NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1080615070|gb|OFN91006|]
View 

phosphoribosylglycinamide formyltransferase [Streptococcus sp. HMSC074F05]

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 4-179 3.72e-91

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: 263.86  E-value: 3.72e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070   4 RIAVFASGNGSNFQVIAEQFP-------VEFVFSDHRDAYVLERAKNLGVVSHAFELKEFDNKAAYEEAIVHLLNEHQID 76
Cdd:cd08645     1 RIAVLASGSGSNLQALIDAIKsgklnaeIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKVD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070  77 LVCLAGYMKIVGPTLLAAYEGRIINIHPAYLPEFPGAHGIEDAWNAGVAESGVTIHWVDSGVDTGKVIKQVRVPRLESDT 156
Cdd:cd08645    81 LIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDT 160

                         170       180
                  ....*....|....*....|...
gi 1080615070 157 LDTFETRIHETEYKLYPEVLERL 179
Cdd:cd08645   161 PETLAERIHALEHRLYPEAIKLL 183
 
Name Accession Description Interval E-value
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 4-179 3.72e-91

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: 263.86  E-value: 3.72e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070   4 RIAVFASGNGSNFQVIAEQFP-------VEFVFSDHRDAYVLERAKNLGVVSHAFELKEFDNKAAYEEAIVHLLNEHQID 76
Cdd:cd08645     1 RIAVLASGSGSNLQALIDAIKsgklnaeIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKVD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070  77 LVCLAGYMKIVGPTLLAAYEGRIINIHPAYLPEFPGAHGIEDAWNAGVAESGVTIHWVDSGVDTGKVIKQVRVPRLESDT 156
Cdd:cd08645    81 LIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDT 160

                         170       180
                  ....*....|....*....|...
gi 1080615070 157 LDTFETRIHETEYKLYPEVLERL 179
Cdd:cd08645   161 PETLAERIHALEHRLYPEAIKLL 183
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 3-179 3.96e-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: 261.89  E-value: 3.96e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070   3 KRIAVFASGNGSNFQVIAE-----QFPVE--FVFSDHRDAYVLERAKNLGVVSHAFELKEFDNKAAYEEAIVHLLNEHQI 75
Cdd:COG0299     2 KRIAVLISGRGSNLQALIDaieagDLPAEivLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYGP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070  76 DLVCLAGYMKIVGPTLLAAYEGRIINIHPAYLPEFPGAHGIEDAWNAGVAESGVTIHWVDSGVDTGKVIKQVRVPRLESD 155
Cdd:COG0299    82 DLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDD 161

                         170       180
                  ....*....|....*....|....
gi 1080615070 156 TLDTFETRIHETEYKLYPEVLERL 179
Cdd:COG0299   162 TEETLAARILEQEHRLYPEAIRLL 185
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 3-179 9.28e-74

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: 219.94  E-value: 9.28e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070   3 KRIAVFASGNGSNFQVIA-------EQFPVEFVFSDHRDAYVLERAKNLGVVSHAFELKEFDNKAAYEEAIVHLLNEHQI 75
Cdd:TIGR00639   1 KRIVVLISGNGSNLQAIIdackegkIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070  76 DLVCLAGYMKIVGPTLLAAYEGRIINIHPAYLPEFPGAHGIEDAWNAGVAESGVTIHWVDSGVDTGKVIKQVRVPRLESD 155
Cdd:TIGR00639  81 DLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPED 160

                         170       180
                  ....*....|....*....|....
gi 1080615070 156 TLDTFETRIHETEYKLYPEVLERL 179
Cdd:TIGR00639 161 TEETLEQRIHKQEHRIYPLAIAWF 184
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 3-176 2.49e-62

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: 190.58  E-value: 2.49e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070   3 KRIAVFASGNGSNFQVIAEQ-------FPVEFVFSDHRDAYVLERAKNLGVVSHAFELKEFDNKAAYEEAIVHLLNEHQI 75
Cdd:pfam00551   1 MKIAVLISGTGSNLQALIDAlrkggqdADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070  76 DLVCLAGYMKIVGPTLLAAYEGRIINIHPAYLPEFPGAHGIEDAWNAGVAESGVTIHWVDSGVDTGKVIKQVRVPRLESD 155
Cdd:pfam00551  81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160

