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phosphoribosylglycinamide formyltransferase [Dichelobacter nodosus]

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); ...
 4-185 5.71e-80

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: 235.74  E-value: 5.71e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922   4 ICVLISGGGSNLAALIAAISCYQWNIRINSVIADRTCA-GKQHAIAAQIPFHLVDRTL--DKTTFAEQLIATV-PPETEL 79
Cdd:cd08645    2 IAVLASGSGSNLQALIDAIKSGKLNAEIVLVISNNPDAyGLERAKKAGIPTFVINRKDfpSREEFDEALLELLkEYKVDL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922  80 IVLAGFLSIIPPSLLHHFP-RIINIHPSLLPKFggagmYGLKVHQAVIAAGERESGCTVHWVNQEIDGGAILAQNRVSVF 158
Cdd:cd08645   82 IVLAGFMRILSPEFLEAFPgRIINIHPSLLPKF-----YGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVL 156

                        170       180
                 ....*....|....*....|....*..
gi 500335922 159 PDDTPEQLQQRILAYEHQLLPATIARL 185
Cdd:cd08645  157 PGDTPETLAERIHALEHRLYPEAIKLL 183
 
Name Accession Description Interval E-value
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 4-185 5.71e-80

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: 235.74  E-value: 5.71e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922   4 ICVLISGGGSNLAALIAAISCYQWNIRINSVIADRTCA-GKQHAIAAQIPFHLVDRTL--DKTTFAEQLIATV-PPETEL 79
Cdd:cd08645    2 IAVLASGSGSNLQALIDAIKSGKLNAEIVLVISNNPDAyGLERAKKAGIPTFVINRKDfpSREEFDEALLELLkEYKVDL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922  80 IVLAGFLSIIPPSLLHHFP-RIINIHPSLLPKFggagmYGLKVHQAVIAAGERESGCTVHWVNQEIDGGAILAQNRVSVF 158
Cdd:cd08645   82 IVLAGFMRILSPEFLEAFPgRIINIHPSLLPKF-----YGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVL 156

                        170       180
                 ....*....|....*....|....*..
gi 500335922 159 PDDTPEQLQQRILAYEHQLLPATIARL 185
Cdd:cd08645  157 PGDTPETLAERIHALEHRLYPEAIKLL 183
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 1-187 1.18e-73

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: 220.68  E-value: 1.18e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922   1 MHQICVLISGGGSNLAALIAAISCYQWNIRINSVIADR-TCAGKQHAIAAQIPFHLVDRTL--DKTTFAEQLIATVPP-E 76
Cdd:COG0299    1 MKRIAVLISGRGSNLQALIDAIEAGDLPAEIVLVISNRpDAYGLERARAAGIPTFVLDHKDfpSREAFDAALLEALDAyG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922  77 TELIVLAGFLSIIPPSLLHHFP-RIINIHPSLLPKFGGagmygLKVHQAVIAAGERESGCTVHWVNQEIDGGAILAQNRV 155
Cdd:COG0299   81 PDLVVLAGFMRILTPEFVRAFPgRIINIHPSLLPAFPG-----LHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAV 155

                        170       180       190
                 ....*....|....*....|....*....|..
gi 500335922 156 SVFPDDTPEQLQQRILAYEHQLLPATIARLFA 187
Cdd:COG0299  156 PVLPDDTEETLAARILEQEHRLYPEAIRLLAE 187
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 6-185 7.45e-55

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 172.95  E-value: 7.45e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922   6 VLISGGGSNLAALIAAISCYQWNIRINSVIADR-TCAGKQHAIAAQIPFHLVDRTLDKT--TFAEQLIATV-PPETELIV 81
Cdd:PLN02331   4 VFVSGGGSNFRAIHDACLDGRVNGDVVVVVTNKpGCGGAEYARENGIPVLVYPKTKGEPdgLSPDELVDALrGAGVDFVL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922  82 LAGFLSIIPPSLLHHFPR-IINIHPSLLPKFGGAGMYGLKVHQAVIAAGERESGCTVHWVNQEIDGGAILAQNRVSVFPD 160
Cdd:PLN02331  84 LAGYLKLIPVELVRAYPRsILNIHPALLPAFGGKGYYGIKVHKAVIASGARYSGPTVHFVDEHYDTGRILAQRVVPVLAT 163

