSVHFVTEELDGGPLVVQAVVPVESEDSA 166
Cdd:cd08648    80 VVLARYMQILSPDFVERYPNRIINIHHSFLPAFKGAKPYHQAFERGVKLIGATAHYVTEELDEGPIIEQDVERVSHRDSV 159

                         170       180
                  ....*....|....*....|....*....
gi 1016362974 167 QTLAQRVHTQEHRIYPLAVRWFAEGRLIL 195
Cdd:cd08648   160 EDLVRKGRDIEKQVLARAVKWHLEDRVLV 188
purU PRK06027
formyltetrahydrofolate deformylase; Reviewed
 7-199 2.77e-33

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 235676 [Multi-domain]  Cd Length: 286  Bit Score: 120.60  E-value: 2.77e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974   7 VVVLLSGTGSNLQALIDSTRTGDSPVRIAAVISNRSDAYGLqrARDAGIDTRSLDHKAfEGREAFDSALIELIDAFNPKL 86
Cdd:PRK06027   92 VVILVSKEDHCLGDLLWRWRSGELPVEIAAVISNHDDLRSL--VERFGIPFHHVPVTK-ETKAEAEARLLELIDEYQPDL 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974  87 VVLAGFMRILSADFVRHYNGRLLNIHPSLLPKYKGLHTHQRALEAGDTEHGCSVHFVTEELDGGPLVVQAVVPVESEDSA 166
Cdd:PRK06027  169 VVLARYMQILSPDFVARFPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVIRVDHRDTA 248

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1016362974 167 QTLAQRVHTQEHRIYPLAVRWFAEGRLILgdHG 199
Cdd:PRK06027  249 EDLVRAGRDVEKQVLARAVRWHLEDRVLV--YG 279
purU PRK13010
formyltetrahydrofolate deformylase; Reviewed
 7-195 1.53e-25

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 139334 [Multi-domain]  Cd Length: 289  Bit Score: 100.64  E-value: 1.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974   7 VVVLLSGTGSNLQALIDSTRTGDSPVRIAAVISNRSDAYGLqrARDAGIDTRSLDhKAFEGREAFDSALIELIDAFNPKL 86
Cdd:PRK13010   96 VVIMVSKFDHCLNDLLYRWRMGELDMDIVGIISNHPDLQPL--AVQHDIPFHHLP-VTPDTKAQQEAQILDLIETSGAEL 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974  87 VVLAGFMRILSADFVRHYNGRLLNIHPSLLPKYKGLHTHQRALEAGDTEHGCSVHFVTEELDGGPLVVQAVVPVESEDSA 166
Cdd:PRK13010  173 VVLARYMQVLSDDLSRKLSGRAINIHHSFLPGFKGARPYHQAHARGVKLIGATAHFVTDDLDEGPIIEQDVERVDHSYSP 252

                         170       180
                  ....*....|....*....|....*....
gi 1016362974 167 QTLAQRVHTQEHRIYPLAVRWFAEGRLIL 195
Cdd:PRK13010  253 EDLVAKGRDVECLTLARAVKAFIEHRVFI 281
PRK13011 PRK13011
formyltetrahydrofolate deformylase; Reviewed
 7-195 1.17e-24

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 237266 [Multi-domain]  Cd Length: 286  Bit Score: 98.13  E-value: 1.17e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974   7 VVVLLSGTGSNLQALIDSTRTGDSPVRIAAVISNRSDAYGLqrARDAGIDTRSL----DHKAfeGREAfdsALIELIDAF 82
Cdd:PRK13011   92 VLIMVSKFDHCLNDLLYRWRIGELPMDIVGVVSNHPDLEPL--AAWHGIPFHHFpitpDTKP--QQEA---QVLDVVEES 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974  83 NPKLVVLAGFMRILSADFVRHYNGRLLNIHPSLLPKYKGLHTHQRALEAGDTEHGCSVHFVTEELDGGPLVVQAVVPVES 162
Cdd:PRK13011  165 GAELVVLARYMQVLSPELCRKLAGRAINIHHSFLPGFKGAKPYHQAYERGVKLIGATAHYVTDDLDEGPIIEQDVERVDH 244