                         170       180
                  ....*....|....*....|.
gi 1080615070 156 TLDTFETRIHETEYKLYPEVL 176
Cdd:pfam00551 161 TAETLYNRVADLEHKALPRVL 181
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 4-179 1.48e-30

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 110.55  E-value: 1.48e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070   4 RIAVFASGNGSNFQVIAEQF-------PVEFVFSDHRDAYVLERAKNLGVVSHAFELKEFDNKAAYEEAIVHLLNEHQID 76
Cdd:PLN02331    1 KLAVFVSGGGSNFRAIHDACldgrvngDVVVVVTNKPGCGGAEYARENGIPVLVYPKTKGEPDGLSPDELVDALRGAGVD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070  77 LVCLAGYMKIVGPTLLAAYEGRIINIHPAYLPEF--PGAHGI---EDAWNAGVAESGVTIHWVDSGVDTGKVIKQVRVPR 151
Cdd:PLN02331   81 FVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFggKGYYGIkvhKAVIASGARYSGPTVHFVDEHYDTGRILAQRVVPV 160

                         170       180
                  ....*....|....*....|....*...
gi 1080615070 152 LESDTLDTFETRIHETEYKLYPEVLERL 179
Cdd:PLN02331  161 LATDTPEELAARVLHEEHQLYVEVVAAL 188
 
Name Accession Description Interval E-value
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 4-179 3.72e-91

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: 263.86  E-value: 3.72e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070   4 RIAVFASGNGSNFQVIAEQFP-------VEFVFSDHRDAYVLERAKNLGVVSHAFELKEFDNKAAYEEAIVHLLNEHQID 76
Cdd:cd08645     1 RIAVLASGSGSNLQALIDAIKsgklnaeIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKVD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070  77 LVCLAGYMKIVGPTLLAAYEGRIINIHPAYLPEFPGAHGIEDAWNAGVAESGVTIHWVDSGVDTGKVIKQVRVPRLESDT 156
Cdd:cd08645    81 LIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDT 160

                         170       180
                  ....*....|....*....|...
gi 1080615070 157 LDTFETRIHETEYKLYPEVLERL 179
Cdd:cd08645   161 PETLAERIHALEHRLYPEAIKLL 183
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 3-179 3.96e-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: 261.89  E-value: 3.96e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070   3 KRIAVFASGNGSNFQVIAE-----QFPVE--FVFSDHRDAYVLERAKNLGVVSHAFELKEFDNKAAYEEAIVHLLNEHQI 75
Cdd:COG0299     2 KRIAVLISGRGSNLQALIDaieagDLPAEivLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYGP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070  76 DLVCLAGYMKIVGPTLLAAYEGRIINIHPAYLPEFPGAHGIEDAWNAGVAESGVTIHWVDSGVDTGKVIKQVRVPRLESD 155
Cdd:COG0299    82 DLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDD 161

                         170       180
                  ....*....|....*....|....
gi 1080615070 156 TLDTFETRIHETEYKLYPEVLERL 179
Cdd:COG0299   162 TEETLAARILEQEHRLYPEAIRLL 185
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 3-179 9.28e-74

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: 219.94  E-value: 9.28e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070   3 KRIAVFASGNGSNFQVIA-------EQFPVEFVFSDHRDAYVLERAKNLGVVSHAFELKEFDNKAAYEEAIVHLLNEHQI 75
Cdd:TIGR00639   1 KRIVVLISGNGSNLQAIIdackegkIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070  76 DLVCLAGYMKIVGPTLLAAYEGRIINIHPAYLPEFPGAHGIEDAWNAGVAESGVTIHWVDSGVDTGKVIKQVRVPRLESD 155
Cdd:TIGR00639  81 DLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPED 160

                         170       180
                  ....*....|....*....|....
gi 1080615070 156 TLDTFETRIHETEYKLYPEVLERL 179
Cdd:TIGR00639 161 TEETLEQRIHKQEHRIYPLAIAWF 184
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 3-176 2.49e-62

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: 190.58  E-value: 2.49e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070   3 KRIAVFASGNGSNFQVIAEQ-------FPVEFVFSDHRDAYVLERAKNLGVVSHAFELKEFDNKAAYEEAIVHLLNEHQI 75
Cdd:pfam00551   1 MKIAVLISGTGSNLQALIDAlrkggqdADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070  76 DLVCLAGYMKIVGPTLLAAYEGRIINIHPAYLPEFPGAHGIEDAWNAGVAESGVTIHWVDSGVDTGKVIKQVRVPRLESD 155
Cdd:pfam00551  81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160

