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phosphoribosylglycinamide formyltransferase [Draconibacterium orientale]

Protein Classification

phosphoribosylglycinamide formyltransferase( domain architecture ID 10171287)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 5-185 2.80e-84

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: 246.53  E-value: 2.80e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029   5 RIAVFASGSGTNAENIFKYFL-GNEKIKIDSLWANKSEAYALVRAQKHGVETFVFNRNQFYN----TNEIIETLRNRKVD 79
Cdd:cd08645    1 RIAVLASGSGSNLQALIDAIKsGKLNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSreefDEALLELLKEYKVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029  80 VIVLAGFLWLIPDKLVENFT--IINIHPALLPKYggkgmYGMHVHKAVVENKETHSGITIHYVNQNYDEGKIIFQTQCEV 157
Cdd:cd08645   81 LIVLAGFMRILSPEFLEAFPgrIINIHPSLLPKF-----YGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPV 155

                        170       180
                 ....*....|....*....|....*...
gi 610422029 158 LPNDTPEQLAAKVHALEYEHYPQVIEKV 185
Cdd:cd08645  156 LPGDTPETLAERIHALEHRLYPEAIKLL 183
 
Name Accession Description Interval E-value
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 5-185 2.80e-84

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: 246.53  E-value: 2.80e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029   5 RIAVFASGSGTNAENIFKYFL-GNEKIKIDSLWANKSEAYALVRAQKHGVETFVFNRNQFYN----TNEIIETLRNRKVD 79
Cdd:cd08645    1 RIAVLASGSGSNLQALIDAIKsGKLNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSreefDEALLELLKEYKVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029  80 VIVLAGFLWLIPDKLVENFT--IINIHPALLPKYggkgmYGMHVHKAVVENKETHSGITIHYVNQNYDEGKIIFQTQCEV 157
Cdd:cd08645   81 LIVLAGFMRILSPEFLEAFPgrIINIHPSLLPKF-----YGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPV 155

                        170       180
                 ....*....|....*....|....*...
gi 610422029 158 LPNDTPEQLAAKVHALEYEHYPQVIEKV 185
Cdd:cd08645  156 LPGDTPETLAERIHALEHRLYPEAIKLL 183
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 4-188 2.19e-67

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: 204.50  E-value: 2.19e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029   4 KRIAVFASGSGTNAENIFKYF-LGNEKIKIDSLWANKSEAYALVRAQKHGVETFVFNRNQFYNTN----EIIETLRNRKV 78
Cdd:COG0299    2 KRIAVLISGRGSNLQALIDAIeAGDLPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREafdaALLEALDAYGP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029  79 DVIVLAGFLWLIPDKLVENFT--IINIHPALLPKYGGkgmygMHVHKAVVENKETHSGITIHYVNQNYDEGKIIFQTQCE 156
Cdd:COG0299   82 DLVVLAGFMRILTPEFVRAFPgrIINIHPSLLPAFPG-----LHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVP 156

                        170       180       190
                 ....*....|....*....|....*....|..
gi 610422029 157 VLPNDTPEQLAAKVHALEYEHYPQVIEKVLNR 188
Cdd:COG0299  157 VLPDDTEETLAARILEQEHRLYPEAIRLLAEG 188
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 5-182 5.98e-54

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 170.64  E-value: 5.98e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029   5 RIAVFASGSGTNAENIFKYFLGNE-KIKIDSLWANKSEAYALVRAQKHGVETFVFNRNQF----YNTNEIIETLRNRKVD 79
Cdd:PLN02331   1 KLAVFVSGGGSNFRAIHDACLDGRvNGDVVVVVTNKPGCGGAEYARENGIPVLVYPKTKGepdgLSPDELVDALRGAGVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029  80 VIVLAGFLWLIPDKLVENF--TIINIHPALLPKYGGKGMYGMHVHKAVVENKETHSGITIHYVNQNYDEGKIIFQTQCEV 157
Cdd:PLN02331  81 FVLLAGYLKLIPVELVRAYprSILNIHPALLPAFGGKGYYGIKVHKAVIASGARYSGPTVHFVDEHYDTGRILAQRVVPV 160

                        170       180
                 ....*....|....*....|....*
gi 610422029 158 LPNDTPEQLAAKVHALEYEHYPQVI 182
Cdd:PLN02331 161 LATDTPEELAARVLHEEHQLYVEVV 185
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 4-189 5.62e-50