                        170       180
                 ....*....|....*....|....*
gi 500335922 161 DTPEQLQQRILAYEHQLLPATIARL 185
Cdd:PLN02331 164 DTPEELAARVLHEEHQLYVEVVAAL 188
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 4-185 3.59e-51

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: 163.31  E-value: 3.59e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922    4 ICVLISGGGSNLAALIAAISCYQWNIRINSVIADRT-CAGKQHAIAAQIPFHLVDRT--LDKTTFAEQLIATVPP-ETEL 79
Cdd:TIGR00639   3 IVVLISGNGSNLQAIIDACKEGKIPASVVLVISNKPdAYGLERAAQAGIPTFVLSLKdfPSREAFDQAIIEELRAhEVDL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922   80 IVLAGFLSIIPPSLLHHFP-RIINIHPSLLPKFGGagmygLKVHQAVIAAGERESGCTVHWVNQEIDGGAILAQNRVSVF 158
Cdd:TIGR00639  83 VVLAGFMRILGPTFLSRFAgRILNIHPSLLPAFPG-----LHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPIL 157

                         170       180
                  ....*....|....*....|....*..
gi 500335922  159 PDDTPEQLQQRILAYEHQLLPATIARL 185
Cdd:TIGR00639 158 PEDTEETLEQRIHKQEHRIYPLAIAWF 184
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 4-182 1.23e-49

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: 158.99  E-value: 1.23e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922    4 ICVLISGGGSNLAALIAAISCYQWNIRINSVIADR-TCAGKQHAIAAQIPFHLVD------RTLDKTTFAEQLIATVPpe 76
Cdd:pfam00551   3 IAVLISGTGSNLQALIDALRKGGQDADVVLVISNKdKAAGLGRAEQAGIPTFVFEhkgltpRSLFDQELADALRALAA-- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922   77 tELIVLAGFLSIIPPSLLHHFP-RIINIHPSLLPKFggagmYGLKVHQAVIAAGERESGCTVHWVNQEIDGGAILAQNRV 155
Cdd:pfam00551  81 -DVIVLAGYMRILPPEFLQAPPgGILNIHPSLLPRF-----RGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAV 154

                         170       180
                  ....*....|....*....|....*..
gi 500335922  156 SVFPDDTPEQLQQRILAYEHQLLPATI 182
Cdd:pfam00551 155 PILPDDTAETLYNRVADLEHKALPRVL 181
 
Name Accession Description Interval E-value
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 4-185 5.71e-80

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: 235.74  E-value: 5.71e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922   4 ICVLISGGGSNLAALIAAISCYQWNIRINSVIADRTCA-GKQHAIAAQIPFHLVDRTL--DKTTFAEQLIATV-PPETEL 79
Cdd:cd08645    2 IAVLASGSGSNLQALIDAIKSGKLNAEIVLVISNNPDAyGLERAKKAGIPTFVINRKDfpSREEFDEALLELLkEYKVDL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922  80 IVLAGFLSIIPPSLLHHFP-RIINIHPSLLPKFggagmYGLKVHQAVIAAGERESGCTVHWVNQEIDGGAILAQNRVSVF 158
Cdd:cd08645   82 IVLAGFMRILSPEFLEAFPgRIINIHPSLLPKF-----YGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVL 156

                        170       180
                 ....*....|....*....|....*..
gi 500335922 159 PDDTPEQLQQRILAYEHQLLPATIARL 185
Cdd:cd08645  157 PGDTPETLAERIHALEHRLYPEAIKLL 183
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 1-187 1.18e-73

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: 220.68  E-value: 1.18e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922   1 MHQICVLISGGGSNLAALIAAISCYQWNIRINSVIADR-TCAGKQHAIAAQIPFHLVDRTL--DKTTFAEQLIATVPP-E 76
Cdd:COG0299    1 MKRIAVLISGRGSNLQALIDAIEAGDLPAEIVLVISNRpDAYGLERARAAGIPTFVLDHKDfpSREAFDAALLEALDAyG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922  77 TELIVLAGFLSIIPPSLLHHFP-RIINIHPSLLPKFGGagmygLKVHQAVIAAGERESGCTVHWVNQEIDGGAILAQNRV 155
Cdd:COG0299   81 PDLVVLAGFMRILTPEFVRAFPgRIINIHPSLLPAFPG-----LHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAV 155

                        170       180       190
                 ....*....|....*....|....*....|..
gi 500335922 156 SVFPDDTPEQLQQRILAYEHQLLPATIARLFA 187
Cdd:COG0299  156 PVLPDDTEETLAARILEQEHRLYPEAIRLLAE 187
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 6-185 7.45e-55

