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Conserved domains on  [gi|446607765|ref|WP_000685111|]
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MULTISPECIES: phosphoribosylglycinamide formyltransferase [Streptococcus]

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); ...
 2-177 2.60e-90

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: 261.55  E-value: 2.60e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765   2 KIAVFASGNGSNFQIIAEQFP-------VSFVFSDHRDAYVLERAQNLTIPSFAFELKEFENKAAYEQAIVNLLDKHEID 74
Cdd:cd08645    1 RIAVLASGSGSNLQALIDAIKsgklnaeIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765  75 LVCLAGYMKIVGEALLSAYEGRIINIHPAYLPEFPGAHGIEDAWEAGVDQSGVTIHWVDSGVDTGQVIQQVRVPRLADDS 154
Cdd:cd08645   81 LIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDT 160

                        170       180
                 ....*....|....*....|...
gi 446607765 155 LESFETRIHETEYQLYPAVLDSL 177
Cdd:cd08645  161 PETLAERIHALEHRLYPEAIKLL 183
 
Name Accession Description Interval E-value
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 2-177 2.60e-90

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: 261.55  E-value: 2.60e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765   2 KIAVFASGNGSNFQIIAEQFP-------VSFVFSDHRDAYVLERAQNLTIPSFAFELKEFENKAAYEQAIVNLLDKHEID 74
Cdd:cd08645    1 RIAVLASGSGSNLQALIDAIKsgklnaeIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765  75 LVCLAGYMKIVGEALLSAYEGRIINIHPAYLPEFPGAHGIEDAWEAGVDQSGVTIHWVDSGVDTGQVIQQVRVPRLADDS 154
Cdd:cd08645   81 LIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDT 160

                        170       180
                 ....*....|....*....|...
gi 446607765 155 LESFETRIHETEYQLYPAVLDSL 177
Cdd:cd08645  161 PETLAERIHALEHRLYPEAIKLL 183
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 1-174 2.68e-90

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: 262.28  E-value: 2.68e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765   1 MKIAVFASGNGSNFQ-----IIAEQFP--VSFVFSDHRDAYVLERAQNLTIPSFAFELKEFENKAAYEQAIVNLLDKHEI 73
Cdd:COG0299    2 KRIAVLISGRGSNLQalidaIEAGDLPaeIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYGP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765  74 DLVCLAGYMKIVGEALLSAYEGRIINIHPAYLPEFPGAHGIEDAWEAGVDQSGVTIHWVDSGVDTGQVIQQVRVPRLADD 153
Cdd:COG0299   82 DLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDD 161

                        170       180
                 ....*....|....*....|.
gi 446607765 154 SLESFETRIHETEYQLYPAVL 174
Cdd:COG0299  162 TEETLAARILEQEHRLYPEAI 182
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 1-174 9.91e-75

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: 222.63  E-value: 9.91e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765    1 MKIAVFASGNGSNFQIIA-------EQFPVSFVFSDHRDAYVLERAQNLTIPSFAFELKEFENKAAYEQAIVNLLDKHEI 73
Cdd:TIGR00639   1 KRIVVLISGNGSNLQAIIdackegkIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765   74 DLVCLAGYMKIVGEALLSAYEGRIINIHPAYLPEFPGAHGIEDAWEAGVDQSGVTIHWVDSGVDTGQVIQQVRVPRLADD 153
Cdd:TIGR00639  81 DLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPED 160

                         170       180
                  ....*....|....*....|.
gi 446607765  154 SLESFETRIHETEYQLYPAVL 174
Cdd:TIGR00639 161 TEETLEQRIHKQEHRIYPLAI 181
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 1-174 2.63e-64

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: 195.59  E-value: 2.63e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765    1 MKIAVFASGNGSNFQIIAEQ-------FPVSFVFSDHRDAYVLERAQNLTIPSFAFELKEFENKAAYEQAIVNLLDKHEI 73
Cdd:pfam00551   1 MKIAVLISGTGSNLQALIDAlrkggqdADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765   74 DLVCLAGYMKIVGEALLSAYEGRIINIHPAYLPEFPGAHGIEDAWEAGVDQSGVTIHWVDSGVDTGQVIQQVRVPRLADD 153
Cdd:pfam00551  81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160

