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Conserved domains on  [gi|490247512|ref|WP_004145656|]
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MULTISPECIES: phosphoribosylglycinamide formyltransferase [Klebsiella]

Protein Classification

phosphoribosylglycinamide formyltransferase( domain architecture ID 10001018)

phosphoribosylglycinamide formyltransferase catalyzes the transfer of a formyl group from lO-formyltetrahydrofolate to glycinamide ribonucleotide

CATH:  3.40.50.170
EC:  2.1.2.2
Gene Symbol:  purN
Gene Ontology:  GO:0006974|GO:0004644|GO:0006189
SCOP:  4000065

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 1-202 8.91e-122

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: 343.17  E-value: 8.91e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512   1 MKNIVVLISGSGSNLQAIIDACGRKQINGTLRAVFSNKADAFGLERARLAGIPAHALAQSQFADREAFDRQLMHEIDAYA 80
Cdd:COG0299    1 MKRIAVLISGRGSNLQALIDAIEAGDLPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512  81 PDLVVLAGYMRILSPAFVSHYQGRLLNIHPSLLPKYPGLHTHRQVLENGDEEHGTSVHFVTDELDGGPVILQAKVPVFAG 160
Cdd:COG0299   81 PDLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPD 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 490247512 161 DSEEEITARVQAQEHAIYPLVISWFVDGRLRMAGNHAWLDER 202
Cdd:COG0299  161 DTEETLAARILEQEHRLYPEAIRLLAEGRLTLDGRRVRLDGE 202
 
Name Accession Description Interval E-value
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 1-202 8.91e-122

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: 343.17  E-value: 8.91e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512   1 MKNIVVLISGSGSNLQAIIDACGRKQINGTLRAVFSNKADAFGLERARLAGIPAHALAQSQFADREAFDRQLMHEIDAYA 80
Cdd:COG0299    1 MKRIAVLISGRGSNLQALIDAIEAGDLPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512  81 PDLVVLAGYMRILSPAFVSHYQGRLLNIHPSLLPKYPGLHTHRQVLENGDEEHGTSVHFVTDELDGGPVILQAKVPVFAG 160
Cdd:COG0299   81 PDLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPD 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 490247512 161 DSEEEITARVQAQEHAIYPLVISWFVDGRLRMAGNHAWLDER 202
Cdd:COG0299  161 DTEETLAARILEQEHRLYPEAIRLLAEGRLTLDGRRVRLDGE 202
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 3-185 6.13e-102

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: 292.37  E-value: 6.13e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512   3 NIVVLISGSGSNLQAIIDACGRKQINGTLRAVFSNKADAFGLERARLAGIPAHALAQSQFADREAFDRQLMHEIDAYAPD 82
Cdd:cd08645    1 RIAVLASGSGSNLQALIDAIKSGKLNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512  83 LVVLAGYMRILSPAFVSHYQGRLLNIHPSLLPKYPGLHTHRQVLENGDEEHGTSVHFVTDELDGGPVILQAKVPVFAGDS 162
Cdd:cd08645   81 LIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDT 160

                        170       180
                 ....*....|....*....|...
gi 490247512 163 EEEITARVQAQEHAIYPLVISWF 185
Cdd:cd08645  161 PETLAERIHALEHRLYPEAIKLL 183
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 2-191 9.15e-101

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: 289.66  E-value: 9.15e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512    2 KNIVVLISGSGSNLQAIIDACGRKQINGTLRAVFSNKADAFGLERARLAGIPAHALAQSQFADREAFDRQLMHEIDAYAP 81
Cdd:TIGR00639   1 KRIVVLISGNGSNLQAIIDACKEGKIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512   82 DLVVLAGYMRILSPAFVSHYQGRLLNIHPSLLPKYPGLHTHRQVLENGDEEHGTSVHFVTDELDGGPVILQAKVPVFAGD 161
Cdd:TIGR00639  81 DLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPED 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 490247512  162 SEEEITARVQAQEHAIYPLVISWFVDGRLR 191
Cdd:TIGR00639 161 TEETLEQRIHKQEHRIYPLAIAWFAQGRLK 190
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 2-182 1.30e-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: 238.35  E-value: 1.30e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512    2 KNIVVLISGSGSNLQAIIDACGRKQINGTLRAVFSNKADAFGLERARLAGIPAHALAQSQFADREAFDRQLMHEIDAYAP 81
Cdd:pfam00551   1 MKIAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512   82 DLVVLAGYMRILSPAFVSHYQGRLLNIHPSLLPKYPGLHTHRQVLENGDEEHGTSVHFVTDELDGGPVILQAKVPVFAGD 161
Cdd:pfam00551  81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160

