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Conserved domains on  [gi|490253861|ref|WP_004151854|]
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MULTISPECIES: formyltetrahydrofolate deformylase [Klebsiella]

Protein Classification

formyltetrahydrofolate deformylase( domain architecture ID 11481955)

formyltetrahydrofolate deformylase catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to tetrahydrofolate (FH4) and formate

EC:  3.5.1.10
Gene Ontology:  GO:0006189|GO:0008864|GO:0006164|GO:0016787
PubMed:  8226647|7868604|24108189

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
purU PRK06027
formyltetrahydrofolate deformylase; Reviewed
 1-280 2.07e-179

formyltetrahydrofolate deformylase; Reviewed


:

Pssm-ID: 235676 [Multi-domain]  Cd Length: 286  Bit Score: 495.01  E-value: 2.07e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861   1 MHSLQRKVLRTICPDQKGLIARITNICYKHELNIVQNNEFVDHRTGRFFMRTELEG---IFNDATLLADLDsALPE---G 74
Cdd:PRK06027   1 MMMMQRYVLTLSCPDRPGIVAAVSNFLYEHGGNIVDADQFVDPETGRFFMRVEFEGdglIFNLETLRADFA-ALAEefeM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861  75 SIRELNPAGRRRVVILVTKEAHCLGDLLMKANYGGLDVDIAAVIGNHDTLRSLVERFGIPFELVSHEGLSREEHDQRMGD 154
Cdd:PRK06027  80 DWRLLDSAERKRVVILVSKEDHCLGDLLWRWRSGELPVEIAAVISNHDDLRSLVERFGIPFHHVPVTKETKAEAEARLLE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861 155 AIAAHEPDYVVLAKYMRVLTPEFVARFPNKIINIHHSFLPAFIGARPYHQAYERGVKIIGATAHYVNDNLDEGPIIMQDV 234
Cdd:PRK06027 160 LIDEYQPDLVVLARYMQILSPDFVARFPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDV 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 490253861 235 IHVDHTYTAEDMMRAGRDVEKNVLSRALYQVLAQRVFVYGNRTIIL 280
Cdd:PRK06027 240 IRVDHRDTAEDLVRAGRDVEKQVLARAVRWHLEDRVLVYGNKTVVF 285
 
Name Accession Description Interval E-value
purU PRK06027
formyltetrahydrofolate deformylase; Reviewed
 1-280 2.07e-179

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 235676 [Multi-domain]  Cd Length: 286  Bit Score: 495.01  E-value: 2.07e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861   1 MHSLQRKVLRTICPDQKGLIARITNICYKHELNIVQNNEFVDHRTGRFFMRTELEG---IFNDATLLADLDsALPE---G 74
Cdd:PRK06027   1 MMMMQRYVLTLSCPDRPGIVAAVSNFLYEHGGNIVDADQFVDPETGRFFMRVEFEGdglIFNLETLRADFA-ALAEefeM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861  75 SIRELNPAGRRRVVILVTKEAHCLGDLLMKANYGGLDVDIAAVIGNHDTLRSLVERFGIPFELVSHEGLSREEHDQRMGD 154
Cdd:PRK06027  80 DWRLLDSAERKRVVILVSKEDHCLGDLLWRWRSGELPVEIAAVISNHDDLRSLVERFGIPFHHVPVTKETKAEAEARLLE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861 155 AIAAHEPDYVVLAKYMRVLTPEFVARFPNKIINIHHSFLPAFIGARPYHQAYERGVKIIGATAHYVNDNLDEGPIIMQDV 234
Cdd:PRK06027 160 LIDEYQPDLVVLARYMQILSPDFVARFPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDV 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 490253861 235 IHVDHTYTAEDMMRAGRDVEKNVLSRALYQVLAQRVFVYGNRTIIL 280
Cdd:PRK06027 240 IRVDHRDTAEDLVRAGRDVEKQVLARAVRWHLEDRVLVYGNKTVVF 285
PurU TIGR00655
formyltetrahydrofolate deformylase; This model describes formyltetrahydrofolate deformylases. ...
 7-280 1.28e-167