                         170       180
                  ....*....|....*....|.
gi 446607765  154 SLESFETRIHETEYQLYPAVL 174
Cdd:pfam00551 161 TAETLYNRVADLEHKALPRVL 181
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 2-177 7.88e-33

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 116.33  E-value: 7.88e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765   2 KIAVFASGNGSNFQIIAEQF-------PVSFVFSDHRDAYVLERAQNLTIPSFAFELKEFENKAAYEQAIVNLLDKHEID 74
Cdd:PLN02331   1 KLAVFVSGGGSNFRAIHDACldgrvngDVVVVVTNKPGCGGAEYARENGIPVLVYPKTKGEPDGLSPDELVDALRGAGVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765  75 LVCLAGYMKIVGEALLSAYEGRIINIHPAYLPEF--PGAHGI---EDAWEAGVDQSGVTIHWVDSGVDTGQVIQQVRVPR 149
Cdd:PLN02331  81 FVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFggKGYYGIkvhKAVIASGARYSGPTVHFVDEHYDTGRILAQRVVPV 160

                        170       180
                 ....*....|....*....|....*...
gi 446607765 150 LADDSLESFETRIHETEYQLYPAVLDSL 177
Cdd:PLN02331 161 LATDTPEELAARVLHEEHQLYVEVVAAL 188
 
Name Accession Description Interval E-value
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 2-177 2.60e-90

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: 261.55  E-value: 2.60e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765   2 KIAVFASGNGSNFQIIAEQFP-------VSFVFSDHRDAYVLERAQNLTIPSFAFELKEFENKAAYEQAIVNLLDKHEID 74
Cdd:cd08645    1 RIAVLASGSGSNLQALIDAIKsgklnaeIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765  75 LVCLAGYMKIVGEALLSAYEGRIINIHPAYLPEFPGAHGIEDAWEAGVDQSGVTIHWVDSGVDTGQVIQQVRVPRLADDS 154
Cdd:cd08645   81 LIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDT 160

                        170       180
                 ....*....|....*....|...
gi 446607765 155 LESFETRIHETEYQLYPAVLDSL 177
Cdd:cd08645  161 PETLAERIHALEHRLYPEAIKLL 183
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 1-174 2.68e-90

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: 262.28  E-value: 2.68e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765   1 MKIAVFASGNGSNFQ-----IIAEQFP--VSFVFSDHRDAYVLERAQNLTIPSFAFELKEFENKAAYEQAIVNLLDKHEI 73
Cdd:COG0299    2 KRIAVLISGRGSNLQalidaIEAGDLPaeIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYGP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765  74 DLVCLAGYMKIVGEALLSAYEGRIINIHPAYLPEFPGAHGIEDAWEAGVDQSGVTIHWVDSGVDTGQVIQQVRVPRLADD 153
Cdd:COG0299   82 DLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDD 161

                        170       180
                 ....*....|....*....|.
gi 446607765 154 SLESFETRIHETEYQLYPAVL 174
Cdd:COG0299  162 TEETLAARILEQEHRLYPEAI 182
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 1-174 9.91e-75

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: 222.63  E-value: 9.91e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765    1 MKIAVFASGNGSNFQIIA-------EQFPVSFVFSDHRDAYVLERAQNLTIPSFAFELKEFENKAAYEQAIVNLLDKHEI 73
Cdd:TIGR00639   1 KRIVVLISGNGSNLQAIIdackegkIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765   74 DLVCLAGYMKIVGEALLSAYEGRIINIHPAYLPEFPGAHGIEDAWEAGVDQSGVTIHWVDSGVDTGQVIQQVRVPRLADD 153
Cdd:TIGR00639  81 DLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPED 160

                         170       180
                  ....*....|....*....|.
gi 446607765  154 SLESFETRIHETEYQLYPAVL 174
Cdd:TIGR00639 161 TEETLEQRIHKQEHRIYPLAI 181
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 1-174 2.63e-64