                         170       180
                  ....*....|....*....|.
gi 490247512  162 SEEEITARVQAQEHAIYPLVI 182
Cdd:pfam00551 161 TAETLYNRVADLEHKALPRVL 181
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 3-191 3.53e-47

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 154.08  E-value: 3.53e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512   3 NIVVLISGSGSNLQAIIDACGRKQINGTLRAVFSNKADAFGLERARLAGIPAHALAQSQFADREAFDRQLMHEIDAYAPD 82
Cdd:PLN02331   1 KLAVFVSGGGSNFRAIHDACLDGRVNGDVVVVVTNKPGCGGAEYARENGIPVLVYPKTKGEPDGLSPDELVDALRGAGVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512  83 LVVLAGYMRILSPAFVSHYQGRLLNIHPSLLPK-----YPGLHTHRQVLENGDEEHGTSVHFVTDELDGGPVILQAKVPV 157
Cdd:PLN02331  81 FVLLAGYLKLIPVELVRAYPRSILNIHPALLPAfggkgYYGIKVHKAVIASGARYSGPTVHFVDEHYDTGRILAQRVVPV 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 490247512 158 FAGDSEEEITARVQAQEHAIYPLVISWFVDGRLR 191
Cdd:PLN02331 161 LATDTPEELAARVLHEEHQLYVEVVAALCEERIV 194
 
Name Accession Description Interval E-value
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 1-202 8.91e-122

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: 343.17  E-value: 8.91e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512   1 MKNIVVLISGSGSNLQAIIDACGRKQINGTLRAVFSNKADAFGLERARLAGIPAHALAQSQFADREAFDRQLMHEIDAYA 80
Cdd:COG0299    1 MKRIAVLISGRGSNLQALIDAIEAGDLPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512  81 PDLVVLAGYMRILSPAFVSHYQGRLLNIHPSLLPKYPGLHTHRQVLENGDEEHGTSVHFVTDELDGGPVILQAKVPVFAG 160
Cdd:COG0299   81 PDLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPD 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 490247512 161 DSEEEITARVQAQEHAIYPLVISWFVDGRLRMAGNHAWLDER 202
Cdd:COG0299  161 DTEETLAARILEQEHRLYPEAIRLLAEGRLTLDGRRVRLDGE 202
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 3-185 6.13e-102

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: 292.37  E-value: 6.13e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512   3 NIVVLISGSGSNLQAIIDACGRKQINGTLRAVFSNKADAFGLERARLAGIPAHALAQSQFADREAFDRQLMHEIDAYAPD 82
Cdd:cd08645    1 RIAVLASGSGSNLQALIDAIKSGKLNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512  83 LVVLAGYMRILSPAFVSHYQGRLLNIHPSLLPKYPGLHTHRQVLENGDEEHGTSVHFVTDELDGGPVILQAKVPVFAGDS 162
Cdd:cd08645   81 LIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDT 160

                        170       180
                 ....*....|....*....|...
gi 490247512 163 EEEITARVQAQEHAIYPLVISWF 185
Cdd:cd08645  161 PETLAERIHALEHRLYPEAIKLL 183
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 2-191 9.15e-101