formyltetrahydrofolate deformylase; This model describes formyltetrahydrofolate deformylases. The enzyme is a homohexamer. Sequences from a related enzyme formyl tetrahydrofolate-specific enzyme, phosphoribosylglycinamide formyltransferase, serve as an outgroup for phylogenetic analysis. Putative members of this family, scoring below the trusted cutoff, include a sequence from Rhodobacter capsulatus that lacks an otherwise conserved C-terminal region. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273199 [Multi-domain]  Cd Length: 280  Bit Score: 464.98  E-value: 1.28e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861    7 KVLRTICPDQKGLIARITNICYKHELNIVQNNEFVDHRTGRFFMRTELEGIFN---DATLLADLDSALPE--GSIRELNP 81
Cdd:TIGR00655   1 GILLVSCPDQKGLVAAISTFIAKHGANIISNDQHTDPETGRFFMRVEFQLEGFrleESSLLAAFKSALAEkfEMTWELIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861   82 AGR-RRVVILVTKEAHCLGDLLMKANYGGLDVDIAAVIGNHDTLRSLVERFGIPFELVSHEGLSREEHDQRMGDAIAAHE 160
Cdd:TIGR00655  81 ADKlKRVAILVSKEDHCLGDLLWRWYSGELDAEIALVISNHEDLRSLVERFGIPFHYIPATKDNRVEHEKRQLELLKQYQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861  161 PDYVVLAKYMRVLTPEFVARFPNKIINIHHSFLPAFIGARPYHQAYERGVKIIGATAHYVNDNLDEGPIIMQDVIHVDHT 240
Cdd:TIGR00655 161 VDLVVLAKYMQILSPDFVKRYPNKIINIHHSFLPAFIGANPYQRAYERGVKIIGATAHYVTEELDEGPIIEQDVVRVDHT 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 490253861  241 YTAEDMMRAGRDVEKNVLSRALYQVLAQRVFVYGNRTIIL 280
Cdd:TIGR00655 241 DNVEDLIRAGRDIEKVVLARAVKLHLEDRVFVYENKTVVF 280
PurU COG0788
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ...
 5-280 1.15e-162

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: 452.58  E-value: 1.15e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861   5 QRKVLRTICPDQKGLIARITNICYKHELNIVQNNEFVDHRTGRFFMRTELEGI---FNDATLLADLDSALPE-GSIRELN 80
Cdd:COG0788    2 TTYILTLSCPDRPGIVAAVTGFLAEHGGNITEADQFVDPETGRFFMRVEFEAPgldFDLEALRAAFAPLAERfGMDWRLH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861  81 PAGRR-RVVILVTKEAHCLGDLLMKANYGGLDVDIAAVIGNHDTLRSLVERFGIPFELVSHEGLSREEHDQRMGDAIAAH 159
Cdd:COG0788   82 DSDRRkRVAILVSKEDHCLNDLLYRWRSGELPAEIPAVISNHPDLRPLAEWFGIPFHHIPVTKETKAEAEARLLELLEEY 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861 160 EPDYVVLAKYMRVLTPEFVARFPNKIINIHHSFLPAFIGARPYHQAYERGVKIIGATAHYVNDNLDEGPIIMQDVIHVDH 239
Cdd:COG0788  162 DIDLVVLARYMQILSPDFCARLPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVERVDH 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 490253861 240 TYTAEDMMRAGRDVEKNVLSRALYQVLAQRVFVYGNRTIIL 280
Cdd:COG0788  242 RDTPEDLVRKGRDVEKRVLARAVRWHLEDRVLVNGNKTVVF 282
FMT_core_Formyl-FH4-Hydrolase_C cd08648
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ...
 85-280 1.54e-115

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: 329.91  E-value: 1.54e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861  85 RRVVILVTKEAHCLGDLLMKANYGGLDVDIAAVIGNHDTLRSLVERFGIPFELVSHEGLSREEHDQRMGDAIAAHEPDYV 164
Cdd:cd08648    1 KRVAIFVSKEDHCLYDLLHRWREGELPCEIPLVISNHPDLRPLAERFGIPFHHIPVTKDTKAEAEAEQLELLEEYGVDLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861 165 VLAKYMRVLTPEFVARFPNKIINIHHSFLPAFIGARPYHQAYERGVKIIGATAHYVNDNLDEGPIIMQDVIHVDHTYTAE 244
Cdd:cd08648   81 VLARYMQILSPDFVERYPNRIINIHHSFLPAFKGAKPYHQAFERGVKLIGATAHYVTEELDEGPIIEQDVERVSHRDSVE 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 490253861 245 DMMRAGRDVEKNVLSRALYQVLAQRVFVYGNRTIIL 280
Cdd:cd08648  161 DLVRKGRDIEKQVLARAVKWHLEDRVLVYGNKTVVF 196
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 85-262 6.75e-74

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: 223.71  E-value: 6.75e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861   85 RRVVILVTKEAHCLGDLLMKANYGGLDVDIAAVIGNHDTL--RSLVERFGIPFELVSHEGL-SREEHDQRMGDAIAAHEP 161
Cdd:pfam00551   1 MKIAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDKAagLGRAEQAGIPTFVFEHKGLtPRSLFDQELADALRALAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861  162 DYVVLAKYMRVLTPEFVARFPNKIINIHHSFLPAFIGARPYHQAYERGVKIIGATAHYVNDNLDEGPIIMQDVIHVDHTY 241
Cdd:pfam00551  81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160

                         170       180
                  ....*....|....*....|.
gi 490253861  242 TAEDMMRAGRDVEKNVLSRAL 262
Cdd:pfam00551 161 TAETLYNRVADLEHKALPRVL 181
 
Name Accession Description Interval E-value
purU PRK06027
formyltetrahydrofolate deformylase; Reviewed
 1-280 2.07e-179