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: 195.59  E-value: 2.63e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765    1 MKIAVFASGNGSNFQIIAEQ-------FPVSFVFSDHRDAYVLERAQNLTIPSFAFELKEFENKAAYEQAIVNLLDKHEI 73
Cdd:pfam00551   1 MKIAVLISGTGSNLQALIDAlrkggqdADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765   74 DLVCLAGYMKIVGEALLSAYEGRIINIHPAYLPEFPGAHGIEDAWEAGVDQSGVTIHWVDSGVDTGQVIQQVRVPRLADD 153
Cdd:pfam00551  81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160

                         170       180
                  ....*....|....*....|.
gi 446607765  154 SLESFETRIHETEYQLYPAVL 174
Cdd:pfam00551 161 TAETLYNRVADLEHKALPRVL 181
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 2-177 7.88e-33

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 116.33  E-value: 7.88e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765   2 KIAVFASGNGSNFQIIAEQF-------PVSFVFSDHRDAYVLERAQNLTIPSFAFELKEFENKAAYEQAIVNLLDKHEID 74
Cdd:PLN02331   1 KLAVFVSGGGSNFRAIHDACldgrvngDVVVVVTNKPGCGGAEYARENGIPVLVYPKTKGEPDGLSPDELVDALRGAGVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765  75 LVCLAGYMKIVGEALLSAYEGRIINIHPAYLPEF--PGAHGI---EDAWEAGVDQSGVTIHWVDSGVDTGQVIQQVRVPR 149
Cdd:PLN02331  81 FVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFggKGYYGIkvhKAVIASGARYSGPTVHFVDEHYDTGRILAQRVVPV 160

                        170       180
                 ....*....|....*....|....*...
gi 446607765 150 LADDSLESFETRIHETEYQLYPAVLDSL 177
Cdd:PLN02331 161 LATDTPEELAARVLHEEHQLYVEVVAAL 188
FMT_core cd08369
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...
 3-176 1.68e-29

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: 106.60  E-value: 1.68e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765   3 IAVFasGNGSNFQIIAEQF------PVSFVFSDHRDAYVLERAQNLTIPSfafelKEFENKAAYEQAIVNLLDKHEIDLV 76
Cdd:cd08369    1 IVIL--GSGNIGQRVLKALlskeghEIVGVVTHPDSPRGTAQLSLELVGG-----KVYLDSNINTPELLELLKEFAPDLI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765  77 CLAGYMKIVGEALLSAYEGRIINIHPAYLPEFPGAHGIEDAWEAGVDQSGVTIHWVDSGVDTGQVIQQVRVPRLADDSLE 156
Cdd:cd08369   74 VSINFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTAG 153

                        170       180
                 ....*....|....*....|
gi 446607765 157 SFETRIHETEYQLYPAVLDS 176
Cdd:cd08369  154 TLYQRLIELGPKLLKEALQK 173
FMT_core_Formyl-FH4-Hydrolase_C cd08648
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ...
 23-158 7.01e-26

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: 98.02  E-value: 7.01e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765  23 VSFVFSDHRDAYVLerAQNLTIPSFAFELKEfENKAAYEQAIVNLLDKHEIDLVCLAGYMKIVGEALLSAYEGRIINIHP 102
Cdd:cd08648   30 IPLVISNHPDLRPL--AERFGIPFHHIPVTK-DTKAEAEAEQLELLEEYGVDLVVLARYMQILSPDFVERYPNRIINIHH 106

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446607765 103 AYLPEFPGAHGIEDAWEAGVDQSGVTIHWVDSGVDTGQVIQQVRVPRLADDSLESF 158
Cdd:cd08648  107 SFLPAFKGAKPYHQAFERGVKLIGATAHYVTEELDEGPIIEQDVERVSHRDSVEDL 162
PurU COG0788
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ...
 55-148 6.58e-24

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: 94.73  E-value: 6.58e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765  55 ENKAAYEQAIVNLLDKHEIDLVCLAGYMKIVGEALLSAYEGRIINIHPAYLPEFPGAHGIEDAWEAGVDQSGVTIHWVDS 134
Cdd:COG0788  145 ETKAEAEARLLELLEEYDIDLVVLARYMQILSPDFCARLPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTA 224

                         90
                 ....*....|....*.
gi 446607765 135 GVDTGQVIQQ--VRVP 148
Cdd:COG0788  225 DLDEGPIIEQdvERVD 240
purU PRK06027
formyltetrahydrofolate deformylase; Reviewed
 26-147 3.31e-20