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: 159.84  E-value: 5.62e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029    4 KRIAVFASGSGTNAENIFKYFL-GNEKIKIDSLWANKSEAYALVRAQKHGVETFVFNRNQFYNT----NEIIETLRNRKV 78
Cdd:TIGR00639   1 KRIVVLISGNGSNLQAIIDACKeGKIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSReafdQAIIEELRAHEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029   79 DVIVLAGFLWLIPDKLVENFT--IINIHPALLPKYGgkgmyGMHVHKAVVENKETHSGITIHYVNQNYDEGKIIFQTQCE 156
Cdd:TIGR00639  81 DLVVLAGFMRILGPTFLSRFAgrILNIHPSLLPAFP-----GLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVP 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 610422029  157 VLPNDTPEQLAAKVHALEYEHYPQVIEKVLNRN 189
Cdd:TIGR00639 156 ILPEDTEETLEQRIHKQEHRIYPLAIAWFAQGR 188
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 4-182 2.22e-46

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: 150.52  E-value: 2.22e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029    4 KRIAVFASGSGTNAENIF-KYFLGNEKIKIDSLWANKSEAYALVRAQKHGVETFVFNRNQFYNT----NEIIETLRNRKV 78
Cdd:pfam00551   1 MKIAVLISGTGSNLQALIdALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRslfdQELADALRALAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029   79 DVIVLAGFLWLIPDKLVENFT--IINIHPALLPKYggkgmYGMHVHKAVVENKETHSGITIHYVNQNYDEGKIIFQTQCE 156
Cdd:pfam00551  81 DVIVLAGYMRILPPEFLQAPPggILNIHPSLLPRF-----RGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVP 155

                         170       180
                  ....*....|....*....|....*.
gi 610422029  157 VLPNDTPEQLAAKVHALEYEHYPQVI 182
Cdd:pfam00551 156 ILPDDTAETLYNRVADLEHKALPRVL 181
 
Name Accession Description Interval E-value
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 5-185 2.80e-84

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: 246.53  E-value: 2.80e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029   5 RIAVFASGSGTNAENIFKYFL-GNEKIKIDSLWANKSEAYALVRAQKHGVETFVFNRNQFYN----TNEIIETLRNRKVD 79
Cdd:cd08645    1 RIAVLASGSGSNLQALIDAIKsGKLNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSreefDEALLELLKEYKVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029  80 VIVLAGFLWLIPDKLVENFT--IINIHPALLPKYggkgmYGMHVHKAVVENKETHSGITIHYVNQNYDEGKIIFQTQCEV 157
Cdd:cd08645   81 LIVLAGFMRILSPEFLEAFPgrIINIHPSLLPKF-----YGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPV 155

                        170       180
                 ....*....|....*....|....*...
gi 610422029 158 LPNDTPEQLAAKVHALEYEHYPQVIEKV 185
Cdd:cd08645  156 LPGDTPETLAERIHALEHRLYPEAIKLL 183
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 4-188 2.19e-67

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: 204.50  E-value: 2.19e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029   4 KRIAVFASGSGTNAENIFKYF-LGNEKIKIDSLWANKSEAYALVRAQKHGVETFVFNRNQFYNTN----EIIETLRNRKV 78
Cdd:COG0299    2 KRIAVLISGRGSNLQALIDAIeAGDLPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREafdaALLEALDAYGP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029  79 DVIVLAGFLWLIPDKLVENFT--IINIHPALLPKYGGkgmygMHVHKAVVENKETHSGITIHYVNQNYDEGKIIFQTQCE 156
Cdd:COG0299   82 DLVVLAGFMRILTPEFVRAFPgrIINIHPSLLPAFPG-----LHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVP 156

                        170       180       190
                 ....*....|....*....|....*....|..
gi 610422029 157 VLPNDTPEQLAAKVHALEYEHYPQVIEKVLNR 188
Cdd:COG0299  157 VLPDDTEETLAARILEQEHRLYPEAIRLLAEG 188
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 5-182 5.98e-54