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 235676 [Multi-domain]  Cd Length: 286  Bit Score: 495.01  E-value: 2.07e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861   1 MHSLQRKVLRTICPDQKGLIARITNICYKHELNIVQNNEFVDHRTGRFFMRTELEG---IFNDATLLADLDsALPE---G 74
Cdd:PRK06027   1 MMMMQRYVLTLSCPDRPGIVAAVSNFLYEHGGNIVDADQFVDPETGRFFMRVEFEGdglIFNLETLRADFA-ALAEefeM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861  75 SIRELNPAGRRRVVILVTKEAHCLGDLLMKANYGGLDVDIAAVIGNHDTLRSLVERFGIPFELVSHEGLSREEHDQRMGD 154
Cdd:PRK06027  80 DWRLLDSAERKRVVILVSKEDHCLGDLLWRWRSGELPVEIAAVISNHDDLRSLVERFGIPFHHVPVTKETKAEAEARLLE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861 155 AIAAHEPDYVVLAKYMRVLTPEFVARFPNKIINIHHSFLPAFIGARPYHQAYERGVKIIGATAHYVNDNLDEGPIIMQDV 234
Cdd:PRK06027 160 LIDEYQPDLVVLARYMQILSPDFVARFPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDV 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 490253861 235 IHVDHTYTAEDMMRAGRDVEKNVLSRALYQVLAQRVFVYGNRTIIL 280
Cdd:PRK06027 240 IRVDHRDTAEDLVRAGRDVEKQVLARAVRWHLEDRVLVYGNKTVVF 285
PurU TIGR00655
formyltetrahydrofolate deformylase; This model describes formyltetrahydrofolate deformylases. ...
 7-280 1.28e-167

formyltetrahydrofolate deformylase; This model describes formyltetrahydrofolate deformylases. The enzyme is a homohexamer. Sequences from a related enzyme formyl tetrahydrofolate-specific enzyme, phosphoribosylglycinamide formyltransferase, serve as an outgroup for phylogenetic analysis. Putative members of this family, scoring below the trusted cutoff, include a sequence from Rhodobacter capsulatus that lacks an otherwise conserved C-terminal region. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273199 [Multi-domain]  Cd Length: 280  Bit Score: 464.98  E-value: 1.28e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861    7 KVLRTICPDQKGLIARITNICYKHELNIVQNNEFVDHRTGRFFMRTELEGIFN---DATLLADLDSALPE--GSIRELNP 81
Cdd:TIGR00655   1 GILLVSCPDQKGLVAAISTFIAKHGANIISNDQHTDPETGRFFMRVEFQLEGFrleESSLLAAFKSALAEkfEMTWELIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861   82 AGR-RRVVILVTKEAHCLGDLLMKANYGGLDVDIAAVIGNHDTLRSLVERFGIPFELVSHEGLSREEHDQRMGDAIAAHE 160
Cdd:TIGR00655  81 ADKlKRVAILVSKEDHCLGDLLWRWYSGELDAEIALVISNHEDLRSLVERFGIPFHYIPATKDNRVEHEKRQLELLKQYQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861  161 PDYVVLAKYMRVLTPEFVARFPNKIINIHHSFLPAFIGARPYHQAYERGVKIIGATAHYVNDNLDEGPIIMQDVIHVDHT 240
Cdd:TIGR00655 161 VDLVVLAKYMQILSPDFVKRYPNKIINIHHSFLPAFIGANPYQRAYERGVKIIGATAHYVTEELDEGPIIEQDVVRVDHT 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 490253861  241 YTAEDMMRAGRDVEKNVLSRALYQVLAQRVFVYGNRTIIL 280
Cdd:TIGR00655 241 DNVEDLIRAGRDIEKVVLARAVKLHLEDRVFVYENKTVVF 280
PurU COG0788
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ...
 5-280 1.15e-162

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: 452.58  E-value: 1.15e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861   5 QRKVLRTICPDQKGLIARITNICYKHELNIVQNNEFVDHRTGRFFMRTELEGI---FNDATLLADLDSALPE-GSIRELN 80
Cdd:COG0788    2 TTYILTLSCPDRPGIVAAVTGFLAEHGGNITEADQFVDPETGRFFMRVEFEAPgldFDLEALRAAFAPLAERfGMDWRLH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861  81 PAGRR-RVVILVTKEAHCLGDLLMKANYGGLDVDIAAVIGNHDTLRSLVERFGIPFELVSHEGLSREEHDQRMGDAIAAH 159
Cdd:COG0788   82 DSDRRkRVAILVSKEDHCLNDLLYRWRSGELPAEIPAVISNHPDLRPLAEWFGIPFHHIPVTKETKAEAEARLLELLEEY 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861 160 EPDYVVLAKYMRVLTPEFVARFPNKIINIHHSFLPAFIGARPYHQAYERGVKIIGATAHYVNDNLDEGPIIMQDVIHVDH 239
Cdd:COG0788  162 DIDLVVLARYMQILSPDFCARLPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVERVDH 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 490253861 240 TYTAEDMMRAGRDVEKNVLSRALYQVLAQRVFVYGNRTIIL 280
Cdd:COG0788  242 RDTPEDLVRKGRDVEKRVLARAVRWHLEDRVLVNGNKTVVF 282
FMT_core_Formyl-FH4-Hydrolase_C cd08648
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ...
 85-280 1.54e-115

