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Conserved domains on  [gi|2751846656|ref|WP_353477328|]
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formyltransferase family protein [Campylobacter jejuni]

Protein Classification

FMT_core domain-containing protein( domain architecture ID 10170233)

FMT_core domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FMT_core cd08369
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...
 2-116 1.76e-50

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: 157.84  E-value: 1.76e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751846656   2 NSKEFLNELKKYSNDLLVSMSFDQIFKEELLKLYPRKIINCHAGKLPFYRGRNILNWALINDEKEFGISVHFIDKGIDTG 81
Cdd:cd08369    57 NTPELLELLKEFAPDLIVSINFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTG 136

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2751846656  82 DIILQKTYEIKDSDDYTTLLNLCHKECANLLYESL 116
Cdd:cd08369   137 DIIAQEVIPISPDDTAGTLYQRLIELGPKLLKEAL 171
 
Name Accession Description Interval E-value
FMT_core cd08369
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...
 2-116 1.76e-50

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: 157.84  E-value: 1.76e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751846656   2 NSKEFLNELKKYSNDLLVSMSFDQIFKEELLKLYPRKIINCHAGKLPFYRGRNILNWALINDEKEFGISVHFIDKGIDTG 81
Cdd:cd08369    57 NTPELLELLKEFAPDLIVSINFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTG 136

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2751846656  82 DIILQKTYEIKDSDDYTTLLNLCHKECANLLYESL 116
Cdd:cd08369   137 DIIAQEVIPISPDDTAGTLYQRLIELGPKLLKEAL 171
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
1-126 5.16e-35

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


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 122.14  E-value: 5.16e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751846656   1 MNSKEFLNELKKYSNDLLVSMSFDQIFKEELLKLYPRKIINCHAGKLPFYRGRNILNWALINDEKEFGISVHFIDKGIDT 80
Cdd:COG0223    65 LKDPEFLEELRALNPDLIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDT 144

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2751846656  81 GDIILQKTYEIKDSDDYTTLLNLCHKECANLLYESLILFLEDNVKA 126
Cdd:COG0223   145 GDILLQEEVPIGPDDTAGSLHDKLAELGAELLLETLDALEAGTLTP 190
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 5-116 1.45e-21

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: 84.65  E-value: 1.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751846656   5 EFLNELKKYSNDLLVSMSFDQIFKEELLKLYPRKIINCHAGKLPFYRGRNILNWALINDEKEFGISVHFIDKGIDTGDII 84
Cdd:pfam00551  70 ELADALRALAADVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPIL 149

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2751846656  85 LQKTYEIKDSDDYTTLLNLCHKECANLLYESL 116
Cdd:pfam00551 150 AQKAVPILPDDTAETLYNRVADLEHKALPRVL 181
fmt TIGR00460
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ...
 5-125 1.03e-20

methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than methionyl-tRNA formyltransferase (fmt) itself are formyltetrahydrofolate dehydrogenases. The mitochondrial methionyl-tRNA formyltransferases are so divergent that, in a multiple alignment of bacterial fmt, mitochondrial fmt, and formyltetrahydrofolate dehydrogenases, the mitochondrial fmt appears the most different. However, because both bacterial and mitochondrial fmt are included in the seed alignment, all credible fmt sequences score higher than any non-fmt sequence. This enzyme modifies Met on initiator tRNA to f-Met. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273088 [Multi-domain]  Cd Length: 313  Bit Score: 84.76  E-value: 1.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751846656   5 EFLNELKKYSNDLLVSMSFDQIFKEELLKLYPRKIINCHAGKLPFYRGRNILNWALINDEKEFGISVHFIDKGIDTGDII 84
Cdd:TIGR00460  69 EELPLVRELKPDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVPKMDAGDIL 148

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2751846656  85 LQKTYEIKDSDDYTTLLNLCHKECANLLYESLILFLEDNVK 125
Cdd:TIGR00460 149 KQETFPIEEEDNSGTLSDKLSELGAQLLIETLKELPEGKNK 189
PRK08125 PRK08125
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ...
 10-116 1.00e-18