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1016362974 163 EDSAQTLAQRVHTQEHRIYPLAVRWFAEGRLIL 195
Cdd:PRK13011  245 AYSPEDLVAKGRDVECLTLARAVKAHIERRVFL 277
PLN02828 PLN02828
formyltetrahydrofolate deformylase
 7-194 4.12e-23

formyltetrahydrofolate deformylase


Pssm-ID: 178422  Cd Length: 268  Bit Score: 93.66  E-value: 4.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974   7 VVVLLSGTGSNLQALIDSTRTGDSPVRIAAVISNR---SDAYGLQRARDAGIDTRSLDHKAFEGREAfdsALIELIDafN 83
Cdd:PLN02828   73 IAVLASKQDHCLIDLLHRWQDGRLPVDITCVISNHergPNTHVMRFLERHGIPYHYLPTTKENKRED---EILELVK--G 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974  84 PKLVVLAGFMRILSADFVRHYNGRLLNIHPSLLPKYKGLHTHQRALEAGDTEHGCSVHFVTEELDGGPLVVQAVVPVESE 163
Cdd:PLN02828  148 TDFLVLARYMQILSGNFLKGYGKDIINIHHGLLPSFKGGNPSKQAFDAGVKLIGATSHFVTEELDAGPIIEQMVERVSHR 227

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1016362974 164 DSAQTLAQRVHTQEHRIYPLAVRWFAEGRLI 194
Cdd:PLN02828  228 DNLRSFVQKSENLEKQCLAKAIKSYCELRVL 258
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
18-173 8.56e-22

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


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 90.55  E-value: 8.56e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974  18 LQALIDStrtgdsPVRIAAVISNRSDAYGL----------QRARDAGID---TRSLDhkafegreafDSALIELIDAFNP 84
Cdd:COG0223    16 LEALLAA------GHEVVAVVTQPDRPAGRgrkltpspvkELALEHGIPvlqPESLK----------DPEFLEELRALNP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974  85 KLVVLAGFMRILSA---DFVRHyngRLLNIHPSLLPKYKGLHTHQRALEAGDTEHGCSVHFVTEELDGGPLVVQAVVPVE 161
Cdd:COG0223    80 DLIVVVAYGQILPKevlDIPRL---GCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDTGDILLQEEVPIG 156

                         170
                  ....*....|..
gi 1016362974 162 SEDSAQTLAQRV 173
Cdd:COG0223   157 PDDTAGSLHDKL 168
PLN02285 PLN02285
methionyl-tRNA formyltransferase
 18-172 9.34e-21

methionyl-tRNA formyltransferase


Pssm-ID: 215159 [Multi-domain]  Cd Length: 334  Bit Score: 88.21  E-value: 9.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974  18 LQALIDSTRTGDSPVRIAAVISNRSDAYG----------LQRARDAGIDTRSLDHKAFEGREAFDSALIELidafNPKLV 87
Cdd:PLN02285   22 LDALLDASQAPDSAFEVAAVVTQPPARRGrgrklmpspvAQLALDRGFPPDLIFTPEKAGEEDFLSALREL----QPDLC 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974  88 VLAGFMRILSADFVRHYNGRLLNIHPSLLPKYKGLHTHQRALEAGDTEHGCSVHFVTEELDGGPLVVQAVVPVESEDSAQ 167
Cdd:PLN02285   98 ITAAYGNILPQKFLDIPKLGTVNIHPSLLPLYRGAAPVQRALQDGVNETGVSVAFTVRALDAGPVIAQERVEVDEDIKAP 177


                  ....*
gi 1016362974 168 TLAQR 172
Cdd:PLN02285  178 ELLPL 182
FMT_core_like_3 cd08653
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 72-173 6.44e-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: 6.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974  72 DSALIELIDAFNPKLVVLAGfMRILSADFVRHYNGRLLNIHPSLLPKYKGLHTHQRALEAGDTEH-GCSVHFVTEELDGG 150
Cdd:cd08653    36 GPEVVAALRALAPDVVSVYG-CGIIKDALLAIPPLGVLNLHGGILPDYRGVHTGFWALANGDPDNvGVTVHLVDAGIDTG 114

                          90       100
                  ....*....|....*....|...
gi 1016362974 151 PLVVQAVVPVESEDSAQTLAQRV 173
Cdd:cd08653   115 DVLAQARPPLAAGDTLLSLYLRL 137
fmt TIGR00460
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ...
 75-173 4.10e-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: 83.60  E-value: 4.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974  75 LIELIDAFNPKLVVLAGFMRILSADFVRHYNGRLLNIHPSLLPKYKGLHTHQRALEAGDTEHGCSVHFVTEELDGGPLVV 154
Cdd:TIGR00460  70 ELPLVRELKPDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVPKMDAGDILK 149