                         170       180
                  ....*....|....*....|.
gi 1080615070 156 TLDTFETRIHETEYKLYPEVL 176
Cdd:pfam00551 161 TAETLYNRVADLEHKALPRVL 181
FMT_core cd08369
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...
 5-178 4.78e-31

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: 110.84  E-value: 4.78e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070   5 IAVFASGNgSNFQVI-----AEQFPVEFVFSDHRDAYVLERAKNLGVVShafelKEFDNKAAYEEAIVHLLNEHQIDLVC 79
Cdd:cd08369     1 IVILGSGN-IGQRVLkallsKEGHEIVGVVTHPDSPRGTAQLSLELVGG-----KVYLDSNINTPELLELLKEFAPDLIV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070  80 LAGYMKIVGPTLLAAYEGRIINIHPAYLPEFPGAHGIEDAWNAGVAESGVTIHWVDSGVDTGKVIKQVRVPRLESDTLDT 159
Cdd:cd08369    75 SINFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTAGT 154

                         170
                  ....*....|....*....
gi 1080615070 160 FETRIHETEYKLYPEVLER 178
Cdd:cd08369   155 LYQRLIELGPKLLKEALQK 173
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 4-179 1.48e-30

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 110.55  E-value: 1.48e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070   4 RIAVFASGNGSNFQVIAEQF-------PVEFVFSDHRDAYVLERAKNLGVVSHAFELKEFDNKAAYEEAIVHLLNEHQID 76
Cdd:PLN02331    1 KLAVFVSGGGSNFRAIHDACldgrvngDVVVVVTNKPGCGGAEYARENGIPVLVYPKTKGEPDGLSPDELVDALRGAGVD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070  77 LVCLAGYMKIVGPTLLAAYEGRIINIHPAYLPEF--PGAHGI---EDAWNAGVAESGVTIHWVDSGVDTGKVIKQVRVPR 151
Cdd:PLN02331   81 FVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFggKGYYGIkvhKAVIASGARYSGPTVHFVDEHYDTGRILAQRVVPV 160

                         170       180
                  ....*....|....*....|....*...
gi 1080615070 152 LESDTLDTFETRIHETEYKLYPEVLERL 179
Cdd:PLN02331  161 LATDTPEELAARVLHEEHQLYVEVVAAL 188
FMT_core_Formyl-FH4-Hydrolase_C cd08648
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ...
 57-160 1.53e-25

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: 97.25  E-value: 1.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070  57 DNKAAYEEAIVHLLNEHQIDLVCLAGYMKIVGPTLLAAYEGRIINIHPAYLPEFPGAHGIEDAWNAGVAESGVTIHWVDS 136
Cdd:cd08648    59 DTKAEAEAEQLELLEEYGVDLVVLARYMQILSPDFVERYPNRIINIHHSFLPAFKGAKPYHQAFERGVKLIGATAHYVTE 138

                          90       100
                  ....*....|....*....|....
gi 1080615070 137 GVDTGKVIKQVRVPRLESDTLDTF 160
Cdd:cd08648   139 ELDEGPIIEQDVERVSHRDSVEDL 162
PurU COG0788
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ...
 57-150 8.02e-22

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: 89.34  E-value: 8.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070  57 DNKAAYEEAIVHLLNEHQIDLVCLAGYMKIVGPTLLAAYEGRIINIHPAYLPEFPGAHGIEDAWNAGVAESGVTIHWVDS 136
Cdd:COG0788   145 ETKAEAEARLLELLEEYDIDLVVLARYMQILSPDFCARLPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTA 224

                          90
                  ....*....|....*.
gi 1080615070 137 GVDTGKVIKQ--VRVP 150
Cdd:COG0788   225 DLDEGPIIEQdvERVD 240
purU PRK06027
formyltetrahydrofolate deformylase; Reviewed
 22-149 5.46e-21

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 235676 [Multi-domain]  Cd Length: 286  Bit Score: 87.08  E-value: 5.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070  22 QFPVEF--VFSDHRDAYVLerAKNLGV----VSHafelkEFDNKAAYEEAIVHLLNEHQIDLVCLAGYMKIVGPTLLAAY 95
Cdd:PRK06027  114 ELPVEIaaVISNHDDLRSL--VERFGIpfhhVPV-----TKETKAEAEARLLELIDEYQPDLVVLARYMQILSPDFVARF 186