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


Pssm-ID: 236156 [Multi-domain]  Cd Length: 660  Bit Score: 80.41  E-value: 1.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751846656  10 LKKYSNDLLVSMSFDQIFKEELLKLYPRKIINCHAGKLPFYRGRNILNWALINDEKEFGISVHFIDKGIDTGDIILQKTY 89
Cdd:PRK08125   71 IRELAPDVIFSFYYRNLLSDEILQLAPAGAFNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQQRV 150

                          90       100       110
                  ....*....|....*....|....*....|
gi 2751846656  90 EIKDSDdytTLLNLCHKEC---ANLLYESL 116
Cdd:PRK08125  151 AIAPDD---TALTLHHKLChaaRQLLEQTL 177
 
Name Accession Description Interval E-value
FMT_core cd08369
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...
 2-116 1.76e-50

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: 157.84  E-value: 1.76e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751846656   2 NSKEFLNELKKYSNDLLVSMSFDQIFKEELLKLYPRKIINCHAGKLPFYRGRNILNWALINDEKEFGISVHFIDKGIDTG 81
Cdd:cd08369    57 NTPELLELLKEFAPDLIVSINFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTG 136

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2751846656  82 DIILQKTYEIKDSDDYTTLLNLCHKECANLLYESL 116
Cdd:cd08369   137 DIIAQEVIPISPDDTAGTLYQRLIELGPKLLKEAL 171
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
1-126 5.16e-35

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


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 122.14  E-value: 5.16e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751846656   1 MNSKEFLNELKKYSNDLLVSMSFDQIFKEELLKLYPRKIINCHAGKLPFYRGRNILNWALINDEKEFGISVHFIDKGIDT 80
Cdd:COG0223    65 LKDPEFLEELRALNPDLIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDT 144

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2751846656  81 GDIILQKTYEIKDSDDYTTLLNLCHKECANLLYESLILFLEDNVKA 126
Cdd:COG0223   145 GDILLQEEVPIGPDDTAGSLHDKLAELGAELLLETLDALEAGTLTP 190
FMT_core_Met-tRNA-FMT_N cd08646
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ...
 1-126 1.34e-31

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: 111.00  E-value: 1.34e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751846656   1 MNSKEFLNELKKYSNDLLVSMSFDQIFKEELLKLYPRKIINCHAGKLPFYRGRNILNWALINDEKEFGISVHFIDKGIDT 80
Cdd:cd08646    65 LKDEEFLEELKALKPDLIVVVAYGQILPKEILDLPPYGCINVHPSLLPKYRGAAPIQRAILNGDKETGVTIMKMDEGLDT 144

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2751846656  81 GDIILQKTYEIKDSDDYTTLLNLCHKECANLLYESLILFLEDNVKA 126
Cdd:cd08646   145 GDILAQEEVPIDPDDTAGELLDKLAELGADLLLEVLDDIEAGKLNP 190
FMT_core_like_3 cd08653
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 2-111 6.09e-26

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: 94.97  E-value: 6.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751846656   2 NSKEFLNELKKYSNDLLVSMsFDQIFKEELLKLYPRKIINCHAGKLPFYRGRNILNWALINDE-KEFGISVHFIDKGIDT 80
Cdd:cd08653    35 NGPEVVAALRALAPDVVSVY-GCGIIKDALLAIPPLGVLNLHGGILPDYRGVHTGFWALANGDpDNVGVTVHLVDAGIDT 113

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2751846656  81 GDIILQKTYEIKDSDDYTTL-LNLCHKECANL 111
Cdd:cd08653   114 GDVLAQARPPLAAGDTLLSLyLRLYRAGVELM 145
FMT_core_like_4 cd08651
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 2-100 4.88e-24

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: 90.79  E-value: 4.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751846656   2 NSKEFLNELKKYSNDLLVSMSFDQIFKEELLKLYPRKIINCHAGKLPFYRGRNILNWALINDEKEFGISVHFIDKGIDTG 81
Cdd:cd08651    63 NDEEIIEWIKEANPDIIFVFGWSQLLKPEILAIPRLGVIGFHPTKLPKNRGRAPIPWAILLGLKETASTFFWMDEGADSG 142