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 235676 [Multi-domain]  Cd Length: 286  Bit Score: 85.16  E-value: 3.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765  26 VFSDHRDAYVLerAQNLTIPSFAFELkEFENKAAYEQAIVNLLDKHEIDLVCLAGYMKIVGEALLSAYEGRIINIHPAYL 105
Cdd:PRK06027 122 VISNHDDLRSL--VERFGIPFHHVPV-TKETKAEAEARLLELIDEYQPDLVVLARYMQILSPDFVARFPGRIINIHHSFL 198

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 446607765 106 PEFPGAHGIEDAWEAGVDQSGVTIHWVDSGVDTGQVIQQ--VRV 147
Cdd:PRK06027 199 PAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQdvIRV 242
FMT_core_like_3 cd08653
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 74-177 1.24e-19

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


Pssm-ID: 187721 [Multi-domain]  Cd Length: 152  Bit Score: 80.72  E-value: 1.24e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765  74 DLVCLAGyMKIVGEALLSAYEGRIINIHPAYLPEFPGAHGIEDA-WEAGVDQSGVTIHWVDSGVDTGQVIQQVRVPRLAD 152
Cdd:cd08653   49 DVVSVYG-CGIIKDALLAIPPLGVLNLHGGILPDYRGVHTGFWAlANGDPDNVGVTVHLVDAGIDTGDVLAQARPPLAAG 127

                         90       100
                 ....*....|....*....|....*
gi 446607765 153 DSLESFETRIHETEYQLYPAVLDSL 177
Cdd:cd08653  128 DTLLSLYLRLYRAGVELMVEAIADL 152
PRK13011 PRK13011
formyltetrahydrofolate deformylase; Reviewed
 26-145 2.34e-18

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 237266 [Multi-domain]  Cd Length: 286  Bit Score: 80.03  E-value: 2.34e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765  26 VFSDHRDAYVLerAQNLTIPSFAFELKEfENKAAYEQAIVNLLDKHEIDLVCLAGYMKIVGEALLSAYEGRIINIHPAYL 105
Cdd:PRK13011 122 VVSNHPDLEPL--AAWHGIPFHHFPITP-DTKPQQEAQVLDVVEESGAELVVLARYMQVLSPELCRKLAGRAINIHHSFL 198

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446607765 106 PEFPGAHGIEDAWEAGVDQSGVTIHWVDSGVDTGQVIQQV 145
Cdd:PRK13011 199 PGFKGAKPYHQAYERGVKLIGATAHYVTDDLDEGPIIEQD 238
purU PRK13010
formyltetrahydrofolate deformylase; Reviewed
 26-145 3.30e-17

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 139334 [Multi-domain]  Cd Length: 289  Bit Score: 77.14  E-value: 3.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765  26 VFSDHRDAyvLERAQNLTIPSFAFELKEfENKAAYEQAIVNLLDKHEIDLVCLAGYMKIVGEALLSAYEGRIINIHPAYL 105
Cdd:PRK13010 126 IISNHPDL--QPLAVQHDIPFHHLPVTP-DTKAQQEAQILDLIETSGAELVVLARYMQVLSDDLSRKLSGRAINIHHSFL 202

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446607765 106 PEFPGAHGIEDAWEAGVDQSGVTIHWVDSGVDTGQVIQQV 145
Cdd:PRK13010 203 PGFKGARPYHQAHARGVKLIGATAHFVTDDLDEGPIIEQD 242
PLN02828 PLN02828
formyltetrahydrofolate deformylase
 55-168 2.13e-16

formyltetrahydrofolate deformylase


Pssm-ID: 178422  Cd Length: 268  Bit Score: 74.40  E-value: 2.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765  55 ENKAayEQAIVNLLdkHEIDLVCLAGYMKIVGEALLSAYEGRIINIHPAYLPEFPGAHGIEDAWEAGVDQSGVTIHWVDS 134
Cdd:PLN02828 134 ENKR--EDEILELV--KGTDFLVLARYMQILSGNFLKGYGKDIINIHHGLLPSFKGGNPSKQAFDAGVKLIGATSHFVTE 209