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 170.64  E-value: 5.98e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029   5 RIAVFASGSGTNAENIFKYFLGNE-KIKIDSLWANKSEAYALVRAQKHGVETFVFNRNQF----YNTNEIIETLRNRKVD 79
Cdd:PLN02331   1 KLAVFVSGGGSNFRAIHDACLDGRvNGDVVVVVTNKPGCGGAEYARENGIPVLVYPKTKGepdgLSPDELVDALRGAGVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029  80 VIVLAGFLWLIPDKLVENF--TIINIHPALLPKYGGKGMYGMHVHKAVVENKETHSGITIHYVNQNYDEGKIIFQTQCEV 157
Cdd:PLN02331  81 FVLLAGYLKLIPVELVRAYprSILNIHPALLPAFGGKGYYGIKVHKAVIASGARYSGPTVHFVDEHYDTGRILAQRVVPV 160

                        170       180
                 ....*....|....*....|....*
gi 610422029 158 LPNDTPEQLAAKVHALEYEHYPQVI 182
Cdd:PLN02331 161 LATDTPEELAARVLHEEHQLYVEVV 185
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 4-189 5.62e-50

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: 159.84  E-value: 5.62e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029    4 KRIAVFASGSGTNAENIFKYFL-GNEKIKIDSLWANKSEAYALVRAQKHGVETFVFNRNQFYNT----NEIIETLRNRKV 78
Cdd:TIGR00639   1 KRIVVLISGNGSNLQAIIDACKeGKIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSReafdQAIIEELRAHEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029   79 DVIVLAGFLWLIPDKLVENFT--IINIHPALLPKYGgkgmyGMHVHKAVVENKETHSGITIHYVNQNYDEGKIIFQTQCE 156
Cdd:TIGR00639  81 DLVVLAGFMRILGPTFLSRFAgrILNIHPSLLPAFP-----GLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVP 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 610422029  157 VLPNDTPEQLAAKVHALEYEHYPQVIEKVLNRN 189
Cdd:TIGR00639 156 ILPEDTEETLEQRIHKQEHRIYPLAIAWFAQGR 188
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 4-182 2.22e-46

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: 150.52  E-value: 2.22e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029    4 KRIAVFASGSGTNAENIF-KYFLGNEKIKIDSLWANKSEAYALVRAQKHGVETFVFNRNQFYNT----NEIIETLRNRKV 78
Cdd:pfam00551   1 MKIAVLISGTGSNLQALIdALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRslfdQELADALRALAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029   79 DVIVLAGFLWLIPDKLVENFT--IINIHPALLPKYggkgmYGMHVHKAVVENKETHSGITIHYVNQNYDEGKIIFQTQCE 156
Cdd:pfam00551  81 DVIVLAGYMRILPPEFLQAPPggILNIHPSLLPRF-----RGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVP 155

                         170       180
                  ....*....|....*....|....*.
gi 610422029  157 VLPNDTPEQLAAKVHALEYEHYPQVI 182
Cdd:pfam00551 156 ILPDDTAETLYNRVADLEHKALPRVL 181
FMT_core cd08369
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...
 6-188 1.40e-27

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: 101.98  E-value: 1.40e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029   6 IAVFasGSGTNAENIFKYFLGNEKIKIDSLWANKSEAYALVRAQKHGVE-TFVFNRNQfyNTNEIIETLRNRKVDVIVLA 84
Cdd:cd08369    1 IVIL--GSGNIGQRVLKALLSKEGHEIVGVVTHPDSPRGTAQLSLELVGgKVYLDSNI--NTPELLELLKEFAPDLIVSI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029  85 GFLWLIPDKLVENF--TIINIHPALLPKYggkgmYGMHVHKAVVENKETHSGITIHYVNQNYDEGKIIFQTQCEVLPNDT 162
Cdd:cd08369   77 NFRQIIPPEILKLPpgGAINIHPSLLPRY-----RGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDT 151

                        170       180
                 ....*....|....*....|....*.
gi 610422029 163 PEQLAAKVhaleYEHYPQVIEKVLNR 188
Cdd:cd08369  152 AGTLYQRL----IELGPKLLKEALQK 173
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
46-188 2.12e-21

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


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 88.62  E-value: 2.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029  46 VRAQKHGVETFVFNRnqfYNTNEIIETLRNRKVDVIVLAGFLWLIPDKLVENFTI--INIHPALLPKYGGkgmyGMHVHK 123
Cdd:COG0223   50 ELALEHGIPVLQPES---LKDPEFLEELRALNPDLIVVVAYGQILPKEVLDIPRLgcINLHASLLPRYRG----AAPIQW 122