                          90
                  ....*....|....*....
gi 2751846656  82 DIILQKTYEIKDSDDYTTL 100
Cdd:cd08651   143 DILSQEPFPIDKDDTANSL 161
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 5-116 1.45e-21

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: 84.65  E-value: 1.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751846656   5 EFLNELKKYSNDLLVSMSFDQIFKEELLKLYPRKIINCHAGKLPFYRGRNILNWALINDEKEFGISVHFIDKGIDTGDII 84
Cdd:pfam00551  70 ELADALRALAADVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPIL 149

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2751846656  85 LQKTYEIKDSDDYTTLLNLCHKECANLLYESL 116
Cdd:pfam00551 150 AQKAVPILPDDTAETLYNRVADLEHKALPRVL 181
FMT_core_ArnA_N cd08644
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ...
 2-105 2.04e-21

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: 84.70  E-value: 2.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751846656   2 NSKEFLNELKKYSNDLLVSMSFDQIFKEELLKLYPRKIINCHAGKLPFYRGRNILNWALINDEKEFGISVHFIDKGIDTG 81
Cdd:cd08644    63 NHPEWVERLRALKPDLIFSFYYRHMISEDILEIARLGAFNLHGSLLPKYRGRAPLNWALINGETETGVTLHRMTKKPDAG 142

                          90       100
                  ....*....|....*....|....*
gi 2751846656  82 DIILQKTYEIKDSDDYTTLLN-LCH 105
Cdd:cd08644   143 AIVDQEKVPILPDDTAKSLFHkLCV 167
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 4-100 1.01e-20

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: 82.44  E-value: 1.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751846656   4 KEFLNELKKYSNDLLVSMSFDQIFKEELLKLYPRKIINCHAGKLPFYRGRNILNWALINDEKEFGISVHFIDKGIDTGDI 83
Cdd:cd08645    68 EALLELLKEYKVDLIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPI 147

                          90
                  ....*....|....*..
gi 2751846656  84 ILQKTYEIKDSDDYTTL 100
Cdd:cd08645   148 IAQAAVPVLPGDTPETL 164
fmt TIGR00460
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ...
 5-125 1.03e-20

methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than methionyl-tRNA formyltransferase (fmt) itself are formyltetrahydrofolate dehydrogenases. The mitochondrial methionyl-tRNA formyltransferases are so divergent that, in a multiple alignment of bacterial fmt, mitochondrial fmt, and formyltetrahydrofolate dehydrogenases, the mitochondrial fmt appears the most different. However, because both bacterial and mitochondrial fmt are included in the seed alignment, all credible fmt sequences score higher than any non-fmt sequence. This enzyme modifies Met on initiator tRNA to f-Met. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273088 [Multi-domain]  Cd Length: 313  Bit Score: 84.76  E-value: 1.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751846656   5 EFLNELKKYSNDLLVSMSFDQIFKEELLKLYPRKIINCHAGKLPFYRGRNILNWALINDEKEFGISVHFIDKGIDTGDII 84
Cdd:TIGR00460  69 EELPLVRELKPDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVPKMDAGDIL 148

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2751846656  85 LQKTYEIKDSDDYTTLLNLCHKECANLLYESLILFLEDNVK 125
Cdd:TIGR00460 149 KQETFPIEEEDNSGTLSDKLSELGAQLLIETLKELPEGKNK 189
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 4-125 1.24e-19

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: 80.08  E-value: 1.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751846656   4 KEFLNELKKYSNDLLVSMSFDQIFKEELLKLYPRKIINCHAGKLPFYRGRNILNWALINDEKEFGISVHFIDKGIDTGDI 83
Cdd:COG0299    70 AALLEALDAYGPDLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPI 149

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2751846656  84 ILQKTYEIKDSDDYTTL----LNLCHKecanLLYESLILFLEDNVK 125
Cdd:COG0299   150 IAQAAVPVLPDDTEETLaariLEQEHR----LYPEAIRLLAEGRLT 191
FMT_core_like_6 cd08820
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 2-116 1.39e-19