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1080615070  96 EGRIINIHPAYLPEFPGAHGIEDAWNAGVAESGVTIHWVDSGVDTGKVIKQ--VRV 149
Cdd:PRK06027  187 PGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQdvIRV 242
PRK13011 PRK13011
formyltetrahydrofolate deformylase; Reviewed
 28-147 3.47e-19

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 237266 [Multi-domain]  Cd Length: 286  Bit Score: 82.34  E-value: 3.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070  28 VFSDHRDAYVLerAKNLGVVSHAFELKEfDNKAAYEEAIVHLLNEHQIDLVCLAGYMKIVGPTLLAAYEGRIINIHPAYL 107
Cdd:PRK13011  122 VVSNHPDLEPL--AAWHGIPFHHFPITP-DTKPQQEAQVLDVVEESGAELVVLARYMQVLSPELCRKLAGRAINIHHSFL 198

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1080615070 108 PEFPGAHGIEDAWNAGVAESGVTIHWVDSGVDTGKVIKQV 147
Cdd:PRK13011  199 PGFKGAKPYHQAYERGVKLIGATAHYVTDDLDEGPIIEQD 238
FMT_core_like_3 cd08653
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 63-179 9.66e-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: 78.41  E-value: 9.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070  63 EEAIVHLLNEHQIDLVCLAGyMKIVGPTLLAAYEGRIINIHPAYLPEFPGAHGIEDA-WNAGVAESGVTIHWVDSGVDTG 141
Cdd:cd08653    36 GPEVVAALRALAPDVVSVYG-CGIIKDALLAIPPLGVLNLHGGILPDYRGVHTGFWAlANGDPDNVGVTVHLVDAGIDTG 114

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1080615070 142 KVIKQVRVPRLESDTLDTFETRIHETEYKLYPEVLERL 179
Cdd:cd08653   115 DVLAQARPPLAAGDTLLSLYLRLYRAGVELMVEAIADL 152
FMT_core_like_4 cd08651
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 63-179 8.73e-17

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: 73.84  E-value: 8.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070  63 EEAIVhLLNEHQIDLVCLAGYMKIVGPTLLAAYEGRIINIHPAYLPEFPGAHGIedAWN--AGVAESGVTIHWVDSGVDT 140
Cdd:cd08651    65 EEIIE-WIKEANPDIIFVFGWSQLLKPEILAIPRLGVIGFHPTKLPKNRGRAPI--PWAilLGLKETASTFFWMDEGADS 141

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1080615070 141 GKVIKQVRVPRLESDTLDTFETRIHETEYKLYPEVLERL 179
Cdd:cd08651   142 GDILSQEPFPIDKDDTANSLYDKIMEAAKQQIDKFLPRL 180
purU PRK13010
formyltetrahydrofolate deformylase; Reviewed
 28-147 1.98e-16

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 139334 [Multi-domain]  Cd Length: 289  Bit Score: 74.83  E-value: 1.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070  28 VFSDHRDAyvLERAKNLGVVSHAFELKEfDNKAAYEEAIVHLLNEHQIDLVCLAGYMKIVGPTLLAAYEGRIINIHPAYL 107
Cdd:PRK13010  126 IISNHPDL--QPLAVQHDIPFHHLPVTP-DTKAQQEAQILDLIETSGAELVVLARYMQVLSDDLSRKLSGRAINIHHSFL 202

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1080615070 108 PEFPGAHGIEDAWNAGVAESGVTIHWVDSGVDTGKVIKQV 147
Cdd:PRK13010  203 PGFKGARPYHQAHARGVKLIGATAHFVTDDLDEGPIIEQD 242
PLN02828 PLN02828
formyltetrahydrofolate deformylase
 63-183 4.38e-16

formyltetrahydrofolate deformylase


Pssm-ID: 178422  Cd Length: 268  Bit Score: 73.63  E-value: 4.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070  63 EEAIVHLLNEhqIDLVCLAGYMKIVGPTLLAAYEGRIINIHPAYLPEFPGAHGIEDAWNAGVAESGVTIHWVDSGVDTGK 142
Cdd:PLN02828  138 EDEILELVKG--TDFLVLARYMQILSGNFLKGYGKDIINIHHGLLPSFKGGNPSKQAFDAGVKLIGATSHFVTEELDAGP 215