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 610422029 124 AVvENKETHSGITIHYVNQNYDEGKIIFQTQCEVLPNDTPEQLAAKVHALeyehYPQVIEKVLNR 188
Cdd:COG0223  123 AI-LNGDTETGVTIMQMDEGLDTGDILLQEEVPIGPDDTAGSLHDKLAEL----GAELLLETLDA 182
FMT_core_Met-tRNA-FMT_N cd08646
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ...
 46-169 3.58e-16

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: 72.86  E-value: 3.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029  46 VRAQKHGVETFVFNRNqfyNTNEIIETLRNRKVDVIVLAGFLWLIPDKLVENFT--IINIHPALLPKYGGkgmyGMHVHK 123
Cdd:cd08646   50 ELALELGLPVLQPEKL---KDEEFLEELKALKPDLIVVVAYGQILPKEILDLPPygCINVHPSLLPKYRG----AAPIQR 122

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 610422029 124 AVvENKETHSGITIHYVNQNYDEGKIIFQTQCEVLPNDTPEQLAAK 169
Cdd:cd08646  123 AI-LNGDKETGVTIMKMDEGLDTGDILAQEEVPIDPDDTAGELLDK 167
FMT_core_like_3 cd08653
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 65-183 1.29e-15

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: 70.32  E-value: 1.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029  65 NTNEIIETLRNRKVDVIVLAGFLwLIPDKL--VENFTIINIHPALLPKYggkgmYGMHVH-KAVVENKETHSGITIHYVN 141
Cdd:cd08653   35 NGPEVVAALRALAPDVVSVYGCG-IIKDALlaIPPLGVLNLHGGILPDY-----RGVHTGfWALANGDPDNVGVTVHLVD 108

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 610422029 142 QNYDEGKIIFQTQCEVLPNDTPEQLAAKVHALEYEHYPQVIE 183
Cdd:cd08653  109 AGIDTGDVLAQARPPLAAGDTLLSLYLRLYRAGVELMVEAIA 150
FMT_core_Formyl-FH4-Hydrolase_C cd08648
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ...
 48-169 9.12e-14

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: 66.43  E-value: 9.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029  48 AQKHGVETFVF---NRNQFYNTNEIIETLRNRKVDVIVLAGFLWLIPDKLVENFT--IINIHPALLPKYGGKGMYgmhvH 122
Cdd:cd08648   44 AERFGIPFHHIpvtKDTKAEAEAEQLELLEEYGVDLVVLARYMQILSPDFVERYPnrIINIHHSFLPAFKGAKPY----H 119

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 610422029 123 KAvvenketHS------GITIHYVNQNYDEGKIIFQTQCEVLPNDTPEQLAAK 169
Cdd:cd08648  120 QA-------FErgvkliGATAHYVTEELDEGPIIEQDVERVSHRDSVEDLVRK 165
FMT_core_ArnA_N cd08644
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ...
 48-170 7.01e-13

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: 64.29  E-value: 7.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029  48 AQKHGVETFvfnRNQFYNTNEIIETLRNRKVDVIVLAGFLWLIPDKLVE--NFTIINIHPALLPKYGGKgmygMHVHKAV 125
Cdd:cd08644   49 AREHGIPVF---TPDDINHPEWVERLRALKPDLIFSFYYRHMISEDILEiaRLGAFNLHGSLLPKYRGR----APLNWAL 121

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 610422029 126 VeNKETHSGITIHYVNQNYDEGKIIFQTQCEVLPNDTPEQLAAKV 170
Cdd:cd08644  122 I-NGETETGVTLHRMTKKPDAGAIVDQEKVPILPDDTAKSLFHKL 165
fmt TIGR00460
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ...
 68-173 8.18e-13

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: 65.11  E-value: 8.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029   68 EIIETLRNRKVDVIVLAGFLWLIPDKLVENF--TIINIHPALLPKYGGkgmyGMHVHKAVVeNKETHSGITIHYVNQNYD 145
Cdd:TIGR00460  69 EELPLVRELKPDVIVVVSFGKILPKEFLDLFpyGCINVHPSLLPRWRG----GAPIQRAIL-NGDKKTGVTIMQMVPKMD 143