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: 79.02  E-value: 1.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751846656   2 NSKEFLNELKKYSNDLLVSMSFDQIFKEELLKLYPRKIINCHAGKLPFYRGRNILNWALINDEKEFGISVHFIDKGIDTG 81
Cdd:cd08820    57 NLHKLLEILENKGVDILISVQYHWILPGSILEKAKEIAFNLHNAPLPEYRGCNQFSHAILNGDDQFGTTIHWMAEGIDSG 136

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2751846656  82 DIILQKTYEIKDSDDYTTLLNLCHKECANLLYESL 116
Cdd:cd08820   137 DIIFEKRFPIPSDCTVISLYILAHYAAIALFGEHI 171
FMT_core_NRPS_like cd08649
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ...
 16-115 2.24e-19

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: 78.45  E-value: 2.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751846656  16 DLLVSMSFDQIFKEELLKLYPRKIINCHAGKLPFYRGRNILNWALINDEKEFGISVHFIDKGIDTGDIILQKTYEIKDSD 95
Cdd:cd08649    63 DWLFSIVNLRILPSEVLALPRKGAINFHDGPLPRYAGLNATSWALLAGETRHGVTWHRIEEGVDAGDILVQRPFDIAPDD 142

                          90       100
                  ....*....|....*....|.
gi 2751846656  96 dyTTL-LNLchkECANLLYES 115
Cdd:cd08649   143 --TALsLNL---KCYEAGIEG 158
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 9-125 2.55e-19

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: 78.95  E-value: 2.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751846656   9 ELKKYSNDLLVSMSFDQIFKEELLKLYPRKIINCHAGKLPFYRGRNILNWALINDEKEFGISVHFIDKGIDTGDIILQKT 88
Cdd:TIGR00639  74 ELRAHEVDLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAK 153

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2751846656  89 YEIKDSDDYTTLLNLCHKECANLLYESLILFLEDNVK 125
Cdd:TIGR00639 154 VPILPEDTEETLEQRIHKQEHRIYPLAIAWFAQGRLK 190
FMT_core_like_5 cd08823
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 2-114 9.97e-19

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: 77.10  E-value: 9.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751846656   2 NSKEFLNE-LKKYSNDLLVSMSFDQIFKEELLKLYPRKIINCHAGKLPFYRGRNILNWALINDEKEFGISVHFIDKGIDT 80
Cdd:cd08823    58 NLKEQLAEwLRALAADTVVVFTFPYRIPQHILDLPPLGFYNLHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMTAEIDR 137

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2751846656  81 GDIILQKTYEIKDSDDYTTLLNLCHKECANLLYE 114
Cdd:cd08823   138 GPIVLEQFTPIHPDDTYGLLCSRLAMLAVGLLEE 171
PRK08125 PRK08125
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ...
 10-116 1.00e-18

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


Pssm-ID: 236156 [Multi-domain]  Cd Length: 660  Bit Score: 80.41  E-value: 1.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751846656  10 LKKYSNDLLVSMSFDQIFKEELLKLYPRKIINCHAGKLPFYRGRNILNWALINDEKEFGISVHFIDKGIDTGDIILQKTY 89
Cdd:PRK08125   71 IRELAPDVIFSFYYRNLLSDEILQLAPAGAFNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQQRV 150

                          90       100       110
                  ....*....|....*....|....*....|
gi 2751846656  90 EIKDSDdytTLLNLCHKEC---ANLLYESL 116
Cdd:PRK08125  151 AIAPDD---TALTLHHKLChaaRQLLEQTL 177
FMT_core_FDH_N cd08647
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ...
 36-102 3.30e-12

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: 60.54  E-value: 3.30e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2751846656  36 PRKIINC--------HAGKLPFYRGRNILNWALINDEKEFGISVHFIDKGIDTGDIILQKTYEIKDSDDYTTLLN 102
Cdd:cd08647    91 PMEVIDApkhgsiiyHPSILPRHRGASAINWTLIHGDKKAGFTIFWADDGLDTGPILLQKECDVLPNDTVDTLYN 165
PRK06988 PRK06988
formyltransferase;
16-91 8.19e-12

formyltransferase;