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: 289.66  E-value: 9.15e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512    2 KNIVVLISGSGSNLQAIIDACGRKQINGTLRAVFSNKADAFGLERARLAGIPAHALAQSQFADREAFDRQLMHEIDAYAP 81
Cdd:TIGR00639   1 KRIVVLISGNGSNLQAIIDACKEGKIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512   82 DLVVLAGYMRILSPAFVSHYQGRLLNIHPSLLPKYPGLHTHRQVLENGDEEHGTSVHFVTDELDGGPVILQAKVPVFAGD 161
Cdd:TIGR00639  81 DLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPED 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 490247512  162 SEEEITARVQAQEHAIYPLVISWFVDGRLR 191
Cdd:TIGR00639 161 TEETLEQRIHKQEHRIYPLAIAWFAQGRLK 190
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 2-182 1.30e-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: 238.35  E-value: 1.30e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512    2 KNIVVLISGSGSNLQAIIDACGRKQINGTLRAVFSNKADAFGLERARLAGIPAHALAQSQFADREAFDRQLMHEIDAYAP 81
Cdd:pfam00551   1 MKIAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512   82 DLVVLAGYMRILSPAFVSHYQGRLLNIHPSLLPKYPGLHTHRQVLENGDEEHGTSVHFVTDELDGGPVILQAKVPVFAGD 161
Cdd:pfam00551  81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160

                         170       180
                  ....*....|....*....|.
gi 490247512  162 SEEEITARVQAQEHAIYPLVI 182
Cdd:pfam00551 161 TAETLYNRVADLEHKALPRVL 181
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 3-191 3.53e-47

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 154.08  E-value: 3.53e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512   3 NIVVLISGSGSNLQAIIDACGRKQINGTLRAVFSNKADAFGLERARLAGIPAHALAQSQFADREAFDRQLMHEIDAYAPD 82
Cdd:PLN02331   1 KLAVFVSGGGSNFRAIHDACLDGRVNGDVVVVVTNKPGCGGAEYARENGIPVLVYPKTKGEPDGLSPDELVDALRGAGVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512  83 LVVLAGYMRILSPAFVSHYQGRLLNIHPSLLPK-----YPGLHTHRQVLENGDEEHGTSVHFVTDELDGGPVILQAKVPV 157
Cdd:PLN02331  81 FVLLAGYLKLIPVELVRAYPRSILNIHPALLPAfggkgYYGIKVHKAVIASGARYSGPTVHFVDEHYDTGRILAQRVVPV 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 490247512 158 FAGDSEEEITARVQAQEHAIYPLVISWFVDGRLR 191
Cdd:PLN02331 161 LATDTPEELAARVLHEEHQLYVEVVAALCEERIV 194
FMT_core cd08369
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...
 6-185 1.38e-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: 125.86  E-value: 1.38e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512   6 VLISGSGSNLQAIIDACgRKQINGTLRAVFSNKADAFGLERARLAGIPAhalaqSQFADREAFDRQLMHEIDAYAPDLVV 85
Cdd:cd08369    1 IVILGSGNIGQRVLKAL-LSKEGHEIVGVVTHPDSPRGTAQLSLELVGG-----KVYLDSNINTPELLELLKEFAPDLIV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512  86 LAGYMRILSPAFVSHYQGRLLNIHPSLLPKYPGLHTHRQVLENGDEEHGTSVHFVTDELDGGPVILQAKVPVFAGDSEEE 165
Cdd:cd08369   75 SINFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTAGT 154

                        170       180
                 ....*....|....*....|
gi 490247512 166 ITARvqaQEHAIYPLVISWF 185
Cdd:cd08369  155 LYQR---LIELGPKLLKEAL 171
PurU COG0788
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ...
 2-195 1.36e-30

Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate hydrolase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440551 [Multi-domain]  Cd Length: 282  Bit Score: 113.61  E-value: 1.36e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512   2 KNIVVLISGSGSNLQAIIDACGRKQINGTLRAVFSNKADAFGLerARLAGIPAHALAQSQfADREAFDRQLMHEIDAYAP 81
Cdd:COG0788   87 KRVAILVSKEDHCLNDLLYRWRSGELPAEIPAVISNHPDLRPL--AEWFGIPFHHIPVTK-ETKAEAEARLLELLEEYDI 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512  82 DLVVLAGYMRILSPAFVSHYQGRLLNIHPSLLPKYPGLHTHRQVLENGDEEHGTSVHFVTDELDGGPVILQAKVPVFAGD 161
Cdd:COG0788  164 DLVVLARYMQILSPDFCARLPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVERVDHRD 243

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 490247512 162 SEEEITARVQAQEhaiyPLVIS----WFVDGRLRMAGN 195
Cdd:COG0788  244 TPEDLVRKGRDVE----KRVLAravrWHLEDRVLVNGN 277
PurU TIGR00655
formyltetrahydrofolate deformylase; This model describes formyltetrahydrofolate deformylases. ...
 2-166 7.96e-28