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: 329.91  E-value: 1.54e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861  85 RRVVILVTKEAHCLGDLLMKANYGGLDVDIAAVIGNHDTLRSLVERFGIPFELVSHEGLSREEHDQRMGDAIAAHEPDYV 164
Cdd:cd08648    1 KRVAIFVSKEDHCLYDLLHRWREGELPCEIPLVISNHPDLRPLAERFGIPFHHIPVTKDTKAEAEAEQLELLEEYGVDLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861 165 VLAKYMRVLTPEFVARFPNKIINIHHSFLPAFIGARPYHQAYERGVKIIGATAHYVNDNLDEGPIIMQDVIHVDHTYTAE 244
Cdd:cd08648   81 VLARYMQILSPDFVERYPNRIINIHHSFLPAFKGAKPYHQAFERGVKLIGATAHYVTEELDEGPIIEQDVERVSHRDSVE 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 490253861 245 DMMRAGRDVEKNVLSRALYQVLAQRVFVYGNRTIIL 280
Cdd:cd08648  161 DLVRKGRDIEKQVLARAVKWHLEDRVLVYGNKTVVF 196
PRK13011 PRK13011
formyltetrahydrofolate deformylase; Reviewed
 8-280 2.01e-94

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 237266 [Multi-domain]  Cd Length: 286  Bit Score: 279.95  E-value: 2.01e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861   8 VLRTICPDQKGLIARITNICYKHELNIVQNNEFVDHRTGRFFMRTE--LEGIFNDATLLADL-DSALPEGSIRELNPAGR 84
Cdd:PRK13011   9 VLTLSCPSAAGIVAAVTGFLAEHGCYITELHSFDDRLSGRFFMRVEfhSEEGLDEDALRAGFaPIAARFGMQWELHDPAA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861  85 R-RVVILVTKEAHCLGDLLMKANYGGLDVDIAAVIGNHDTLRSLVERFGIPFElvsHEGLSRE---EHDQRMGDAIAAHE 160
Cdd:PRK13011  89 RpKVLIMVSKFDHCLNDLLYRWRIGELPMDIVGVVSNHPDLEPLAAWHGIPFH---HFPITPDtkpQQEAQVLDVVEESG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861 161 PDYVVLAKYMRVLTPEFVARFPNKIINIHHSFLPAFIGARPYHQAYERGVKIIGATAHYVNDNLDEGPIIMQDVIHVDHT 240
Cdd:PRK13011 166 AELVVLARYMQVLSPELCRKLAGRAINIHHSFLPGFKGAKPYHQAYERGVKLIGATAHYVTDDLDEGPIIEQDVERVDHA 245

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 490253861 241 YTAEDMMRAGRDVEKNVLSRALYQVLAQRVFVYGNRTIIL 280
Cdd:PRK13011 246 YSPEDLVAKGRDVECLTLARAVKAHIERRVFLNGNRTVVF 285
purU PRK13010
formyltetrahydrofolate deformylase; Reviewed
 8-280 1.20e-85

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 139334 [Multi-domain]  Cd Length: 289  Bit Score: 257.80  E-value: 1.20e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861   8 VLRTICPDQKGLIARITNICYKHELNIVQNNEFVDHRTGRFFMRTELEGIFNDATLLADLDSALpeGSIRE-------LN 80
Cdd:PRK13010  11 VLTLACPSAPGIVAAVSGFLAEKGCYIVELTQFDDDESGRFFMRVSFHAQSAEAASVDTFRQEF--QPVAEkfdmqwaIH 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861  81 PAG-RRRVVILVTKEAHCLGDLLMKANYGGLDVDIAAVIGNHDTLRSLVERFGIPFELVSHEGLSREEHDQRMGDAIAAH 159
Cdd:PRK13010  89 PDGqRPKVVIMVSKFDHCLNDLLYRWRMGELDMDIVGIISNHPDLQPLAVQHDIPFHHLPVTPDTKAQQEAQILDLIETS 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861 160 EPDYVVLAKYMRVLTPEFVARFPNKIINIHHSFLPAFIGARPYHQAYERGVKIIGATAHYVNDNLDEGPIIMQDVIHVDH 239
Cdd:PRK13010 169 GAELVVLARYMQVLSDDLSRKLSGRAINIHHSFLPGFKGARPYHQAHARGVKLIGATAHFVTDDLDEGPIIEQDVERVDH 248

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 490253861 240 TYTAEDMMRAGRDVEKNVLSRALYQVLAQRVFVYGNRTIIL 280
Cdd:PRK13010 249 SYSPEDLVAKGRDVECLTLARAVKAFIEHRVFINGDRTVVF 289
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 85-262 6.75e-74

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: 223.71  E-value: 6.75e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861   85 RRVVILVTKEAHCLGDLLMKANYGGLDVDIAAVIGNHDTL--RSLVERFGIPFELVSHEGL-SREEHDQRMGDAIAAHEP 161
Cdd:pfam00551   1 MKIAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDKAagLGRAEQAGIPTFVFEHKGLtPRSLFDQELADALRALAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861  162 DYVVLAKYMRVLTPEFVARFPNKIINIHHSFLPAFIGARPYHQAYERGVKIIGATAHYVNDNLDEGPIIMQDVIHVDHTY 241
Cdd:pfam00551  81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160