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 172.95  E-value: 7.45e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922   6 VLISGGGSNLAALIAAISCYQWNIRINSVIADR-TCAGKQHAIAAQIPFHLVDRTLDKT--TFAEQLIATV-PPETELIV 81
Cdd:PLN02331   4 VFVSGGGSNFRAIHDACLDGRVNGDVVVVVTNKpGCGGAEYARENGIPVLVYPKTKGEPdgLSPDELVDALrGAGVDFVL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922  82 LAGFLSIIPPSLLHHFPR-IINIHPSLLPKFGGAGMYGLKVHQAVIAAGERESGCTVHWVNQEIDGGAILAQNRVSVFPD 160
Cdd:PLN02331  84 LAGYLKLIPVELVRAYPRsILNIHPALLPAFGGKGYYGIKVHKAVIASGARYSGPTVHFVDEHYDTGRILAQRVVPVLAT 163

                        170       180
                 ....*....|....*....|....*
gi 500335922 161 DTPEQLQQRILAYEHQLLPATIARL 185
Cdd:PLN02331 164 DTPEELAARVLHEEHQLYVEVVAAL 188
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 4-185 3.59e-51

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: 163.31  E-value: 3.59e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922    4 ICVLISGGGSNLAALIAAISCYQWNIRINSVIADRT-CAGKQHAIAAQIPFHLVDRT--LDKTTFAEQLIATVPP-ETEL 79
Cdd:TIGR00639   3 IVVLISGNGSNLQAIIDACKEGKIPASVVLVISNKPdAYGLERAAQAGIPTFVLSLKdfPSREAFDQAIIEELRAhEVDL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922   80 IVLAGFLSIIPPSLLHHFP-RIINIHPSLLPKFGGagmygLKVHQAVIAAGERESGCTVHWVNQEIDGGAILAQNRVSVF 158
Cdd:TIGR00639  83 VVLAGFMRILGPTFLSRFAgRILNIHPSLLPAFPG-----LHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPIL 157

                         170       180
                  ....*....|....*....|....*..
gi 500335922  159 PDDTPEQLQQRILAYEHQLLPATIARL 185
Cdd:TIGR00639 158 PEDTEETLEQRIHKQEHRIYPLAIAWF 184
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 4-182 1.23e-49

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: 158.99  E-value: 1.23e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922    4 ICVLISGGGSNLAALIAAISCYQWNIRINSVIADR-TCAGKQHAIAAQIPFHLVD------RTLDKTTFAEQLIATVPpe 76
Cdd:pfam00551   3 IAVLISGTGSNLQALIDALRKGGQDADVVLVISNKdKAAGLGRAEQAGIPTFVFEhkgltpRSLFDQELADALRALAA-- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922   77 tELIVLAGFLSIIPPSLLHHFP-RIINIHPSLLPKFggagmYGLKVHQAVIAAGERESGCTVHWVNQEIDGGAILAQNRV 155
Cdd:pfam00551  81 -DVIVLAGYMRILPPEFLQAPPgGILNIHPSLLPRF-----RGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAV 154

                         170       180
                  ....*....|....*....|....*..
gi 500335922  156 SVFPDDTPEQLQQRILAYEHQLLPATI 182
Cdd:pfam00551 155 PILPDDTAETLYNRVADLEHKALPRVL 181
FMT_core cd08369
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...
 78-184 2.42e-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: 101.60  E-value: 2.42e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922  78 ELIVLAGFLSIIPPSLLHHFPR-IINIHPSLLPKFGGAGMyglkVHQAVIaAGERESGCTVHWVNQEIDGGAILAQNRVS 156
Cdd:cd08369   71 DLIVSINFRQIIPPEILKLPPGgAINIHPSLLPRYRGVNP----LAWAII-NGEKETGVTVHYMDEGIDTGDIIAQEVIP 145

                         90       100
                 ....*....|....*....|....*...
gi 500335922 157 VFPDDTPEQLQQRILAYEHQLLPATIAR 184
Cdd:cd08369  146 ISPDDTAGTLYQRLIELGPKLLKEALQK 173
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
43-187 1.61e-22