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: 106.36  E-value: 7.96e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512    2 KNIVVLISGSGSNLQAIIDACGRKQINGTLRAVFSNKADAFGLerARLAGIPAHALAQSQFADREAFDRQLmHEIDAYAP 81
Cdd:TIGR00655  85 KRVAILVSKEDHCLGDLLWRWYSGELDAEIALVISNHEDLRSL--VERFGIPFHYIPATKDNRVEHEKRQL-ELLKQYQV 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512   82 DLVVLAGYMRILSPAFVSHYQGRLLNIHPSLLPKYPGLHTHRQVLENGDEEHGTSVHFVTDELDGGPVILQAKVPVFAGD 161
Cdd:TIGR00655 162 DLVVLAKYMQILSPDFVKRYPNKIINIHHSFLPAFIGANPYQRAYERGVKIIGATAHYVTEELDEGPIIEQDVVRVDHTD 241


                  ....*
gi 490247512  162 SEEEI 166
Cdd:TIGR00655 242 NVEDL 246
FMT_core_Formyl-FH4-Hydrolase_C cd08648
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ...
 33-195 3.31e-27

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: 102.26  E-value: 3.31e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512  33 AVFSNKADAFGLerARLAGIPAHALAQSQfADREAFDRQLMHEIDAYAPDLVVLAGYMRILSPAFVSHYQGRLLNIHPSL 112
Cdd:cd08648   32 LVISNHPDLRPL--AERFGIPFHHIPVTK-DTKAEAEAEQLELLEEYGVDLVVLARYMQILSPDFVERYPNRIINIHHSF 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512 113 LPKYPGLHTHRQVLENGDEEHGTSVHFVTDELDGGPVILQAKVPVFAGDSEEEITARVQAQEHAIYPLVISWFVDGRLRM 192
Cdd:cd08648  109 LPAFKGAKPYHQAFERGVKLIGATAHYVTEELDEGPIIEQDVERVSHRDSVEDLVRKGRDIEKQVLARAVKWHLEDRVLV 188


                 ...
gi 490247512 193 AGN 195
Cdd:cd08648  189 YGN 191
purU PRK06027
formyltetrahydrofolate deformylase; Reviewed
 2-157 6.85e-25

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 235676 [Multi-domain]  Cd Length: 286  Bit Score: 98.64  E-value: 6.85e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512   2 KNIVVLISGSGSNLQAIIDACGRKQINGTLRAVFSNKADAFGLerARLAGIPAHALAQSQFADREAFDRQLmHEIDAYAP 81
Cdd:PRK06027  90 KRVVILVSKEDHCLGDLLWRWRSGELPVEIAAVISNHDDLRSL--VERFGIPFHHVPVTKETKAEAEARLL-ELIDEYQP 166

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490247512  82 DLVVLAGYMRILSPAFVSHYQGRLLNIHPSLLPKYPGLHTHRQVLENGDEEHGTSVHFVTDELDGGPVILQAKVPV 157
Cdd:PRK06027 167 DLVVLARYMQILSPDFVARFPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVIRV 242
PRK13011 PRK13011
formyltetrahydrofolate deformylase; Reviewed
 32-195 1.33e-21

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 237266 [Multi-domain]  Cd Length: 286  Bit Score: 89.66  E-value: 1.33e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512  32 RAVFSNKADAFGLerARLAGIPAHALAQSQfADREAFDRQLMHEIDAYAPDLVVLAGYMRILSPAFVSHYQGRLLNIHPS 111
Cdd:PRK13011 120 VGVVSNHPDLEPL--AAWHGIPFHHFPITP-DTKPQQEAQVLDVVEESGAELVVLARYMQVLSPELCRKLAGRAINIHHS 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512 112 LLPKYPGLHTHRQVLENGDEEHGTSVHFVTDELDGGPVILQAKVPVFAGDSEEEITARVQAQEHAIYPLVISWFVDGRLR 191
Cdd:PRK13011 197 FLPGFKGAKPYHQAYERGVKLIGATAHYVTDDLDEGPIIEQDVERVDHAYSPEDLVAKGRDVECLTLARAVKAHIERRVF 276


                 ....
gi 490247512 192 MAGN 195
Cdd:PRK13011 277 LNGN 280
FMT_core_like_3 cd08653
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 76-170 5.81e-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: 5.81e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512  76 IDAYAPDLVVLAGyMRILSPAFVSHYQGRLLNIHPSLLPKYPGLHTHRQVLENGDEEH-GTSVHFVTDELDGGPVILQAK 154
Cdd:cd08653   43 LRALAPDVVSVYG-CGIIKDALLAIPPLGVLNLHGGILPDYRGVHTGFWALANGDPDNvGVTVHLVDAGIDTGDVLAQAR 121

                         90
                 ....*....|....*.
gi 490247512 155 VPVFAGDSEEEITARV 170
Cdd:cd08653  122 PPLAAGDTLLSLYLRL 137
purU PRK13010
formyltetrahydrofolate deformylase; Reviewed
 33-195 1.70e-19

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 139334 [Multi-domain]  Cd Length: 289  Bit Score: 84.08  E-value: 1.70e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512  33 AVFSNKADAfgLERARLAGIPAHAL--AQSQFADREAfdrQLMHEIDAYAPDLVVLAGYMRILSPAFVSHYQGRLLNIHP 110
Cdd:PRK13010 125 GIISNHPDL--QPLAVQHDIPFHHLpvTPDTKAQQEA---QILDLIETSGAELVVLARYMQVLSDDLSRKLSGRAINIHH 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512 111 SLLPKYPGLHTHRQVLENGDEEHGTSVHFVTDELDGGPVILQAKVPVFAGDSEEEITARVQAQEHAIYPLVISWFVDGRL 190
Cdd:PRK13010 200 SFLPGFKGARPYHQAHARGVKLIGATAHFVTDDLDEGPIIEQDVERVDHSYSPEDLVAKGRDVECLTLARAVKAFIEHRV 279


                 ....*
gi 490247512 191 RMAGN 195
Cdd:PRK13010 280 FINGD 284
PLN02828 PLN02828
formyltetrahydrofolate deformylase
 44-152 1.16e-18

formyltetrahydrofolate deformylase


Pssm-ID: 178422  Cd Length: 268  Bit Score: 81.72  E-value: 1.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512  44 LERArlaGIPAHALAQSQFADREAFDRQLMHEIDayapdLVVLAGYMRILSPAFVSHYQGRLLNIHPSLLPKYPGLHTHR 123
Cdd:PLN02828 119 LERH---GIPYHYLPTTKENKREDEILELVKGTD-----FLVLARYMQILSGNFLKGYGKDIINIHHGLLPSFKGGNPSK 190

                         90       100
                 ....*....|....*....|....*....
gi 490247512 124 QVLENGDEEHGTSVHFVTDELDGGPVILQ 152
Cdd:PLN02828 191 QAFDAGVKLIGATSHFVTEELDAGPIIEQ 219
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
75-170 3.86e-17

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


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 77.84  E-value: 3.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512  75 EIDAYAPDLVVLAGYMRILSPAFVSHYQGRLLNIHPSLLPKYPGL-HTHRQVLeNGDEEHGTSVHFVTDELDGGPVILQA 153
Cdd:COG0223   73 ELRALNPDLIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAaPIQWAIL-NGDTETGVTIMQMDEGLDTGDILLQE 151

                         90
                 ....*....|....*..
gi 490247512 154 KVPVFAGDSEEEITARV 170
Cdd:COG0223  152 EVPIGPDDTAGSLHDKL 168
PLN02285 PLN02285
methionyl-tRNA formyltransferase
 45-157 3.10e-16

methionyl-tRNA formyltransferase


Pssm-ID: 215159 [Multi-domain]  Cd Length: 334  Bit Score: 75.89  E-value: 3.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512  45 ERARLAGIPAHALAQSQFADREAFdrqlMHEIDAYAPDLVVLAGYMRILSPAFVSHYQGRLLNIHPSLLPKYPGLHTHRQ 124
Cdd:PLN02285  62 QLALDRGFPPDLIFTPEKAGEEDF----LSALRELQPDLCITAAYGNILPQKFLDIPKLGTVNIHPSLLPLYRGAAPVQR 137