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446607765 135 GVDTGQVIQQVrVPRLAD-DSLESFETRIHETEYQ 168
Cdd:PLN02828 210 ELDAGPIIEQM-VERVSHrDNLRSFVQKSENLEKQ 243
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
1-177 4.29e-15

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


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 71.29  E-value: 4.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765   1 MKIAVFASgngSNF------QIIAEQFPVSFVFSdHRDAY-----------VLERAQNLTIPSFAFE-LKEfenkaayeQ 62
Cdd:COG0223    1 MRIVFMGT---PDFavpsleALLAAGHEVVAVVT-QPDRPagrgrkltpspVKELALEHGIPVLQPEsLKD--------P 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765  63 AIVNLLDKHEIDLVCLAGYMKIVGEALLSAYEGRIINIHPAYLPEFPGAHGIEDAWEAGVDQSGVTIHWVDSGVDTGQVI 142
Cdd:COG0223   69 EFLEELRALNPDLIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDTGDIL 148

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 446607765 143 QQVRVPRLADDSLESFETRIHETEYQLYPAVLDSL 177
Cdd:COG0223  149 LQEEVPIGPDDTAGSLHDKLAELGAELLLETLDAL 183
FMT_core_like_4 cd08651
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 62-177 8.81e-14

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: 65.75  E-value: 8.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765  62 QAIVNLLDKHEIDLVCLAGYMKIVGEALLSAYEGRIINIHPAYLPEFPGAHGIEDAWEAGVDQSGVTIHWVDSGVDTGQV 141
Cdd:cd08651   65 EEIIEWIKEANPDIIFVFGWSQLLKPEILAIPRLGVIGFHPTKLPKNRGRAPIPWAILLGLKETASTFFWMDEGADSGDI 144

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446607765 142 IQQVRVPRLADDSLESFETRIHETEYQLYPAVLDSL 177
Cdd:cd08651  145 LSQEPFPIDKDDTANSLYDKIMEAAKQQIDKFLPRL 180
FMT_core_Met-tRNA-FMT_N cd08646
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ...
 37-157 2.06e-11

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: 59.76  E-value: 2.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765  37 ERAQNLTIPSFAFE-LKEFEnkaayeqaIVNLLDKHEIDLVCLAGYMKIVGEALLSAYEGRIINIHPAYLPEFPGAHGIE 115
Cdd:cd08646   50 ELALELGLPVLQPEkLKDEE--------FLEELKALKPDLIVVVAYGQILPKEILDLPPYGCINVHPSLLPKYRGAAPIQ 121

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446607765 116 DAWEAGVDQSGVTIHWVDSGVDTGQVIQQVRVPRLADDSLES 157
Cdd:cd08646  122 RAILNGDKETGVTIMKMDEGLDTGDILAQEEVPIDPDDTAGE 163
fmt TIGR00460
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ...
 38-153 4.79e-10

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: 57.03  E-value: 4.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765   38 RAQNLTIP---SFAFE--LKEFENKAAYEQAIVNLLDKHEIDLVCLAGYMKIVGEALLSAYEGRIINIHPAYLPEFPGAH 112
Cdd:TIGR00460  39 RGKKLTPPpvkVLAEEkgIPVFQPEKQRQLEELPLVRELKPDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGA 118

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 446607765  113 GIEDAWEAGVDQSGVTIHWVDSGVDTGQVIQQVRVPRLADD 153
Cdd:TIGR00460 119 PIQRAILNGDKKTGVTIMQMVPKMDAGDILKQETFPIEEED 159
FMT_core_like_6 cd08820
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 45-157 1.17e-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: 187722 [Multi-domain]  Cd Length: 173  Bit Score: 54.75  E-value: 1.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765  45 PSFAFELKEFENKAAYE----QAIVNLLDKHEIDLVCLAGYMKIVGEALLSAYEGRIINIHPAYLPEFPGAHGIEDAWEA 120
Cdd:cd08820   38 PADVWEGSEPLYDIGSTernlHKLLEILENKGVDILISVQYHWILPGSILEKAKEIAFNLHNAPLPEYRGCNQFSHAILN 117

