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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612269439  83 ALFLAAAGVKAHRVLDINDAAFISSLGHM--DGVISLRCYQKFSADYVRAFSRRgklLWNLHPGDLPRYRGVMTLFRAMM 160
Cdd:cd08369   40 QLSLELVGGKVYLDSNINTPELLELLKEFapDLIVSINFRQIIPPEILKLPPGG---AINIHPSLLPRYRGVNPLAWAII 116

                         90       100
                 ....*....|....*....|....
gi 612269439 161 NGDKDCAVTLHEMDEHWDAGPVLA 184
Cdd:cd08369  117 NGEKETGVTVHYMDEGIDTGDIIA 140

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612269439  83 ALFLAAAGVKAHRVLDINDAAFISSLGHM--DGVISLRCYQKFSADYVRAFSRRgklLWNLHPGDLPRYRGVMTLFRAMM 160
Cdd:cd08369   40 QLSLELVGGKVYLDSNINTPELLELLKEFapDLIVSINFRQIIPPEILKLPPGG---AINIHPSLLPRYRGVNPLAWAII 116

                         90       100
                 ....*....|....*....|....
gi 612269439 161 NGDKDCAVTLHEMDEHWDAGPVLA 184
Cdd:cd08369  117 NGEKETGVTVHYMDEGIDTGDIIA 140

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

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 612269439 139 WNLHPGDLPRYRGVMTLFRAMMNGDKDCAVTLHEMDEHWDAGPVLAR 185
Cdd:COG0223  104 INLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDTGDILLQ 150

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612269439  114 VISLRCYQKF-SADYVRAFsrRGKLLwNLHPGDLPRYRGVMTLFRAMMNGDKDCAVTLHEMDEHWDAGPVLARLPAELRH 192
Cdd:pfam00551  82 VIVLAGYMRIlPPEFLQAP--PGGIL-NIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILP 158

                  ...
gi 612269439  193 DLS 195
Cdd:pfam00551 159 DDT 161

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612269439  83 ALFLAAAGVKAHRVLDINDAAFISSLGHM--DGVISLRCYQKFSADYVRAFSRRgklLWNLHPGDLPRYRGVMTLFRAMM 160
Cdd:cd08369   40 QLSLELVGGKVYLDSNINTPELLELLKEFapDLIVSINFRQIIPPEILKLPPGG---AINIHPSLLPRYRGVNPLAWAII 116

                         90       100
                 ....*....|....*....|....
gi 612269439 161 NGDKDCAVTLHEMDEHWDAGPVLA 184
Cdd:cd08369  117 NGEKETGVTVHYMDEGIDTGDIIA 140

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]

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612269439  140 NLHPGDLPRYRGVMTLFRAMMNGDKDCAVTLHEMDEHWDAGPVLARLPAELRHDLSFLENMMLLGVQSGTFL 211
Cdd:TIGR00460 105 NVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVPKMDAGDILKQETFPIEEEDNSGTLSDKLSELGAQLL 176

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612269439 139 WNLHPGDLPRYRGVMTLFRAMMNGDKDCAVTLHEMDEHWDAGPVLARLPAELRHDLSFLENMMLLGVQSGTFLARQLMRA 218
Cdd:cd08646  104 INVHPSLLPKYRGAAPIQRAILNGDKETGVTIMKMDEGLDTGDILAQEEVPIDPDDTAGELLDKLAELGADLLLEVLDDI 183

                         90
                 ....*....|....
gi 612269439 219 ERSEaIAAEKQGDS 232
Cdd:cd08646  184 EAGK-LNPVPQDES 196

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612269439 121 QKFSADYVRAFSRR----GKLL-------WNLHPGDLPRYRGVMTLFRAMMNGDKDCAVTLHEMDEHWDAGPVLARLP-A 188
Cdd:cd08644   72 RALKPDLIFSFYYRhmisEDILeiarlgaFNLHGSLLPKYRGRAPLNWALINGETETGVTLHRMTKKPDAGAIVDQEKvP 151

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 612269439 189 ELRHDLSFlENMMLLGVQSGTFLARQLMRAERSEAIA-AEKQGDSRYWG 236
Cdd:cd08644  152 ILPDDTAK-SLFHKLCVAARRLLARTLPALKAGKARErPQDETQASYFG 199

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

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612269439 108 LGHMDGVISLRCYQKFSADYVRafsrrGKLLWNLHPGDLPRYRGVMTLFRAMMNGDKdCAVTLHEMDEHWDAGPVLAR 185
Cdd:PRK07579  63 VERYDLVLSFHCKQRFPAKLVN-----GVRCINIHPGFNPYNRGWFPQVFSIINGLK-IGATIHEMDEQLDHGPIIAQ 134

formyltransferase;

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 612269439 130 AFSRRGKLlwNLHPGDLPRYRGVMTLFRAMMNGDKDCAVTLHEMDEHWDAGPVLAR 185
Cdd:PRK06988  96 ALAPRGAY--NMHGSLLPKYRGRVPVNWAVLNGETETGATLHEMVAKPDAGAIVDQ 149

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612269439  78 AYQPPALFLAAAGVKAHRVLDINDAAFISSLghmdgvislrcyQKFSADY-------------VRAFSRRGKLlwNLHPG 144
Cdd:cd08651   41 DYLDLDSFARKNGIPYYKFTDINDEEIIEWI------------KEANPDIifvfgwsqllkpeILAIPRLGVI--GFHPT 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 612269439 145 DLPRYRGVMTLFRAMMNGDKDCAVTLHEMDEHWDAGPVLARLPAELRHD 193
Cdd:cd08651  107 KLPKNRGRAPIPWAILLGLKETASTFFWMDEGADSGDILSQEPFPIDKD 155

methionyl-tRNA formyltransferase

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 612269439 140 NLHPGDLPRYRGVMTLFRAMMNGDKDCAVTLHEMDEHWDAGPVLAR 185
Cdd:PLN02285 120 NIHPSLLPLYRGAAPVQRALQDGVNETGVSVAFTVRALDAGPVIAQ 165

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 612269439 142 HPGDLPRYRGVMTLFRAMMNGDKDCAVTLHEMDEHWDAGPVL 183
Cdd:cd08647  106 HPSILPRHRGASAINWTLIHGDKKAGFTIFWADDGLDTGPIL 147