                          90
                  ....*....|....*....
gi 1016362974 155 QAVVPVESEDSAQTLAQRV 173
Cdd:TIGR00460 150 QETFPIEEEDNSGTLSDKL 168
FMT_core_Met-tRNA-FMT_N cd08646
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ...
 72-172 2.17e-18

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: 79.41  E-value: 2.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974  72 DSALIELIDAFNPKLVVLAGFMRILSADFVRHYNGRLLNIHPSLLPKYKG---LhthQRALEAGDTEHGCSVHFVTEELD 148
Cdd:cd08646    67 DEEFLEELKALKPDLIVVVAYGQILPKEILDLPPYGCINVHPSLLPKYRGaapI---QRAILNGDKETGVTIMKMDEGLD 143

                          90       100
                  ....*....|....*....|....
gi 1016362974 149 GGPLVVQAVVPVESEDSAQTLAQR 172
Cdd:cd08646   144 TGDILAQEEVPIDPDDTAGELLDK 167
FMT_core_NRPS_like cd08649
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ...
 94-169 7.24e-12

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: 61.12  E-value: 7.24e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1016362974  94 RILSADFVRHYNGRLLNIHPSLLPKYKGLHTHQRALEAGDTEHGCSVHFVTEELDGGPLVVQAVVPVESEDSAQTL 169
Cdd:cd08649    72 RILPSEVLALPRKGAINFHDGPLPRYAGLNATSWALLAGETRHGVTWHRIEEGVDAGDILVQRPFDIAPDDTALSL 147
FMT_core_like_5 cd08823
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 75-173 3.69e-11

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


Pssm-ID: 187725 [Multi-domain]  Cd Length: 177  Bit Score: 59.38  E-value: 3.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974  75 LIELIDAFNPKLVVLAGFMRILSADFVRHYNGRLLNIHPSLLPKYKGLHTHQRALEAGDTEHGCSVHFVTEELDGGPLVV 154
Cdd:cd08823    63 LAEWLRALAADTVVVFTFPYRIPQHILDLPPLGFYNLHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMTAEIDRGPIVL 142

                          90
                  ....*....|....*....
gi 1016362974 155 QAVVPVESEDSAQTLAQRV 173
Cdd:cd08823   143 EQFTPIHPDDTYGLLCSRL 161
FMT_core_ArnA_N cd08644
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ...
 76-180 1.04e-10

ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for the modification of lipid A with 4-amino-4-deoxy-L-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. The C-terminal dehydrogenase domain of ArnA catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O), while the N-terminal formyltransferase domain of ArnA catalyzes the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). This domain family represents the catalytic core of the N-terminal formyltransferase domain. The formyltransferase also contains a smaller C-terminal domain the may be involved in substrate binding. ArnA forms a hexameric structure, in which the dehydrogenase domains are arranged at the center of the particle with the transformylase domains on the outside of the particle.


Pssm-ID: 187713 [Multi-domain]  Cd Length: 203  Bit Score: 58.90  E-value: 1.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974  76 IELIDAFNPKLVVLAGFMRILSADFVRHYNGRLLNIHPSLLPKYKGLHTHQRALEAGDTEHGCSVHFVTEELDGGPLVVQ 155
Cdd:cd08644    68 VERLRALKPDLIFSFYYRHMISEDILEIARLGAFNLHGSLLPKYRGRAPLNWALINGETETGVTLHRMTKKPDAGAIVDQ 147

                          90       100
                  ....*....|....*....|....*
gi 1016362974 156 AVVPVESEDSAQTLAQRVHTQEHRI 180
Cdd:cd08644   148 EKVPILPDDTAKSLFHKLCVAARRL 172
FMT_core_like_4 cd08651
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 18-173 6.78e-10

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


Pssm-ID: 187720 [Multi-domain]  Cd Length: 180  Bit Score: 56.12  E-value: 6.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974  18 LQALIDSTRTgdspvrIAAVIS-------NRSDAYGLQR-ARDAGIdtrsldhKAFEGREAFDSALIELIDAFNPKLVVL 89
Cdd:cd08651    15 LEAILEAGGE------VVGVITlddsssnNDSDYLDLDSfARKNGI-------PYYKFTDINDEEIIEWIKEANPDIIFV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974  90 AGFMRILSADFVRHYNGRLLNIHPSLLPKYKGLHTHQRALEAGDTEHGCSVHFVTEELDGGPLVVQAVVPVESEDSAQTL 169
Cdd:cd08651    82 FGWSQLLKPEILAIPRLGVIGFHPTKLPKNRGRAPIPWAILLGLKETASTFFWMDEGADSGDILSQEPFPIDKDDTANSL 161