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


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 92.09  E-value: 1.61e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922  43 KQHAIAAQIPFHLVDRtLDKTTFAEQLIATVPpetELIVLAGFLSIIPPSLLHHFPR-IINIHPSLLPKFGGAGmyglKV 121
Cdd:COG0223   49 KELALEHGIPVLQPES-LKDPEFLEELRALNP---DLIVVVAYGQILPKEVLDIPRLgCINLHASLLPRYRGAA----PI 120

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500335922 122 HQAVIAaGERESGCTVHWVNQEIDGGAILAQNRVSVFPDDTPEQLQQRILAYEHQLLPATIARLFA 187
Cdd:COG0223  121 QWAILN-GDTETGVTIMQMDEGLDTGDILLQEEVPIGPDDTAGSLHDKLAELGAELLLETLDALEA 185
FMT_core_Met-tRNA-FMT_N cd08646
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ...
 43-169 4.14e-20

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: 83.65  E-value: 4.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922  43 KQHAIAAQIPFHLVDRTldKTTFAEQLIATVPPEteLIVLAGFLSIIPPSLLHHFPR-IINIHPSLLPKFGGAGmyglKV 121
Cdd:cd08646   49 KELALELGLPVLQPEKL--KDEEFLEELKALKPD--LIVVVAYGQILPKEILDLPPYgCINVHPSLLPKYRGAA----PI 120

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 500335922 122 HQAvIAAGERESGCTVHWVNQEIDGGAILAQNRVSVFPDDTPEQLQQR 169
Cdd:cd08646  121 QRA-ILNGDKETGVTIMKMDEGLDTGDILAQEEVPIDPDDTAGELLDK 167
PurU COG0788
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ...
 51-169 1.42e-19

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: 83.56  E-value: 1.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922  51 IPFHLVDRT-LDKTTFAEQLIATVPP-ETELIVLAGFLSIIPPSLLHHFP-RIINIHPSLLPKFGGAGMYglkvHQA--- 124
Cdd:COG0788  135 IPFHHIPVTkETKAEAEARLLELLEEyDIDLVVLARYMQILSPDFCARLPgRIINIHHSFLPAFKGAKPY----HQAyer 210

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 500335922 125 ---VIaageresGCTVHWVNQEIDGGAILAQNRVSVFPDDTPEQLQQR 169
Cdd:COG0788  211 gvkLI-------GATAHYVTADLDEGPIIEQDVERVDHRDTPEDLVRK 251
FMT_core_Formyl-FH4-Hydrolase_C cd08648
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ...
 51-166 4.57e-18

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: 77.99  E-value: 4.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922  51 IPFHLVDRTLDKTTFAEQ----LIATVppETELIVLAGFLSIIPPSLLHHFP-RIINIHPSLLPKFGGAGMYglkvHQAv 125
Cdd:cd08648   49 IPFHHIPVTKDTKAEAEAeqleLLEEY--GVDLVVLARYMQILSPDFVERYPnRIINIHHSFLPAFKGAKPY----HQA- 121

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 500335922 126 IAAGERESGCTVHWVNQEIDGGAILAQNRVSVFPDDTPEQL 166
Cdd:cd08648  122 FERGVKLIGATAHYVTEELDEGPIIEQDVERVSHRDSVEDL 162
purU PRK06027
formyltetrahydrofolate deformylase; Reviewed
 51-168 1.43e-15

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 235676 [Multi-domain]  Cd Length: 286  Bit Score: 72.83  E-value: 1.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922  51 IPFHLVDRTLDKTTFAEQLIATVPPET--ELIVLAGFLSIIPPSLLHHFP-RIINIHPSLLPKFGGAGMYglkvHQA--- 124
Cdd:PRK06027 138 IPFHHVPVTKETKAEAEARLLELIDEYqpDLVVLARYMQILSPDFVARFPgRIINIHHSFLPAFKGAKPY----HQAyer 213

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 500335922 125 ---VIAAgeresgcTVHWVNQEIDGGAILAQNRVSVFPDDTPEQLQQ 168
Cdd:PRK06027 214 gvkLIGA-------TAHYVTADLDEGPIIEQDVIRVDHRDTAEDLVR 253
PRK13011 PRK13011
formyltetrahydrofolate deformylase; Reviewed
 43-166 7.18e-14