                         170       180
                  ....*....|....*....|.
gi 490253861  242 TAEDMMRAGRDVEKNVLSRAL 262
Cdd:pfam00551 161 TAETLYNRVADLEHKALPRVL 181
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 108-279 4.76e-51

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: 166.36  E-value: 4.76e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861 108 GGLDVDIAAVIGNHDTLRSL--VERFGIPFELVSHEGL-SREEHDQRMGDAIAAHEPDYVVLAKYMRVLTPEFVARFPNK 184
Cdd:COG0299   25 GDLPAEIVLVISNRPDAYGLerARAAGIPTFVLDHKDFpSREAFDAALLEALDAYGPDLVVLAGFMRILTPEFVRAFPGR 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861 185 IINIHHSFLPAFIGARPYHQAYERGVKIIGATAHYVNDNLDEGPIIMQDVIHVDHTYTAEDMMRAGRDVEKNVLSRALYQ 264
Cdd:COG0299  105 IINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDDTEETLAARILEQEHRLYPEAIRL 184

                        170
                 ....*....|....*
gi 490253861 265 VLAQRVFVYGNRTII 279
Cdd:COG0299  185 LAEGRLTLDGRRVRL 199
PLN02828 PLN02828
formyltetrahydrofolate deformylase
 86-280 1.90e-46

formyltetrahydrofolate deformylase


Pssm-ID: 178422  Cd Length: 268  Bit Score: 156.44  E-value: 1.90e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861  86 RVVILVTKEAHCLGDLLMKANYGGLDVDIAAVIGNHDT-----LRSLVERFGIPFE-LVSHEGLSREEHDQRMgdaiaAH 159
Cdd:PLN02828  72 KIAVLASKQDHCLIDLLHRWQDGRLPVDITCVISNHERgpnthVMRFLERHGIPYHyLPTTKENKREDEILEL-----VK 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861 160 EPDYVVLAKYMRVLTPEFVARFPNKIINIHHSFLPAFIGARPYHQAYERGVKIIGATAHYVNDNLDEGPIIMQDVIHVDH 239
Cdd:PLN02828 147 GTDFLVLARYMQILSGNFLKGYGKDIINIHHGLLPSFKGGNPSKQAFDAGVKLIGATSHFVTEELDAGPIIEQMVERVSH 226

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 490253861 240 TYTAEDMMRAGRDVEKNVLSRALYQVLAQRVFVYG-NRTIIL 280
Cdd:PLN02828 227 RDNLRSFVQKSENLEKQCLAKAIKSYCELRVLPYGtNKTVVF 268
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 108-245 7.39e-46

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: 152.16  E-value: 7.39e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861 108 GGLDVDIAAVIGNHDTLRSLV--ERFGIPFELVSH-EGLSREEHDQRMGDAIAAHEPDYVVLAKYMRVLTPEFVARFPNK 184
Cdd:cd08645   23 GKLNAEIVLVISNNPDAYGLEraKKAGIPTFVINRkDFPSREEFDEALLELLKEYKVDLIVLAGFMRILSPEFLEAFPGR 102

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490253861 185 IINIHHSFLPAFIGARPYHQAYERGVKIIGATAHYVNDNLDEGPIIMQDVIHVDHTYTAED 245
Cdd:cd08645  103 IINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDTPET 163
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 86-270 3.64e-41

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: 140.58  E-value: 3.64e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861   86 RVVILVTKEAHCLGDLLMKANYGGLDVDIAAVIGNHDTLRSLV--ERFGIPFELVSHEGL-SREEHDQRMGDAIAAHEPD 162
Cdd:TIGR00639   2 RIVVLISGNGSNLQAIIDACKEGKIPASVVLVISNKPDAYGLEraAQAGIPTFVLSLKDFpSREAFDQAIIEELRAHEVD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861  163 YVVLAKYMRVLTPEFVARFPNKIINIHHSFLPAFIGARPYHQAYERGVKIIGATAHYVNDNLDEGPIIMQDVIHVDHTYT 242
Cdd:TIGR00639  82 LVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPEDT 161

                         170       180
                  ....*....|....*....|....*...
gi 490253861  243 AEDMMRAGRDVEKNVLSRALYQVLAQRV 270
Cdd:TIGR00639 162 EETLEQRIHKQEHRIYPLAIAWFAQGRL 189
FMT_core cd08369
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...
 87-264 4.23e-37

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: 129.33  E-value: 4.23e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861  87 VVILVTKEahcLGDLLMKANYGGLDVDIAAVIGNHDTLRSLVERFGIPFELVSHegLSREEHDQRMGDAIAAHEPDYVVL 166
Cdd:cd08369    1 IVILGSGN---IGQRVLKALLSKEGHEIVGVVTHPDSPRGTAQLSLELVGGKVY--LDSNINTPELLELLKEFAPDLIVS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861 167 AKYMRVLTPEFVARFPNKIINIHHSFLPAFIGARPYHQAYERGVKIIGATAHYVNDNLDEGPIIMQDVIHVDHTYTAEDM 246
Cdd:cd08369   76 INFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTAGTL 155