                         90       100       110
                 ....*....|....*....|....*....|...
gi 490247512 125 VLENGDEEHGTSVHFVTDELDGGPVILQAKVPV 157
Cdd:PLN02285 138 ALQDGVNETGVSVAFTVRALDAGPVIAQERVEV 170
FMT_core_Met-tRNA-FMT_N cd08646
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ...
 45-169 1.19e-15

Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA formyltransferase (Met-tRNA-FMT), N-terminal formyltransferase domain. Met-tRNA-FMT transfers a formyl group from N-10 formyltetrahydrofolate to the amino terminal end of a methionyl-aminoacyl-tRNA acyl moiety, yielding formyl-Met-tRNA. Formyl-Met-tRNA plays essential role in protein translation initiation by forming complex with IF2. The formyl group plays a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and by impairing its binding to EFTU-GTP. The N-terminal domain contains a Rossmann fold and it is the catalytic domain of the enzyme.


Pssm-ID: 187715 [Multi-domain]  Cd Length: 204  Bit Score: 72.09  E-value: 1.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512  45 ERARLAGIPAHalaQSQFADREAFDRQLMheidAYAPDLVVLAGYMRILSPAFVSHYQGRLLNIHPSLLPKYPG---LHt 121
Cdd:cd08646   50 ELALELGLPVL---QPEKLKDEEFLEELK----ALKPDLIVVVAYGQILPKEILDLPPYGCINVHPSLLPKYRGaapIQ- 121

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 490247512 122 hrQVLENGDEEHGTSVHFVTDELDGGPVILQAKVPVFAGDSEEEITAR 169
Cdd:cd08646  122 --RAILNGDKETGVTIMKMDEGLDTGDILAQEEVPIDPDDTAGELLDK 167
FMT_core_like_5 cd08823
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 48-170 7.07e-13

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


Pssm-ID: 187725 [Multi-domain]  Cd Length: 177  Bit Score: 64.00  E-value: 7.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512  48 RLAGIPAHALAQSQFADREAF---------DR-----------QLMHEIDAyapDLVVLAGYMRILSPAFVSHYQGRLLN 107
Cdd:cd08823   22 RLAGIAVPAHNASYFPQIFVFtgirrlvskQRvdtanlkeqlaEWLRALAA---DTVVVFTFPYRIPQHILDLPPLGFYN 98

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490247512 108 IHPSLLPKYPGLHTHRQVLENGDEEHGTSVHFVTDELDGGPVILQAKVPVFAGDSEEEITARV 170
Cdd:cd08823   99 LHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMTAEIDRGPIVLEQFTPIHPDDTYGLLCSRL 161
fmt TIGR00460
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ...
 81-172 1.92e-11

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: 62.03  E-value: 1.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512   81 PDLVVLAGYMRILSPAFVSHYQGRLLNIHPSLLPKYPGLH-THRQVLeNGDEEHGTSVHFVTDELDGGPVILQAKVPVFA 159
Cdd:TIGR00460  79 PDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGApIQRAIL-NGDKKTGVTIMQMVPKMDAGDILKQETFPIEE 157

                          90
                  ....*....|...
gi 490247512  160 GDSEEEITARVQA 172
Cdd:TIGR00460 158 EDNSGTLSDKLSE 170
FMT_core_ArnA_N cd08644
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ...
 45-170 4.60e-08

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: 51.19  E-value: 4.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512  45 ERARLAGIPAhalaqsqFADREAFDRQLMHEIDAYAPDLVVLAGYMRILSPAFVSHYQGRLLNIHPSLLPKYPGLHTHRQ 124
Cdd:cd08644   47 QLAREHGIPV-------FTPDDINHPEWVERLRALKPDLIFSFYYRHMISEDILEIARLGAFNLHGSLLPKYRGRAPLNW 119

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 490247512 125 VLENGDEEHGTSVHFVTDELDGGPVILQAKVPVFAGDSEEEITARV 170
Cdd:cd08644  120 ALINGETETGVTLHRMTKKPDAGAIVDQEKVPILPDDTAKSLFHKL 165
PRK08125 PRK08125
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ...
 15-161 3.27e-07