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 237266 [Multi-domain]  Cd Length: 286  Bit Score: 68.09  E-value: 7.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922  43 KQHAIAAQIPFHLVDRTLDKTTFAEQLIATVPPET--ELIVLAGFLSIIPPSLLHHFP-RIINIHPSLLPKFGGAGMYgl 119
Cdd:PRK13011 130 EPLAAWHGIPFHHFPITPDTKPQQEAQVLDVVEESgaELVVLARYMQVLSPELCRKLAgRAINIHHSFLPGFKGAKPY-- 207

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 500335922 120 kvHQAvIAAGERESGCTVHWVNQEIDGGAILAQNRVSVFPDDTPEQL 166
Cdd:PRK13011 208 --HQA-YERGVKLIGATAHYVTDDLDEGPIIEQDVERVDHAYSPEDL 251
fmt TIGR00460
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ...
 43-187 1.08e-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: 67.81  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922   43 KQHAIAAQIPF--HLVDRTLDKTTFAEQLiatvppETELIVLAGFLSIIPPSLLHHFP-RIINIHPSLLPKFGGAGmygl 119
Cdd:TIGR00460  49 KVLAEEKGIPVfqPEKQRQLEELPLVREL------KPDVIVVVSFGKILPKEFLDLFPyGCINVHPSLLPRWRGGA---- 118

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500335922  120 KVHQAVIaAGERESGCTVHWVNQEIDGGAILAQNRVSVFPDDTPEQLQQRILAYEHQLLPATIARLFA 187
Cdd:TIGR00460 119 PIQRAIL-NGDKKTGVTIMQMVPKMDAGDILKQETFPIEEEDNSGTLSDKLSELGAQLLIETLKELPE 185
FMT_core_like_2 cd08822
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 71-172 2.94e-12

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: 62.48  E-value: 2.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922  71 ATVPPETELIVLAGFLSIIPPSLLHHFPR-IINIHPSLLPKFGGAGmyglKVHQAvIAAGERESGCTVHWVNQEIDGGAI 149
Cdd:cd08822   61 DAIPPGTDLIVAAHCHAFISAKTRARARLgAIGYHPSLLPRHRGRD----AVEWT-IRMRDPITGGTVYHLDDGVDGGPI 135

                         90       100
                 ....*....|....*....|...
gi 500335922 150 LAQNRVSVFPDDTPEQLQQRILA 172
Cdd:cd08822  136 AAQDWCHVRPGDTAAELWRRALA 158
FMT_core_ArnA_N cd08644
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ...
 102-187 2.53e-11

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: 60.05  E-value: 2.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922 102 NIHPSLLPKFGGAGmyglKVHQAVIAaGERESGCTVHWVNQEIDGGAILAQNRVSVFPDDTPEQLQQRILAYEHQLLPAT 181
Cdd:cd08644  102 NLHGSLLPKYRGRA----PLNWALIN-GETETGVTLHRMTKKPDAGAIVDQEKVPILPDDTAKSLFHKLCVAARRLLART 176


                 ....*.
gi 500335922 182 IARLFA 187
Cdd:cd08644  177 LPALKA 182
FMT_core_like_3 cd08653
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 78-185 2.62e-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: 187721 [Multi-domain]  Cd Length: 152  Bit Score: 58.76  E-value: 2.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922  78 ELIVLAGfLSIIPPSLLHHFP-RIINIHPSLLPKFGG--AGMYGLkvhqaviAAGERES-GCTVHWVNQEIDGGAILAQN 153
Cdd:cd08653   49 DVVSVYG-CGIIKDALLAIPPlGVLNLHGGILPDYRGvhTGFWAL-------ANGDPDNvGVTVHLVDAGIDTGDVLAQA 120

                         90       100       110
                 ....*....|....*....|....*....|..
gi 500335922 154 RVSVFPDDTPEQLQQRILAYEHQLLPATIARL 185
Cdd:cd08653  121 RPPLAAGDTLLSLYLRLYRAGVELMVEAIADL 152
PLN02828 PLN02828
formyltetrahydrofolate deformylase
 51-182 4.48e-11

formyltetrahydrofolate deformylase


Pssm-ID: 178422  Cd Length: 268  Bit Score: 60.14  E-value: 4.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922  51 IPFHLVDRTldKTTFAEQLIATVPPETELIVLAGFLSIIPPSLLHHFPR-IINIHPSLLPKFGGAGMYglkvHQAvIAAG 129
Cdd:PLN02828 124 IPYHYLPTT--KENKREDEILELVKGTDFLVLARYMQILSGNFLKGYGKdIINIHHGLLPSFKGGNPS----KQA-FDAG 196