                        170
                 ....*....|....*...
gi 490253861 247 MRAGRDVEKNVLSRALYQ 264
Cdd:cd08369  156 YQRLIELGPKLLKEALQK 173
ACT_F4HF-DF cd04875
N-terminal ACT domain of formyltetrahydrofolate deformylase (F4HF-DF; formyltetrahydrofolate ...
 8-71 3.02e-19

N-terminal ACT domain of formyltetrahydrofolate deformylase (F4HF-DF; formyltetrahydrofolate hydrolase); This CD includes the N-terminal ACT domain of formyltetrahydrofolate deformylase (F4HF-DF; formyltetrahydrofolate hydrolase) which catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate. Formyl-FH4 hydrolase generates the formate that is used by purT-encoded 5'-phosphoribosylglycinamide transformylase for step three of de novo purine nucleotide synthesis. Formyl-FH4 hydrolase, a hexamer which is activated by methionine and inhibited by glycine, is proposed to regulate the balance FH4 and C1-FH4 in response to changing growth conditions. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153147 [Multi-domain]  Cd Length: 74  Bit Score: 79.53  E-value: 3.02e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490253861   8 VLRTICPDQKGLIARITNICYKHELNIVQNNEFVDHRTGRFFMRTELEGIFNDATlLADLDSAL 71
Cdd:cd04875    1 ILTLSCPDRPGIVAAVSGFLAEHGGNIVESDQFVDPDSGRFFMRVEFELEGFDLS-REALEAAF 63
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 141-246 3.50e-18

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 80.51  E-value: 3.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861 141 EGLSREEhdqrMGDAIAAHEPDYVVLAKYMRVLTPEFVARFPNKIINIHHSFLPAFIGARPY----HQAY-ERGVKIIGA 215
Cdd:PLN02331  63 DGLSPDE----LVDALRGAGVDFVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFGGKGYYgikvHKAViASGARYSGP 138

                         90       100       110
                 ....*....|....*....|....*....|.
gi 490253861 216 TAHYVNDNLDEGPIIMQDVIHVDHTYTAEDM 246
Cdd:PLN02331 139 TVHFVDEHYDTGRILAQRVVPVLATDTPEEL 169
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
154-270 1.34e-13

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


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 69.36  E-value: 1.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861 154 DAIAAHEPDYVVLAKYMRVLTPEFVARFPNKIINIHHSFLPAFIGARPYHQAYERGVKIIGATAHYVNDNLDEGPIIMQD 233
Cdd:COG0223   72 EELRALNPDLIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDTGDILLQE 151

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 490253861 234 VIHVDHTYTAED----MMRAGRDveknVLSRALYQVLAQRV 270
Cdd:COG0223  152 EVPIGPDDTAGSlhdkLAELGAE----LLLETLDALEAGTL 188
FMT_core_Met-tRNA-FMT_N cd08646
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ...
 154-247 3.39e-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: 64.00  E-value: 3.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861 154 DAIAAHEPDYVVLAKYMRVLTPEFVARFPNKIINIHHSFLPAFIGARPYHQAYERGVKIIGATAHYVNDNLDEGPIIMQD 233
Cdd:cd08646   72 EELKALKPDLIVVVAYGQILPKEILDLPPYGCINVHPSLLPKYRGAAPIQRAILNGDKETGVTIMKMDEGLDTGDILAQE 151

                         90
                 ....*....|....
gi 490253861 234 VIHVDHTYTAEDMM 247
Cdd:cd08646  152 EVPIDPDDTAGELL 165
PLN02285 PLN02285
methionyl-tRNA formyltransferase
 80-247 1.37e-11

methionyl-tRNA formyltransferase


Pssm-ID: 215159 [Multi-domain]  Cd Length: 334  Bit Score: 63.94  E-value: 1.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861  80 NPAGRRRVVILVTKE--AHCLGDLLMKANYGGLDVDIAAVIGNHDTLR------------SLVERFGIPFELVSHEGLSR 145
Cdd:PLN02285   2 GSGRKKRLVFLGTPEvaATVLDALLDASQAPDSAFEVAAVVTQPPARRgrgrklmpspvaQLALDRGFPPDLIFTPEKAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861 146 EEHdqrMGDAIAAHEPDYVVLAKYMRVLTPEFVARFPNKIINIHHSFLPAFIGARPYHQAYERGVKIIGATAHYVNDNLD 225
Cdd:PLN02285  82 EED---FLSALRELQPDLCITAAYGNILPQKFLDIPKLGTVNIHPSLLPLYRGAAPVQRALQDGVNETGVSVAFTVRALD 158