Pssm-ID: 235902 [Multi-domain]  Cd Length: 312  Bit Score: 60.48  E-value: 8.19e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2751846656  16 DLLVSMSFDQIFKEELLKLYPRKIINCHAGKLPFYRGRNILNWALINDEKEFGISVHFIDKGIDTGDIILQKTYEI 91
Cdd:PRK06988   79 DFIFSFYYRHMIPVDLLALAPRGAYNMHGSLLPKYRGRVPVNWAVLNGETETGATLHEMVAKPDAGAIVDQTAVPI 154
PLN02285 PLN02285
methionyl-tRNA formyltransferase
 2-116 3.86e-10

methionyl-tRNA formyltransferase


Pssm-ID: 215159 [Multi-domain]  Cd Length: 334  Bit Score: 55.85  E-value: 3.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751846656   2 NSKEFLNELKKYSNDLLVSMSFDQIFKEELLKLYPRKIINCHAGKLPFYRGRNILNWALINDEKEFGISVHFIDKGIDTG 81
Cdd:PLN02285   81 GEEDFLSALRELQPDLCITAAYGNILPQKFLDIPKLGTVNIHPSLLPLYRGAAPVQRALQDGVNETGVSVAFTVRALDAG 160

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2751846656  82 DIILQKTYEIKDSDDYTTLLNLCHKECANLLYESL 116
Cdd:PLN02285  161 PVIAQERVEVDEDIKAPELLPLLFELGTKLLLREL 195
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 5-124 3.34e-09

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 52.39  E-value: 3.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751846656   5 EFLNELKKYSNDLLVSMSFDQIFKEELLKLYPRKIINCHAGKLPFYRGRNI----LNWALINDEKEF-GISVHFIDKGID 79
Cdd:PLN02331   69 ELVDALRGAGVDFVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFGGKGYygikVHKAVIASGARYsGPTVHFVDEHYD 148

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2751846656  80 TGDIILQKTYEIKDSDDYTTL----LNLCHK---ECANLLYESLILFLEDNV 124
Cdd:PLN02331  149 TGRILAQRVVPVLATDTPEELaarvLHEEHQlyvEVVAALCEERIVWREDGV 200
FMT_core_like_2 cd08822
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 16-86 2.99e-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: 187724 [Multi-domain]  Cd Length: 192  Bit Score: 41.29  E-value: 2.99e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2751846656  16 DLLVSMSFDQIFKEELLKLYPRKIINCHAGKLPFYRGRNILNWALINDEKEFGISVHFIDKGIDTGDIILQ 86
Cdd:cd08822    68 DLIVAAHCHAFISAKTRARARLGAIGYHPSLLPRHRGRDAVEWTIRMRDPITGGTVYHLDDGVDGGPIAAQ 138
PRK07579 PRK07579
dTDP-4-amino-4,6-dideoxyglucose formyltransferase;
9-102 6.93e-05

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


Pssm-ID: 236058 [Multi-domain]  Cd Length: 245  Bit Score: 40.66  E-value: 6.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751846656   9 ELKKYSNDLLvsMSFDQIFKEELLKLYPRKI------INCHAGKLPFYRGRNILNWALINDEKeFGISVHFIDKGIDTGD 82
Cdd:PRK07579   54 DVAERVAEIV--ERYDLVLSFHCKQRFPAKLvngvrcINIHPGFNPYNRGWFPQVFSIINGLK-IGATIHEMDEQLDHGP 130

                          90       100
                  ....*....|....*....|
gi 2751846656  83 IILQKTYEIKDSDDYTTLLN 102
Cdd:PRK07579  131 IIAQREVEIESWDSSGSVYA 150
PRK13011 PRK13011
formyltetrahydrofolate deformylase; Reviewed
 13-86 3.87e-03

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 237266 [Multi-domain]  Cd Length: 286  Bit Score: 35.73  E-value: 3.87e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2751846656  13 YSNDLLVSMSFDQIFKEELLKLYPRKIINCHAGKLPFYRGRNILNWALINDEKEFGISVHFIDKGIDTGDIILQ 86
Cdd:PRK13011  164 SGAELVVLARYMQVLSPELCRKLAGRAINIHHSFLPGFKGAKPYHQAYERGVKLIGATAHYVTDDLDEGPIIEQ 237
 
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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