                  ....
gi 1016362974 170 AQRV 173
Cdd:cd08651   162 YDKI 165
FMT_core_like_6 cd08820
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 29-169 5.85e-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: 53.60  E-value: 5.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974  29 DSPVRIAAVISNRSDAYGLQ---RARDAGIDTRSLdhkafegreafdSALIELIDAFNPKLVVLAGFMRILSADFVRHYN 105
Cdd:cd08820    24 RGSFEIIAVLTNTSPADVWEgsePLYDIGSTERNL------------HKLLEILENKGVDILISVQYHWILPGSILEKAK 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1016362974 106 GRLLNIHPSLLPKYKGLHTHQRALEAGDTEHGCSVHFVTEELDGGPLVVQAVVPVESEDSAQTL 169
Cdd:cd08820    92 EIAFNLHNAPLPEYRGCNQFSHAILNGDDQFGTTIHWMAEGIDSGDIIFEKRFPIPSDCTVISL 155
PRK08125 PRK08125
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ...
 76-173 6.80e-09

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


Pssm-ID: 236156 [Multi-domain]  Cd Length: 660  Bit Score: 54.99  E-value: 6.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974  76 IELIDAFNPKLVVLAGFMRILSADFVRHYNGRLLNIHPSLLPKYKGLHTHQRALEAGDTEHGCSVHFVTEELDGGPLVVQ 155
Cdd:PRK08125   68 VERIRELAPDVIFSFYYRNLLSDEILQLAPAGAFNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQ 147

                          90
                  ....*....|....*...
gi 1016362974 156 AVVPVESEDSAQTLAQRV 173
Cdd:PRK08125  148 QRVAIAPDDTALTLHHKL 165
FMT_core_like_2 cd08822
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 112-201 9.85e-08

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


Pssm-ID: 187724 [Multi-domain]  Cd Length: 192  Bit Score: 50.15  E-value: 9.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974 112 HPSLLPKYKGLHTHQRALEAGDTEHGCSVHFVTEELDGGPLVVQAVVPVESEDSAQTLAQRVhtqehrIYPLAVRWFAEG 191
Cdd:cd08822    95 HPSLLPRHRGRDAVEWTIRMRDPITGGTVYHLDDGVDGGPIAAQDWCHVRPGDTAAELWRRA------LAPMGVKLLTQV 168

                          90
                  ....*....|
gi 1016362974 192 RLILGDHGAL 201
Cdd:cd08822   169 IDALLRGGNL 178
PRK06988 PRK06988
formyltransferase;
109-166 3.57e-07

formyltransferase;


Pssm-ID: 235902 [Multi-domain]  Cd Length: 312  Bit Score: 49.69  E-value: 3.57e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1016362974 109 LNIHPSLLPKYKGLHTHQRALEAGDTEHGCSVHFVTEELDGGPLVVQAVVPVESEDSA 166
Cdd:PRK06988  103 YNMHGSLLPKYRGRVPVNWAVLNGETETGATLHEMVAKPDAGAIVDQTAVPILPDDTA 160
FMT_core_FDH_N cd08647
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ...
 112-204 8.14e-07

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: 47.83  E-value: 8.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016362974 112 HPSLLPKYKGLHTHQRALEAGDTEHGCSVHFVTEELDGGPLVVQAVVPVESEDSAQTLAQRVhtqehrIYP-------LA 184
Cdd:cd08647   106 HPSILPRHRGASAINWTLIHGDKKAGFTIFWADDGLDTGPILLQKECDVLPNDTVDTLYNRF------LYPegikamvEA 179

                          90       100
                  ....*....|....*....|...
gi 1016362974 185 VRWFAEG---RLILGDHGALLDG 204
Cdd:cd08647   180 VRLIAEGkapRIPQPEEGATYEG 202
PRK07579 PRK07579
dTDP-4-amino-4,6-dideoxyglucose formyltransferase;
107-177 5.62e-05

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


Pssm-ID: 236058 [Multi-domain]  Cd Length: 245  Bit Score: 42.97  E-value: 5.62e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1016362974 107 RLLNIHPSLLPKYKGLHTHQRALeAGDTEHGCSVHFVTEELDGGPLVVQAVVPVESEDSAQTLAQRVHTQE 177
Cdd:PRK07579   87 RCINIHPGFNPYNRGWFPQVFSI-INGLKIGATIHEMDEQLDHGPIIAQREVEIESWDSSGSVYARVMDIE 156
 
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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