                        170       180
                 ....*....|....*....|..
gi 490253861 226 EGPIIMQDVIHVDHTYTAEDMM 247
Cdd:PLN02285 159 AGPVIAQERVEVDEDIKAPELL 180
FMT_core_like_5 cd08823
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 162-241 8.79e-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: 187725 [Multi-domain]  Cd Length: 177  Bit Score: 56.68  E-value: 8.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861 162 DYVVLAKYMRVLTPEFVARFPNKIINIHHSFLPAFIGARP-YHQAYERGVKiIGATAHYVNDNLDEGPIIMQDV--IHVD 238
Cdd:cd08823   73 DTVVVFTFPYRIPQHILDLPPLGFYNLHPGLLPAYRGPDPlFWQIRNQEQE-TAITVHKMTAEIDRGPIVLEQFtpIHPD 151


                 ...
gi 490253861 239 HTY 241
Cdd:cd08823  152 DTY 154
PRK06988 PRK06988
formyltransferase;
96-267 9.62e-10

formyltransferase;


Pssm-ID: 235902 [Multi-domain]  Cd Length: 312  Bit Score: 58.17  E-value: 9.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861  96 HCLGDLLMKAnyggldVDIAAVIGNHD---------TLRSLVERFGIPFelVSHEGLSREEHDQRmgdaIAAHEPDYVVL 166
Cdd:PRK06988  16 RCLQVLLARG------VDVALVVTHEDnpteniwfgSVAAVAAEHGIPV--ITPADPNDPELRAA----VAAAAPDFIFS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861 167 AKYMRVLTPEFVARFPNKIINIHHSFLPAFIGARPYHQAYERGVKIIGATAHYVNDNLDEGPIIMQDVIHVDHTYTAEDM 246
Cdd:PRK06988  84 FYYRHMIPVDLLALAPRGAYNMHGSLLPKYRGRVPVNWAVLNGETETGATLHEMVAKPDAGAIVDQTAVPILPDDTAAQV 163

                        170       180
                 ....*....|....*....|.
gi 490253861 247 MRAGRDVEKNVLSRALYQVLA 267
Cdd:PRK06988 164 FDKVTVAAEQTLWRVLPALLA 184
FMT_core_like_3 cd08653
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 148-261 1.84e-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: 187721 [Multi-domain]  Cd Length: 152  Bit Score: 52.21  E-value: 1.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861 148 HDQRMGDAIAAHEPDyVVLAKYMRVLTPEFVARFPNKIINIHHSFLPAFIGARP-YHQAYERGVKIIGATAHYVNDNLDE 226
Cdd:cd08653   35 NGPEVVAALRALAPD-VVSVYGCGIIKDALLAIPPLGVLNLHGGILPDYRGVHTgFWALANGDPDNVGVTVHLVDAGIDT 113

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 490253861 227 GPIIMQDVIHVDHTYTAEDMM----RAGRDVEKNVLSRA 261
Cdd:cd08653  114 GDVLAQARPPLAAGDTLLSLYlrlyRAGVELMVEAIADL 152
FMT_core_ArnA_N cd08644
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ...
 86-270 4.40e-08

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: 52.35  E-value: 4.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861  86 RVVILVTKEAHCLG-DLLMKANYggldvDIAAVIGNHD---------TLRSLVERFGIPfeLVSHEGLSREEhdqrMGDA 155
Cdd:cd08644    2 KAVVFAYHEVGYRClEALLAAGF-----EVVAVFTHTDnpgeniwfgSVAQLAREHGIP--VFTPDDINHPE----WVER 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861 156 IAAHEPDYVVLAKYMRVLTPEFVARFPNKIINIHHSFLPAFIGARPYHQAYERGVKIIGATAHYVNDNLDEGPIIMQDVI 235
Cdd:cd08644   71 LRALKPDLIFSFYYRHMISEDILEIARLGAFNLHGSLLPKYRGRAPLNWALINGETETGVTLHRMTKKPDAGAIVDQEKV 150

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 490253861 236 HVDHTYTAEDMMRAGRDVEKNVLSRALYQVLAQRV 270
Cdd:cd08644  151 PILPDDTAKSLFHKLCVAARRLLARTLPALKAGKA 185
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 8-71 7.15e-07

ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95, which is inhibited by serine. Aspartokinase EC:2.7.2.4, which is regulated by lysine. Acetolactate synthase small regulatory subunit, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51. formyltetrahydrofolate deformylase EC:3.5.1.10, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5


Pssm-ID: 426468 [Multi-domain]  Cd Length: 66  Bit Score: 45.76  E-value: 7.15e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490253861    8 VLRTICPDQKGLIARITNICYKHELNIVQNNEFVDHRTGRFFMRTELEGIFNDATLLADLDSAL 71
Cdd:pfam01842   2 VLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGGIVFVVIVVDEEDLEEVLEALKKLE 65
FMT_core_like_4 cd08651
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 123-243 3.56e-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: 187720 [Multi-domain]  Cd Length: 180  Bit Score: 46.49  E-value: 3.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861 123 TLRSLVERFGIPFELVSHEglsreeHDQRMGDAIAAHEPDYVVLAKYMRVLTPEFVARFPNKIINIHHSFLPAFIGARPY 202
Cdd:cd08651   44 DLDSFARKNGIPYYKFTDI------NDEEIIEWIKEANPDIIFVFGWSQLLKPEILAIPRLGVIGFHPTKLPKNRGRAPI 117