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 500335922 130 ERESGCTVHWVNQEIDGGAILAQNRVSVFPDDTPEQLQQRILAYEHQLLPATI 182
Cdd:PLN02828 197 VKLIGATSHFVTEELDAGPIIEQMVERVSHRDNLRSFVQKSENLEKQCLAKAI 249
purU PRK13010
formyltetrahydrofolate deformylase; Reviewed
 51-166 1.17e-10

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 139334 [Multi-domain]  Cd Length: 289  Bit Score: 59.04  E-value: 1.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922  51 IPFHLVDRTLDKTTFAE----QLIATvpPETELIVLAGFLSIIPPSLLHHFP-RIINIHPSLLPKFGGAGMYglkvHQAV 125
Cdd:PRK13010 142 IPFHHLPVTPDTKAQQEaqilDLIET--SGAELVVLARYMQVLSDDLSRKLSgRAINIHHSFLPGFKGARPY----HQAH 215

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 500335922 126 iAAGERESGCTVHWVNQEIDGGAILAQNRVSVFPDDTPEQL 166
Cdd:PRK13010 216 -ARGVKLIGATAHFVTDDLDEGPIIEQDVERVDHSYSPEDL 255
PLN02285 PLN02285
methionyl-tRNA formyltransferase
 44-178 1.20e-10

methionyl-tRNA formyltransferase


Pssm-ID: 215159 [Multi-domain]  Cd Length: 334  Bit Score: 59.32  E-value: 1.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922  44 QHAIAAQIPFHLV---DRTLDKTtFAEQLIATVPpetELIVLAGFLSIIPPSLLHhFPR--IINIHPSLLPKFGGAGmyg 118
Cdd:PLN02285  62 QLALDRGFPPDLIftpEKAGEED-FLSALRELQP---DLCITAAYGNILPQKFLD-IPKlgTVNIHPSLLPLYRGAA--- 133

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922 119 lKVHQAvIAAGERESGCTVHWVNQEIDGGAILAQNRVSVFPDDTPEQLQQRILAYEHQLL 178
Cdd:PLN02285 134 -PVQRA-LQDGVNETGVSVAFTVRALDAGPVIAQERVEVDEDIKAPELLPLLFELGTKLL 191
PRK06988 PRK06988
formyltransferase;
87-183 7.06e-10

formyltransferase;


Pssm-ID: 235902 [Multi-domain]  Cd Length: 312  Bit Score: 57.01  E-value: 7.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922  87 SIIPPSLLHHFPR-IINIHPSLLPKFGGAgmygLKVHQAVIAaGERESGCTVHWVNQEIDGGAILAQNRVSVFPDDTPEQ 165
Cdd:PRK06988  88 HMIPVDLLALAPRgAYNMHGSLLPKYRGR----VPVNWAVLN-GETETGATLHEMVAKPDAGAIVDQTAVPILPDDTAAQ 162

                         90       100
                 ....*....|....*....|..
gi 500335922 166 LQQRIL-AYEHQL---LPATIA 183
Cdd:PRK06988 163 VFDKVTvAAEQTLwrvLPALLA 184
FMT_core_like_5 cd08823
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 81-185 4.42e-09

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


Pssm-ID: 187725 [Multi-domain]  Cd Length: 177  Bit Score: 53.60  E-value: 4.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922  81 VLAGFLSIIPPSLLHHFPR-IINIHPSLLPKFGGAGMYGLKvhqavIAAGERESGCTVHWVNQEIDGGAILAQNRVSVFP 159
Cdd:cd08823   76 VVFTFPYRIPQHILDLPPLgFYNLHPGLLPAYRGPDPLFWQ-----IRNQEQETAITVHKMTAEIDRGPIVLEQFTPIHP 150

                         90       100
                 ....*....|....*....|....*.
gi 500335922 160 DDTPEQLQQRILAYEHQLLPATIARL 185
Cdd:cd08823  151 DDTYGLLCSRLAMLAVGLLEELYQNL 176
PRK08125 PRK08125
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ...
 102-185 8.72e-09

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


Pssm-ID: 236156 [Multi-domain]  Cd Length: 660  Bit Score: 54.22  E-value: 8.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922 102 NIHPSLLPKFGGagmyglkvhQA----VIAAGERESGCTVHWVNQEIDGGAILAQNRVSVFPDDTPEQLQQRILAYEHQL 177
Cdd:PRK08125 102 NLHGSLLPKYRG---------RAplnwVLVNGETETGVTLHRMVKRADAGAIVAQQRVAIAPDDTALTLHHKLCHAARQL 172