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


Pssm-ID: 236156 [Multi-domain]  Cd Length: 660  Bit Score: 49.98  E-value: 3.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512  15 LQAIIDAcgrkqinG-TLRAVFSNKADA-----FGlERARLA---GIPAHA---LAQSQFADReafdrqlmheIDAYAPD 82
Cdd:PRK08125  16 IEALLAA-------GyEIAAVFTHTDNPgenhfFG-SVARLAaelGIPVYApedVNHPLWVER----------IRELAPD 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490247512  83 LVVLAGYMRILSPAFVSHYQGRLLNIHPSLLPKYPGLHTHRQVLENGDEEHGTSVHFVTDELDGGPVILQAKVPVFAGD 161
Cdd:PRK08125  78 VIFSFYYRNLLSDEILQLAPAGAFNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQQRVAIAPDD 156
FMT_core_NRPS_like cd08649
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ...
 91-161 1.63e-06

N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins involved in the synthesis of Oxazolomycin; This family represents the N-terminal formyl transferase catalytic core domain present in a subgroup of non-ribosomal peptide synthetases. In Streptomyces albus a member of this family has been shown to be involved in the synthesis of oxazolomycin (OZM). OZM is a hybrid peptide-polyketide antibiotic and exhibits potent antitumor and antiviral activities. It is a multi-domain protein consisting of a formyl transferase domain, a Flavin-utilizing monoxygenase domain, a LuxE domain functioning as an acyl protein synthetase and a pp-binding domain, which may function as an acyl carrier. It shows sequence similarity with other peptide-polyketide biosynthesis proteins.


Pssm-ID: 187718 [Multi-domain]  Cd Length: 166  Bit Score: 46.48  E-value: 1.63e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490247512  91 RILSPAFVSHYQGRLLNIHPSLLPKYPGLHTHRQVLENGDEEHGTSVHFVTDELDGGPVILQAKVPVFAGD 161
Cdd:cd08649   72 RILPSEVLALPRKGAINFHDGPLPRYAGLNATSWALLAGETRHGVTWHRIEEGVDAGDILVQRPFDIAPDD 142
FMT_core_like_6 cd08820
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 24-157 3.07e-06

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: 45.89  E-value: 3.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512  24 RKQINGT--LRAVFSNKADAFGLErarlaGIPAHALAQSqfadreafDRQLMHEIDAYAP----DLVVLAGYMRILSPAF 97
Cdd:cd08820   20 RLQDRGSfeIIAVLTNTSPADVWE-----GSEPLYDIGS--------TERNLHKLLEILEnkgvDILISVQYHWILPGSI 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512  98 VSHYQGRLLNIHPSLLPKYPGLHTHRQVLENGDEEHGTSVHFVTDELDGGPVILQAKVPV 157
Cdd:cd08820   87 LEKAKEIAFNLHNAPLPEYRGCNQFSHAILNGDDQFGTTIHWMAEGIDSGDIIFEKRFPI 146
FMT_core_FDH_N cd08647
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ...
 109-169 4.11e-06

10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family represents the N-terminal hydrolase domain of the bifunctional protein 10-formyltetrahydrofolate dehydrogenase (FDH). This domain contains a 10-formyl-tetrahydrofolate (10-formyl-THF) binding site and shares sequence homology and structural topology with other enzymes utilizing this substrate. This domain functions as a hydrolase, catalyzing the conversion of 10-formyl-THF, a precursor for nucleotide biosynthesis, to tetrahydrofolate (THF). The overall FDH reaction mechanism is a coupling of two sequential reactions, a hydrolase and a formyl dehydrogenase, bridged by a substrate transfer step. The N-terminal hydrolase domain removes the formyl group from 10-formyl-THF and the C-terminal NADP-dependent dehydrogenase domain then reduces the formyl group to carbon dioxide. The two catalytic domains are connected by a third intermediate linker domain that transfers the formyl group, covalently attached to the sulfhydryl group of the phosphopantetheine arm, from the N-terminal domain to the C-terminal domain.