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 490253861 203 HQAYERGVKIIGATAHYVNDNLDEGPIIMQDVIHVDHTYTA 243
Cdd:cd08651  118 PWAILLGLKETASTFFWMDEGADSGDILSQEPFPIDKDDTA 158
FMT_core_like_2 cd08822
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 156-248 3.09e-05

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


Pssm-ID: 187724 [Multi-domain]  Cd Length: 192  Bit Score: 43.60  E-value: 3.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861 156 IAAHEPDYVvlakymrvlTPEFVARFPNKIINIHHSFLPAFIGARPYHQAYERGVKIIGATAHYVNDNLDEGPIIMQDVI 235
Cdd:cd08822   71 VAAHCHAFI---------SAKTRARARLGAIGYHPSLLPRHRGRDAVEWTIRMRDPITGGTVYHLDDGVDGGPIAAQDWC 141

                         90
                 ....*....|...
gi 490253861 236 HVDHTYTAEDMMR 248
Cdd:cd08822  142 HVRPGDTAAELWR 154
PRK08125 PRK08125
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ...
 154-270 2.65e-04

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


Pssm-ID: 236156 [Multi-domain]  Cd Length: 660  Bit Score: 42.28  E-value: 2.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861 154 DAIAAHEPDYVVLAKYMRVLTPEFVARFPNKIINIHHSFLPAFIGARPYHQAYERGVKIIGATAHYVNDNLDEGPIIMQD 233
Cdd:PRK08125  69 ERIRELAPDVIFSFYYRNLLSDEILQLAPAGAFNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQQ 148

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 490253861 234 VIHVDHTYTAEDMMRAGRDVEKNVLSRALYQVLAQRV 270
Cdd:PRK08125 149 RVAIAPDDTALTLHHKLCHAARQLLEQTLPAIKHGNI 185
PRK07579 PRK07579
dTDP-4-amino-4,6-dideoxyglucose formyltransferase;
165-238 3.90e-03

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


Pssm-ID: 236058 [Multi-domain]  Cd Length: 245  Bit Score: 37.96  E-value: 3.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253861 165 VLAKYMRVLTPEFVARFPNKI------INIHHSFLPAFIGARPYHQAYERGVKIiGATAHYVNDNLDEGPIIMQDVIHVD 238
Cdd:PRK07579  62 IVERYDLVLSFHCKQRFPAKLvngvrcINIHPGFNPYNRGWFPQVFSIINGLKI-GATIHEMDEQLDHGPIIAQREVEIE 140
ACT cd02116
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 9-61 4.78e-03

ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme; Members of this CD belong to the superfamily of ACT regulatory domains. Pairs of ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme. The ACT domain has been detected in a number of diverse proteins; some of these proteins are involved in amino acid and purine biosynthesis, phenylalanine hydroxylation, regulation of bacterial metabolism and transcription, and many remain to be characterized. ACT domain-containing enzymes involved in amino acid and purine synthesis are in many cases allosteric enzymes with complex regulation enforced by the binding of ligands. The ACT domain is commonly involved in the binding of a small regulatory molecule, such as the amino acids L-Ser and L-Phe in the case of D-3-phosphoglycerate dehydrogenase and the bifunctional chorismate mutase-prephenate dehydratase enzyme (P-protein), respectively. Aspartokinases typically consist of two C-terminal ACT domains in a tandem repeat, but the second ACT domain is inserted within the first, resulting in, what is normally the terminal beta strand of ACT2, formed from a region N-terminal of ACT1. ACT domain repeats have been shown to have nonequivalent ligand-binding sites with complex regulatory patterns such as those seen in the bifunctional enzyme, aspartokinase-homoserine dehydrogenase (ThrA). In other enzymes, such as phenylalanine hydroxylases, the ACT domain appears to function as a flexible small module providing allosteric regulation via transmission of conformational changes, these conformational changes are not necessarily initiated by regulatory ligand binding at the ACT domain itself. ACT domains are present either singularly, N- or C-terminal, or in pairs present C-terminal or between two catalytic domains. Unique to cyanobacteria are four ACT domains C-terminal to an aspartokinase domain. A few proteins are composed almost entirely of ACT domain repeats as seen in the four ACT domain protein, the ACR protein, found in higher plants; and the two ACT domain protein, the glycine cleavage system transcriptional repressor (GcvR) protein, found in some bacteria. Also seen are single ACT domain proteins similar to the Streptococcus pneumoniae ACT domain protein (uncharacterized pdb structure 1ZPV) found in both bacteria and archaea. Purportedly, the ACT domain is an evolutionarily mobile ligand binding regulatory module that has been fused to different enzymes at various times.


Pssm-ID: 153139 [Multi-domain]  Cd Length: 60  Bit Score: 34.58  E-value: 4.78e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 490253861   9 LRTICPDQKGLIARITNICYKHELNI--VQNNEFVDHRTGRFFMRTELEGIFNDA 61
Cdd:cd02116    1 LTVSGPDRPGLLAKVLSVLAEAGINItsIEQRTSGDGGEADIFIVVDGDGDLEKL 55
 
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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