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446607765 121 GVDQSGVTIHWVDSGVDTGQVIQQVRVPRLADDSLES 157
Cdd:cd08820  118 GDDQFGTTIHWMAEGIDSGDIIFEKRFPIPSDCTVIS 154
PLN02285 PLN02285
methionyl-tRNA formyltransferase
 35-175 7.23e-09

methionyl-tRNA formyltransferase


Pssm-ID: 215159 [Multi-domain]  Cd Length: 334  Bit Score: 53.93  E-value: 7.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765  35 VLERAQNLTIPSFAFelkeFENKAAYEQAIVNLLDKHEIDLVCLAGYMKIVGEALLSAYEGRIINIHPAYLPEFPGAHGI 114
Cdd:PLN02285  60 VAQLALDRGFPPDLI----FTPEKAGEEDFLSALRELQPDLCITAAYGNILPQKFLDIPKLGTVNIHPSLLPLYRGAAPV 135

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446607765 115 EDAWEAGVDQSGVTIHWVDSGVDTGQVIQQVRVPRLADDSLESFETRIHETEYQL----YPAVLD 175
Cdd:PLN02285 136 QRALQDGVNETGVSVAFTVRALDAGPVIAQERVEVDEDIKAPELLPLLFELGTKLllreLPSVLD 200
FMT_core_NRPS_like cd08649
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ...
 67-177 1.73e-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: 45.71  E-value: 1.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765  67 LLDKHEIDLVCLAGYMKIVGEALLSAYEGRIINIHPAYLPEFPGAHGIEDAWEAGVDQSGVTIHWVDSGVDTGQVIQQVR 146
Cdd:cd08649   56 LLSDEPFDWLFSIVNLRILPSEVLALPRKGAINFHDGPLPRYAGLNATSWALLAGETRHGVTWHRIEEGVDAGDILVQRP 135

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446607765 147 VPRLADDSLESFETRIHETEYQLYPAVLDSL 177
Cdd:cd08649  136 FDIAPDDTALSLNLKCYEAGIEGFGELIDEL 166
FMT_core_like_5 cd08823
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 18-162 1.78e-06

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


Pssm-ID: 187725 [Multi-domain]  Cd Length: 177  Bit Score: 45.90  E-value: 1.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765  18 AEQFPVSFVFSdhrdayVLERAQNLTIPSFAFELKEFenkAAYEQAIvnlldkhEIDLVCLAGYMKIVGEALLSAYEGRI 97
Cdd:cd08823   33 ASYFPQIFVFT------GIRRLVSKQRVDTANLKEQL---AEWLRAL-------AADTVVVFTFPYRIPQHILDLPPLGF 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446607765  98 INIHPAYLPEFPGAHGIEDAWEAGVDQSGVTIHWVDSGVDTGQVIQQVRVPRLADDSLESFETRI 162
Cdd:cd08823   97 YNLHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMTAEIDRGPIVLEQFTPIHPDDTYGLLCSRL 161
FMT_core_FDH_N cd08647
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ...
 95-180 3.61e-06

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


Pssm-ID: 187716 [Multi-domain]  Cd Length: 203  Bit Score: 45.52  E-value: 3.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765  95 GRIInIHPAYLPEFPGAHGIEDAWEAGVDQSGVTIHWVDSGVDTGQVIQQVRVPRLADDSLESFETRIheteyqLYPAvl 174
Cdd:cd08647  101 GSII-YHPSILPRHRGASAINWTLIHGDKKAGFTIFWADDGLDTGPILLQKECDVLPNDTVDTLYNRF------LYPE-- 171


                 ....*.
gi 446607765 175 dslGIK 180
Cdd:cd08647  172 ---GIK 174
PRK07579 PRK07579
dTDP-4-amino-4,6-dideoxyglucose formyltransferase;
96-177 3.56e-04

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


Pssm-ID: 236058 [Multi-domain]  Cd Length: 245  Bit Score: 39.89  E-value: 3.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607765  96 RIINIHPAYLPE----FPGAHGIEDAWeagvdQSGVTIHWVDSGVDTGQVIQQVRVPRLADDSLESFETRIHETEYQLYP 171
Cdd:PRK07579  87 RCINIHPGFNPYnrgwFPQVFSIINGL-----KIGATIHEMDEQLDHGPIIAQREVEIESWDSSGSVYARVMDIERELVL 161


                 ....*.
gi 446607765 172 AVLDSL 177
Cdd:PRK07579 162 EHFDAI 167
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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