Pssm-ID: 187716 [Multi-domain]  Cd Length: 203  Bit Score: 45.90  E-value: 4.11e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490247512 109 HPSLLPKYPGLHTHRQVLENGDEEHGTSVHFVTDELDGGPVILQAKVPVFAGDSEEEITAR 169
Cdd:cd08647  106 HPSILPRHRGASAINWTLIHGDKKAGFTIFWADDGLDTGPILLQKECDVLPNDTVDTLYNR 166
FMT_core_like_2 cd08822
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 6-188 4.24e-06

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: 45.53  E-value: 4.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512   6 VLISGSGSNLQAIIDACGRKQIngTLRAVfSNKADAFGLERARL-AGIPAHALAQSQFADREAfdrqlmheiDAYAPDLV 84
Cdd:cd08822    3 IAIAGQKWFGTAVLEALRARGI--ALLGV-AAPEEGDRLAAAARtAGSRGLPRAGVAVLPADA---------IPPGTDLI 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512  85 VLAGYMRILSPAFVSHYQGRLLNIHPSLLPKYPGLHTHRQVLENGDEEHGTSVHFVTDELDGGPVILQAKVPVFAGDSEE 164
Cdd:cd08822   71 VAAHCHAFISAKTRARARLGAIGYHPSLLPRHRGRDAVEWTIRMRDPITGGTVYHLDDGVDGGPIAAQDWCHVRPGDTAA 150

                        170       180       190
                 ....*....|....*....|....*....|.
gi 490247512 165 EITARvqaqehAIYPL-------VISWFVDG 188
Cdd:cd08822  151 ELWRR------ALAPMgvklltqVIDALLRG 175
PRK07579 PRK07579
dTDP-4-amino-4,6-dideoxyglucose formyltransferase;
104-189 8.72e-06

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


Pssm-ID: 236058 [Multi-domain]  Cd Length: 245  Bit Score: 45.28  E-value: 8.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512 104 RLLNIHPSLLPKYPGLHTHRQVLENgDEEHGTSVHFVTDELDGGPVILQAKVPVFAGDSEEEITARVQAQEHAIYPLVIS 183
Cdd:PRK07579  87 RCINIHPGFNPYNRGWFPQVFSIIN-GLKIGATIHEMDEQLDHGPIIAQREVEIESWDSSGSVYARVMDIERELVLEHFD 165


                 ....*.
gi 490247512 184 WFVDGR 189
Cdd:PRK07579 166 AIRDGS 171
PRK06988 PRK06988
formyltransferase;
76-170 8.88e-06

formyltransferase;


Pssm-ID: 235902 [Multi-domain]  Cd Length: 312  Bit Score: 45.45  E-value: 8.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512  76 IDAYAPDLVVLAGYMRILSPAFVSHYQGRLLNIHPSLLPKYPG-LHTHRQVLeNGDEEHGTSVHFVTDELDGGPVILQAK 154
Cdd:PRK06988  73 VAAAAPDFIFSFYYRHMIPVDLLALAPRGAYNMHGSLLPKYRGrVPVNWAVL-NGETETGATLHEMVAKPDAGAIVDQTA 151

                         90
                 ....*....|....*.
gi 490247512 155 VPVFAGDSEEEITARV 170
Cdd:PRK06988 152 VPILPDDTAAQVFDKV 167
FMT_core_like_4 cd08651
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 15-177 2.16e-05

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


Pssm-ID: 187720 [Multi-domain]  Cd Length: 180  Bit Score: 43.41  E-value: 2.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512  15 LQAIIDAcgrkqiNGTLRAVFSNKADAFG--------LERARLAGIPAHALAQSQFADREAFdrqlmheIDAYAPDLVVL 86
Cdd:cd08651   15 LEAILEA------GGEVVGVITLDDSSSNndsdyldlDSFARKNGIPYYKFTDINDEEIIEW-------IKEANPDIIFV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247512  87 AGYMRILSPAFVSHYQGRLLNIHPSLLPKYPGLHTHRQVLENGDEEHGTSVHFVTDELDGGPVILQAKVPVfagdsEEEI 166
Cdd:cd08651   82 FGWSQLLKPEILAIPRLGVIGFHPTKLPKNRGRAPIPWAILLGLKETASTFFWMDEGADSGDILSQEPFPI-----DKDD 156

                        170
                 ....*....|.
gi 490247512 167 TARVQAQEHAI 177
Cdd:cd08651  157 TANSLYDKIME 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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