                 ....*...
gi 500335922 178 LPATIARL 185
Cdd:PRK08125 173 LEQTLPAI 180
FMT_core_like_4 cd08651
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 51-185 4.14e-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: 187720 [Multi-domain]  Cd Length: 180  Bit Score: 50.73  E-value: 4.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922  51 IPFHLVDRTLDKTTfaEQLIATVPPETELIVlaGFLSIIPPSLLHHFPR-IINIHPSLLPKFGGAGmyglKVHQAvIAAG 129
Cdd:cd08651   54 IPYYKFTDINDEEI--IEWIKEANPDIIFVF--GWSQLLKPEILAIPRLgVIGFHPTKLPKNRGRA----PIPWA-ILLG 124

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 500335922 130 ERESGCTVHWVNQEIDGGAILAQNRVSVFPDDTPEQLQQRILAYEHQLLPATIARL 185
Cdd:cd08651  125 LKETASTFFWMDEGADSGDILSQEPFPIDKDDTANSLYDKIMEAAKQQIDKFLPRL 180
FMT_core_FDH_N cd08647
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ...
 78-171 4.99e-07

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


Pssm-ID: 187716 [Multi-domain]  Cd Length: 203  Bit Score: 48.21  E-value: 4.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922  78 ELIVLAGFLSIIPPSLLHHfPRIINI--HPSLLPKFGGAGMYGLKVHQaviaaGERESGCTVHWVNQEIDGGAILAQNRV 155
Cdd:cd08647   79 ELNVLPFCSQFIPMEVIDA-PKHGSIiyHPSILPRHRGASAINWTLIH-----GDKKAGFTIFWADDGLDTGPILLQKEC 152

                         90
                 ....*....|....*.
gi 500335922 156 SVFPDDTPEQLQQRIL 171
Cdd:cd08647  153 DVLPNDTVDTLYNRFL 168
FMT_core_NRPS_like cd08649
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ...
 86-162 8.11e-06

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


Pssm-ID: 187718 [Multi-domain]  Cd Length: 166  Bit Score: 44.17  E-value: 8.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922  86 LSIIPPSLLHhFPRI--INIHPSLLPKFGGagmyglkVHQAVIA--AGERESGCTVHWVNQEIDGGAILAQNRVSVFPDD 161
Cdd:cd08649   71 LRILPSEVLA-LPRKgaINFHDGPLPRYAG-------LNATSWAllAGETRHGVTWHRIEEGVDAGDILVQRPFDIAPDD 142


                 .
gi 500335922 162 T 162
Cdd:cd08649  143 T 143
FMT_core_like_6 cd08820
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 75-177 1.90e-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: 187722 [Multi-domain]  Cd Length: 173  Bit Score: 43.20  E-value: 1.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922  75 PETELIVLAGFLSIIPPSLLHHFPRI-INIHPSLLPKFGGAGMYGLkvhqaVIAAGERESGCTVHWVNQEIDGGAILAQN 153
Cdd:cd08820   68 KGVDILISVQYHWILPGSILEKAKEIaFNLHNAPLPEYRGCNQFSH-----AILNGDDQFGTTIHWMAEGIDSGDIIFEK 142

                         90       100
                 ....*....|....*....|....
gi 500335922 154 RVSVFPDDTPEQLQqrILAYEHQL 177
Cdd:cd08820  143 RFPIPSDCTVISLY--ILAHYAAI 164
PRK07579 PRK07579
dTDP-4-amino-4,6-dideoxyglucose formyltransferase;
91-186 6.98e-04

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


Pssm-ID: 236058 [Multi-domain]  Cd Length: 245  Bit Score: 39.12  E-value: 6.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500335922  91 PSLLHHFPRIINIHPSLLPKfgGAGMYGlkvhQAVIAAGERESGCTVHWVNQEIDGGAILAQNRVSVFPDDTPEQLQQRI 170
Cdd:PRK07579  79 PAKLVNGVRCINIHPGFNPY--NRGWFP----QVFSIINGLKIGATIHEMDEQLDHGPIIAQREVEIESWDSSGSVYARV 152

                         90
                 ....*....|....*.
gi 500335922 171 LAYEHQLLPATIARLF 186
Cdd:PRK07579 153 MDIERELVLEHFDAIR 168
 
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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