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1080615070 143 VIKQVrVPRL-ESDTLDTFETRiheteyklyPEVLERLGVAR 183
Cdd:PLN02828  216 IIEQM-VERVsHRDNLRSFVQK---------SENLEKQCLAK 247
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
63-179 5.64e-16

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


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 73.99  E-value: 5.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070  63 EEAIVHLLNEHQIDLVCLAGYMKIVGPTLLAAYEGRIINIHPAYLPEFPGA----HGIEdawnAGVAESGVTIHWVDSGV 138
Cdd:COG0223    67 DPEFLEELRALNPDLIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAapiqWAIL----NGDTETGVTIMQMDEGL 142

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1080615070 139 DTGKVIKQVRVPRLESDTLDTFETRIHETEYKLYPEVLERL 179
Cdd:COG0223   143 DTGDILLQEEVPIGPDDTAGSLHDKLAELGAELLLETLDAL 183
FMT_core_Met-tRNA-FMT_N cd08646
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ...
 63-159 1.57e-12

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: 62.85  E-value: 1.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070  63 EEAIVHLLNEHQIDLVCLAGYMKIVGPTLLAAYEGRIINIHPAYLPEFPGAHGIEDAWNAGVAESGVTIHWVDSGVDTGK 142
Cdd:cd08646    67 DEEFLEELKALKPDLIVVVAYGQILPKEILDLPPYGCINVHPSLLPKYRGAAPIQRAILNGDKETGVTIMKMDEGLDTGD 146

                          90
                  ....*....|....*..
gi 1080615070 143 VIKQVRVPRLESDTLDT 159
Cdd:cd08646   147 ILAQEEVPIDPDDTAGE 163
FMT_core_like_6 cd08820
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 50-177 1.69e-10

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: 57.07  E-value: 1.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070  50 AFELKEFDNKAAYEEAIVH----LLNEHQIDLVCLAGYMKIVGPTLLAAYEGRIINIHPAYLPEFPGAHGIEDAWNAGVA 125
Cdd:cd08820    41 VWEGSEPLYDIGSTERNLHklleILENKGVDILISVQYHWILPGSILEKAKEIAFNLHNAPLPEYRGCNQFSHAILNGDD 120

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1080615070 126 ESGVTIHWVDSGVDTGKVIKQVRVPRLESDTLDTFETRIHETEYKLYPEVLE 177
Cdd:cd08820   121 QFGTTIHWMAEGIDSGDIIFEKRFPIPSDCTVISLYILAHYAAIALFGEHIT 172
fmt TIGR00460
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ...
 69-179 2.09e-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: 58.18  E-value: 2.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070  69 LLNEHQIDLVCLAGYMKIVGPTLLAAYEGRIINIHPAYLPEFPGAHGIEDAWNAGVAESGVTIHWVDSGVDTGKVIKQVR 148
Cdd:TIGR00460  73 LVRELKPDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVPKMDAGDILKQET 152

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1080615070 149 VPRLESDTLDTFETRIHETEYKLYPEVLERL 179
Cdd:TIGR00460 153 FPIEEEDNSGTLSDKLSELGAQLLIETLKEL 183
PLN02285 PLN02285
methionyl-tRNA formyltransferase
 37-183 1.18e-09

methionyl-tRNA formyltransferase


Pssm-ID: 215159 [Multi-domain]  Cd Length: 334  Bit Score: 56.24  E-value: 1.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070  37 VLERAKNLGVVSHAFelkeFDNKAAYEEAIVHLLNEHQIDLVCLAGYMKIVGPTLLAAYEGRIINIHPAYLPEFPGAHGI 116
Cdd:PLN02285   60 VAQLALDRGFPPDLI----FTPEKAGEEDFLSALRELQPDLCITAAYGNILPQKFLDIPKLGTVNIHPSLLPLYRGAAPV 135