                          90       100
                  ....*....|....*....|....*...
gi 610422029  146 EGKIIFQTQCEVLPNDTPEQLAAKVHAL 173
Cdd:TIGR00460 144 AGDILKQETFPIEEEDNSGTLSDKLSEL 171
PurU COG0788
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ...
 68-169 1.51e-11

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: 61.22  E-value: 1.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029  68 EIIETLRNRKVDVIVLAGFLWLIPDKLVENFT--IINIHPALLPKYGGKGMYgmhvHKAvvenketHS------GITIHY 139
Cdd:COG0788  153 RLLELLEEYDIDLVVLARYMQILSPDFCARLPgrIINIHHSFLPAFKGAKPY----HQA-------YErgvkliGATAHY 221

                         90       100       110
                 ....*....|....*....|....*....|
gi 610422029 140 VNQNYDEGKIIFQTQCEVLPNDTPEQLAAK 169
Cdd:COG0788  222 VTADLDEGPIIEQDVERVDHRDTPEDLVRK 251
FMT_core_like_4 cd08651
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 33-170 6.89e-11

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


Pssm-ID: 187720 [Multi-domain]  Cd Length: 180  Bit Score: 58.43  E-value: 6.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029  33 DSLWANKSEAYALVR-AQKHGVETFVFNRNqfyNTNEIIETLRNRKVDVIVLAGFLWLIPDKLVE--NFTIINIHPALLP 109
Cdd:cd08651   33 DSSSNNDSDYLDLDSfARKNGIPYYKFTDI---NDEEIIEWIKEANPDIIFVFGWSQLLKPEILAipRLGVIGFHPTKLP 109

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 610422029 110 KYGGKGMygmhVHKAVVEN-KEThsGITIHYVNQNYDEGKIIFQTQCEVLPNDTPEQLAAKV 170
Cdd:cd08651  110 KNRGRAP----IPWAILLGlKET--ASTFFWMDEGADSGDILSQEPFPIDKDDTANSLYDKI 165
PRK06988 PRK06988
formyltransferase;
48-170 1.64e-10

formyltransferase;


Pssm-ID: 235902 [Multi-domain]  Cd Length: 312  Bit Score: 58.55  E-value: 1.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029  48 AQKHGVETFVFNRNqfyNTNEIIETLRNRKVDVIVLAGFLWLIPDKLVENFTI--INIHPALLPKYGGKgmygMHVHKAV 125
Cdd:PRK06988  51 AAEHGIPVITPADP---NDPELRAAVAAAAPDFIFSFYYRHMIPVDLLALAPRgaYNMHGSLLPKYRGR----VPVNWAV 123

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 610422029 126 VeNKETHSGITIHYVNQNYDEGKIIFQTQCEVLPNDTPEQLAAKV 170
Cdd:PRK06988 124 L-NGETETGATLHEMVAKPDAGAIVDQTAVPILPDDTAAQVFDKV 167
purU PRK06027
formyltetrahydrofolate deformylase; Reviewed
 68-169 7.25e-09

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 235676 [Multi-domain]  Cd Length: 286  Bit Score: 53.96  E-value: 7.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029  68 EIIETLRNRKVDVIVLAGFLWLIPDKLVENFT--IINIHPALLPKYGGKGMYgmhvHKAvvenketHS------GITIHY 139
Cdd:PRK06027 156 RLLELIDEYQPDLVVLARYMQILSPDFVARFPgrIINIHHSFLPAFKGAKPY----HQA-------YErgvkliGATAHY 224

                         90       100       110
                 ....*....|....*....|....*....|...
gi 610422029 140 VNQNYDEGKIIFQtqcEVLP---NDTPEQLAAK 169
Cdd:PRK06027 225 VTADLDEGPIIEQ---DVIRvdhRDTAEDLVRA 254
FMT_core_like_5 cd08823
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 71-162 1.54e-08

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


Pssm-ID: 187725 [Multi-domain]  Cd Length: 177  Bit Score: 51.68  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029  71 ETLRNRKVDVIVLAGFLWLIPDKLVE--NFTIINIHPALLPKYGGKG-MYGMhvhkavVENKETHSGITIHYVNQNYDEG 147
Cdd:cd08823   65 EWLRALAADTVVVFTFPYRIPQHILDlpPLGFYNLHPGLLPAYRGPDpLFWQ------IRNQEQETAITVHKMTAEIDRG 138

                         90
                 ....*....|....*
gi 610422029 148 KIIFQTQCEVLPNDT 162
Cdd:cd08823  139 PIVLEQFTPIHPDDT 153
FMT_core_like_6 cd08820
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 65-184 2.26e-08

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


Pssm-ID: 187722 [Multi-domain]  Cd Length: 173  Bit Score: 51.29  E-value: 2.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029  65 NTNEIIETLRNRKVDVIVLAGFLWLIPDKLVE--NFTIINIHPALLPKYGGkgmYGMHVHkaVVENKETHSGITIHYVNQ 142
Cdd:cd08820   57 NLHKLLEILENKGVDILISVQYHWILPGSILEkaKEIAFNLHNAPLPEYRG---CNQFSH--AILNGDDQFGTTIHWMAE 131

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 610422029 143 NYDEGKIIFQTQCEVLPNDTPEQLAAKVHALEYEHYPQVIEK 184
Cdd:cd08820  132 GIDSGDIIFEKRFPIPSDCTVISLYILAHYAAIALFGEHITD 173
FMT_core_NRPS_like cd08649
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ...
 48-185 5.80e-08

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: 49.95  E-value: 5.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029  48 AQKHGVEtfVFNrnqfyNTNEIIETLRNRKVDVIVLAGFLWLIPDKLVENFTI--INIHPALLPKYGGkgmygMHVHKAV 125
Cdd:cd08649   39 AAAEGIA--VLE-----PGEALEELLSDEPFDWLFSIVNLRILPSEVLALPRKgaINFHDGPLPRYAG-----LNATSWA 106

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029 126 VENKETHSGITIHYVNQNYDEGKIIFQTQCEVLPNDTPEQLAAKVHALEYEHYPQVIEKV 185
Cdd:cd08649  107 LLAGETRHGVTWHRIEEGVDAGDILVQRPFDIAPDDTALSLNLKCYEAGIEGFGELIDEL 166
PRK13011 PRK13011
formyltetrahydrofolate deformylase; Reviewed
 79-169 1.23e-07

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 237266 [Multi-domain]  Cd Length: 286  Bit Score: 50.37  E-value: 1.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029  79 DVIVLAGFLWLIPDKLVENFT--IINIHPALLPKYGGKGMYgmhvHKAvvenketHS------GITIHYVNQNYDEGKII 150
Cdd:PRK13011 167 ELVVLARYMQVLSPELCRKLAgrAINIHHSFLPGFKGAKPY----HQA-------YErgvkliGATAHYVTDDLDEGPII 235

                         90
                 ....*....|....*....
gi 610422029 151 FQTQCEVLPNDTPEQLAAK 169
Cdd:PRK13011 236 EQDVERVDHAYSPEDLVAK 254
purU PRK13010
formyltetrahydrofolate deformylase; Reviewed
 20-169 5.81e-07

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 139334 [Multi-domain]  Cd Length: 289  Bit Score: 48.25  E-value: 5.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029  20 IFKYFLGNEKIKIDSLWANKSEAYALVRaqKHGVETFVF---NRNQFYNTNEIIETLRNRKVDVIVLAGFLWLIPDKLVE 96
Cdd:PRK13010 111 LYRWRMGELDMDIVGIISNHPDLQPLAV--QHDIPFHHLpvtPDTKAQQEAQILDLIETSGAELVVLARYMQVLSDDLSR 188

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 610422029  97 NFT--IINIHPALLPKYGGKGMYgmhvHKAVVENKEThSGITIHYVNQNYDEGKIIFQTQCEVLPNDTPEQLAAK 169
Cdd:PRK13010 189 KLSgrAINIHHSFLPGFKGARPY----HQAHARGVKL-IGATAHFVTDDLDEGPIIEQDVERVDHSYSPEDLVAK 258
PRK07579 PRK07579
dTDP-4-amino-4,6-dideoxyglucose formyltransferase;
65-189 7.21e-07

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


Pssm-ID: 236058 [Multi-domain]  Cd Length: 245  Bit Score: 47.98  E-value: 7.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029  65 NTNEIIEtlrnrKVDVIVLAGFLWLIPDKLVENFTIINIHPALLPKygGKGMYGmHVHKAVVENKethSGITIHYVNQNY 144
Cdd:PRK07579  58 RVAEIVE-----RYDLVLSFHCKQRFPAKLVNGVRCINIHPGFNPY--NRGWFP-QVFSIINGLK---IGATIHEMDEQL 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 610422029 145 DEGKIIFQTQCEVLPNDTPEQLAAKVHALEYEHYPQVIEKVLNRN 189
Cdd:PRK07579 127 DHGPIIAQREVEIESWDSSGSVYARVMDIERELVLEHFDAIRDGS 171
FMT_core_FDH_N cd08647
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ...
 46-174 1.04e-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: 47.06  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029  46 VRAQKHGVETFVFNRNQFYNTN--EIIETLRNRKVDVIVLAGFLWLIPDKLVE---NFTIInIHPALLPKYGGKGMYG-- 118
Cdd:cd08647   44 LEAEKDGVPVFKFPRWRAKGQAipEVVAKYKALGAELNVLPFCSQFIPMEVIDapkHGSII-YHPSILPRHRGASAINwt 122

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 610422029 119 -MHVHKavvenketHSGITIHYVNQNYDEGKIIFQTQCEVLPNDT----------PEQLAAKVHALE 174
Cdd:cd08647  123 lIHGDK--------KAGFTIFWADDGLDTGPILLQKECDVLPNDTvdtlynrflyPEGIKAMVEAVR 181
FMT_core_like_2 cd08822
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 78-166 3.87e-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: 42.45  E-value: 3.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029  78 VDVIVLAGFLWLIPDK--LVENFTIINIHPALLPKYGGKGMygmhVHKAVVENkETHSGITIHYVNQNYDEGKIIFQTQC 155
Cdd:cd08822   67 TDLIVAAHCHAFISAKtrARARLGAIGYHPSLLPRHRGRDA----VEWTIRMR-DPITGGTVYHLDDGVDGGPIAAQDWC 141

                         90
                 ....*....|.
gi 610422029 156 EVLPNDTPEQL 166
Cdd:cd08822  142 HVRPGDTAAEL 152
PLN02828 PLN02828
formyltetrahydrofolate deformylase
 68-174 1.21e-04

formyltetrahydrofolate deformylase


Pssm-ID: 178422  Cd Length: 268  Bit Score: 41.27  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029  68 EIIETLRNrkVDVIVLAGFLWLIPDKLVENF--TIINIHPALLPKYGGKgmygmHVHKAVVENKETHSGITIHYVNQNYD 145
Cdd:PLN02828 140 EILELVKG--TDFLVLARYMQILSGNFLKGYgkDIINIHHGLLPSFKGG-----NPSKQAFDAGVKLIGATSHFVTEELD 212

                         90       100
                 ....*....|....*....|....*....
gi 610422029 146 EGKIIFQTQCEVLPNDTPEQLAAKVHALE 174
Cdd:PLN02828 213 AGPIIEQMVERVSHRDNLRSFVQKSENLE 241
PRK08125 PRK08125
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ...
 102-170 2.84e-04

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


Pssm-ID: 236156 [Multi-domain]  Cd Length: 660  Bit Score: 40.74  E-value: 2.84e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 610422029 102 NIHPALLPKYGGKGMYGMhvhkaVVENKETHSGITIHYVNQNYDEGKIIFQTQCEVLPNDTPEQLAAKV 170
Cdd:PRK08125 102 NLHGSLLPKYRGRAPLNW-----VLVNGETETGVTLHRMVKRADAGAIVAQQRVAIAPDDTALTLHHKL 165
PLN02285 PLN02285
methionyl-tRNA formyltransferase
 70-173 5.92e-04

methionyl-tRNA formyltransferase


Pssm-ID: 215159 [Multi-domain]  Cd Length: 334  Bit Score: 39.68  E-value: 5.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610422029  70 IETLRNRKVDVIVLAGFLWLIPDKLVE--NFTIINIHPALLPKYGGKGmygmHVHKAvVENKETHSGITIHYVNQNYDEG 147
Cdd:PLN02285  86 LSALRELQPDLCITAAYGNILPQKFLDipKLGTVNIHPSLLPLYRGAA----PVQRA-LQDGVNETGVSVAFTVRALDAG 160

                         90       100
                 ....*....|....*....|....*.
gi 610422029 148 KIIFQTQCEVLPNDTPEQLAAKVHAL 173
Cdd:PLN02285 161 PVIAQERVEVDEDIKAPELLPLLFEL 186
 
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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