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1080615070 117 EDAWNAGVAESGVTIHWVDSGVDTGKVIKQVRVPRLESDTLDTFETRIHETEYKL----YPEVLERLGVAR 183
Cdd:PLN02285  136 QRALQDGVNETGVSVAFTVRALDAGPVIAQERVEVDEDIKAPELLPLLFELGTKLllreLPSVLDGSAKDK 206
FMT_core_NRPS_like cd08649
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ...
 44-179 1.68e-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: 51.49  E-value: 1.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070  44 LGVVSHAFELKEFdnkaAYEEAIVHL---------LNEHQIDLVCLAGYMKIVGPTLLAAYEGRIINIHPAYLPEFPGAH 114
Cdd:cd08649    26 AAVVSTDPAIRAW----AAAEGIAVLepgealeelLSDEPFDWLFSIVNLRILPSEVLALPRKGAINFHDGPLPRYAGLN 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080615070 115 GIEDAWNAGVAESGVTIHWVDSGVDTGKVIKQVRVPRLESDTLDTFETRIHETEYKLYPEVLERL 179
Cdd:cd08649   102 ATSWALLAGETRHGVTWHRIEEGVDAGDILVQRPFDIAPDDTALSLNLKCYEAGIEGFGELIDEL 166
FMT_core_FDH_N cd08647
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ...
 97-174 2.92e-08

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: 51.30  E-value: 2.92e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080615070  97 GRIInIHPAYLPEFPGAHGIEDAWNAGVAESGVTIHWVDSGVDTGKVIKQVRVPRLESDTLDTFETRIheteykLYPE 174
Cdd:cd08647   101 GSII-YHPSILPRHRGASAINWTLIHGDKKAGFTIFWADDGLDTGPILLQKECDVLPNDTVDTLYNRF------LYPE 171
FMT_core_like_5 cd08823
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 20-179 3.05e-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: 45.13  E-value: 3.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070  20 AEQFPVEFVFSdhrdayVLERAKNLGVVSHAFElkefdnkaayEEAIVHLLNEHQIDLVCLAGYMKIVGPTLLAAYEGRI 99
Cdd:cd08823    33 ASYFPQIFVFT------GIRRLVSKQRVDTANL----------KEQLAEWLRALAADTVVVFTFPYRIPQHILDLPPLGF 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070 100 INIHPAYLPEFPGAHGIEDAWNAGVAESGVTIHWVDSGVDTGKVIKQVRVPRLESDTLDTFETRIHETEYKLYPEVLERL 179
Cdd:cd08823    97 YNLHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMTAEIDRGPIVLEQFTPIHPDDTYGLLCSRLAMLAVGLLEELYQNL 176
PRK07579 PRK07579
dTDP-4-amino-4,6-dideoxyglucose formyltransferase;
98-179 6.90e-04

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


Pssm-ID: 236058 [Multi-domain]  Cd Length: 245  Bit Score: 39.12  E-value: 6.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070  98 RIINIHPAYLPE----FPGAHGIEDAwnagvAESGVTIHWVDSGVDTGKVIKQVRVPRLESDTLDTFETRIHETEYKLYP 173
Cdd:PRK07579   87 RCINIHPGFNPYnrgwFPQVFSIING-----LKIGATIHEMDEQLDHGPIIAQREVEIESWDSSGSVYARVMDIERELVL 161


                  ....*.
gi 1080615070 174 EVLERL 179
Cdd:PRK07579  162 EHFDAI 167
PRK06988 PRK06988
formyltransferase;
83-156 2.11e-03

formyltransferase;


Pssm-ID: 235902 [Multi-domain]  Cd Length: 312  Bit Score: 37.75  E-value: 2.11e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1080615070  83 YMKIVGPTLLAAYEGRIINIHPAYLPEFPGAHGIEDAWNAGVAESGVTIHWVDSGVDTGKVIKQVRVPRLESDT 156
Cdd:PRK06988   86 YRHMIPVDLLALAPRGAYNMHGSLLPKYRGRVPVNWAVLNGETETGATLHEMVAKPDAGAIVDQTAVPILPDDT 159
FMT_core_like_2 cd08822
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 76-181 6.86e-03

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: 35.90  E-value: 6.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080615070  76 DLVCLAGYMKIVGPTLLAAYEGRIINIHPAYLPEFPGAHGIEdaWNAGVAE--SGVTIHWVDSGVDTGKVIKQvrvprle 153
Cdd:cd08822    68 DLIVAAHCHAFISAKTRARARLGAIGYHPSLLPRHRGRDAVE--WTIRMRDpiTGGTVYHLDDGVDGGPIAAQ------- 138

                          90       100
                  ....*....|....*....|....*...
gi 1080615070 154 sdtlDTFETRIHETEYKLYPEVLERLGV 181
Cdd:cd08822   139 ----DWCHVRPGDTAAELWRRALAPMGV 162
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH