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Conserved domains on  [gi|880808712|ref|WP_048660881|]
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MULTISPECIES: formyltetrahydrofolate deformylase [Vibrio]

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
 1-277 2.87e-176

formyltetrahydrofolate deformylase; Reviewed


:

Pssm-ID: 235676 [Multi-domain]  Cd Length: 286  Bit Score: 486.92  E-value: 2.87e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712   1 MERKTLLTHCTDAPGLISKITNICYKHQLNIIHNNEFVDNTSGHFFMRTELEG---YFNDETLLADLDqALP---QNTKR 74
Cdd:PRK06027   4 MQRYVLTLSCPDRPGIVAAVSNFLYEHGGNIVDADQFVDPETGRFFMRVEFEGdglIFNLETLRADFA-ALAeefEMDWR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712  75 KLVDSSRKRVVILVTKEAHCLGDILMKNFDGSLDVEIAAVVGNYDILQSLTERFDIPYHHVSHEGLNREEHEKKMLEVID 154
Cdd:PRK06027  83 LLDSAERKRVVILVSKEDHCLGDLLWRWRSGELPVEIAAVISNHDDLRSLVERFGIPFHHVPVTKETKAEAEARLLELID 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712 155 QYEADYLVLAKYMRVLTPGFVERYNHKIINIHHSFLPAFIGAKPYQQAYERGVKIIGATAHFVTNDLDEGPIIKQDVIPV 234
Cdd:PRK06027 163 EYQPDLVVLARYMQILSPDFVARFPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVIRV 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 880808712 235 DHNFSAKDMAQAGRDVEKNVLSKALNKVINDHVFVYGNKTVIL 277
Cdd:PRK06027 243 DHRDTAEDLVRAGRDVEKQVLARAVRWHLEDRVLVYGNKTVVF 285
 
Name Accession Description Interval E-value
purU PRK06027
formyltetrahydrofolate deformylase; Reviewed
 1-277 2.87e-176

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 235676 [Multi-domain]  Cd Length: 286  Bit Score: 486.92  E-value: 2.87e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712   1 MERKTLLTHCTDAPGLISKITNICYKHQLNIIHNNEFVDNTSGHFFMRTELEG---YFNDETLLADLDqALP---QNTKR 74
Cdd:PRK06027   4 MQRYVLTLSCPDRPGIVAAVSNFLYEHGGNIVDADQFVDPETGRFFMRVEFEGdglIFNLETLRADFA-ALAeefEMDWR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712  75 KLVDSSRKRVVILVTKEAHCLGDILMKNFDGSLDVEIAAVVGNYDILQSLTERFDIPYHHVSHEGLNREEHEKKMLEVID 154
Cdd:PRK06027  83 LLDSAERKRVVILVSKEDHCLGDLLWRWRSGELPVEIAAVISNHDDLRSLVERFGIPFHHVPVTKETKAEAEARLLELID 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712 155 QYEADYLVLAKYMRVLTPGFVERYNHKIINIHHSFLPAFIGAKPYQQAYERGVKIIGATAHFVTNDLDEGPIIKQDVIPV 234
Cdd:PRK06027 163 EYQPDLVVLARYMQILSPDFVARFPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVIRV 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 880808712 235 DHNFSAKDMAQAGRDVEKNVLSKALNKVINDHVFVYGNKTVIL 277
Cdd:PRK06027 243 DHRDTAEDLVRAGRDVEKQVLARAVRWHLEDRVLVYGNKTVVF 285
PurU COG0788
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ...
 1-277 1.19e-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: 1.19e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712   1 MERKTLLTHCTDAPGLISKITNICYKHQLNIIHNNEFVDNTSGHFFMRTELEGY---FNDETLLADLDQALPQ-NTKRKL 76
Cdd:COG0788    1 MTTYILTLSCPDRPGIVAAVTGFLAEHGGNITEADQFVDPETGRFFMRVEFEAPgldFDLEALRAAFAPLAERfGMDWRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712  77 VDSS-RKRVVILVTKEAHCLGDILMKNFDGSLDVEIAAVVGNYDILQSLTERFDIPYHHVSHEGLNREEHEKKMLEVIDQ 155
Cdd:COG0788   81 HDSDrRKRVAILVSKEDHCLNDLLYRWRSGELPAEIPAVISNHPDLRPLAEWFGIPFHHIPVTKETKAEAEARLLELLEE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712 156 YEADYLVLAKYMRVLTPGFVERYNHKIINIHHSFLPAFIGAKPYQQAYERGVKIIGATAHFVTNDLDEGPIIKQDVIPVD 235
Cdd:COG0788  161 YDIDLVVLARYMQILSPDFCARLPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVERVD 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 880808712 236 HNFSAKDMAQAGRDVEKNVLSKALNKVINDHVFVYGNKTVIL 277
Cdd:COG0788  241 HRDTPEDLVRKGRDVEKRVLARAVRWHLEDRVLVNGNKTVVF 282
PurU TIGR00655
formyltetrahydrofolate deformylase; This model describes formyltetrahydrofolate deformylases. ...
 4-277 7.00e-151

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: 422.61  E-value: 7.00e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712    4 KTLLTHCTDAPGLISKITNICYKHQLNIIHNNEFVDNTSGHFFMRTELEGYFN---DETLLADLDQALPQ--NTKRKLVD 78
Cdd:TIGR00655   1 GILLVSCPDQKGLVAAISTFIAKHGANIISNDQHTDPETGRFFMRVEFQLEGFrleESSLLAAFKSALAEkfEMTWELIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712   79 SSR-KRVVILVTKEAHCLGDILMKNFDGSLDVEIAAVVGNYDILQSLTERFDIPYHHVSHEGLNREEHEKKMLEVIDQYE 157
Cdd:TIGR00655  81 ADKlKRVAILVSKEDHCLGDLLWRWYSGELDAEIALVISNHEDLRSLVERFGIPFHYIPATKDNRVEHEKRQLELLKQYQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712  158 ADYLVLAKYMRVLTPGFVERYNHKIINIHHSFLPAFIGAKPYQQAYERGVKIIGATAHFVTNDLDEGPIIKQDVIPVDHN 237
Cdd:TIGR00655 161 VDLVVLAKYMQILSPDFVKRYPNKIINIHHSFLPAFIGANPYQRAYERGVKIIGATAHYVTEELDEGPIIEQDVVRVDHT 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 880808712  238 FSAKDMAQAGRDVEKNVLSKALNKVINDHVFVYGNKTVIL 277
Cdd:TIGR00655 241 DNVEDLIRAGRDIEKVVLARAVKLHLEDRVFVYENKTVVF 280
FMT_core_Formyl-FH4-Hydrolase_C cd08648
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ...
 82-277 2.23e-112

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: 321.82  E-value: 2.23e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712  82 KRVVILVTKEAHCLGDILMKNFDGSLDVEIAAVVGNYDILQSLTERFDIPYHHVSHEGLNREEHEKKMLEVIDQYEADYL 161
Cdd:cd08648    1 KRVAIFVSKEDHCLYDLLHRWREGELPCEIPLVISNHPDLRPLAERFGIPFHHIPVTKDTKAEAEAEQLELLEEYGVDLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712 162 VLAKYMRVLTPGFVERYNHKIINIHHSFLPAFIGAKPYQQAYERGVKIIGATAHFVTNDLDEGPIIKQDVIPVDHNFSAK 241
Cdd:cd08648   81 VLARYMQILSPDFVERYPNRIINIHHSFLPAFKGAKPYHQAFERGVKLIGATAHYVTEELDEGPIIEQDVERVSHRDSVE 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 880808712 242 DMAQAGRDVEKNVLSKALNKVINDHVFVYGNKTVIL 277
Cdd:cd08648  161 DLVRKGRDIEKQVLARAVKWHLEDRVLVYGNKTVVF 196
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 82-259 1.88e-60

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: 189.42  E-value: 1.88e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712   82 KRVVILVTKEAHCLGDILMKNFDGSLDVEIAAVVGNYDILQSLT--ERFDIPYHHVSHEGL-NREEHEKKMLEVIDQYEA 158
Cdd:pfam00551   1 MKIAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGraEQAGIPTFVFEHKGLtPRSLFDQELADALRALAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712  159 DYLVLAKYMRVLTPGFVERYNHKIINIHHSFLPAFIGAKPYQQAYERGVKIIGATAHFVTNDLDEGPIIKQDVIPVDHNF 238
Cdd:pfam00551  81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160

                         170       180
                  ....*....|....*....|.
gi 880808712  239 SAKDMAQAGRDVEKNVLSKAL 259
Cdd:pfam00551 161 TAETLYNRVADLEHKALPRVL 181
 
Name Accession Description Interval E-value
purU PRK06027
formyltetrahydrofolate deformylase; Reviewed
 1-277 2.87e-176

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 235676 [Multi-domain]  Cd Length: 286  Bit Score: 486.92  E-value: 2.87e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712   1 MERKTLLTHCTDAPGLISKITNICYKHQLNIIHNNEFVDNTSGHFFMRTELEG---YFNDETLLADLDqALP---QNTKR 74
Cdd:PRK06027   4 MQRYVLTLSCPDRPGIVAAVSNFLYEHGGNIVDADQFVDPETGRFFMRVEFEGdglIFNLETLRADFA-ALAeefEMDWR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712  75 KLVDSSRKRVVILVTKEAHCLGDILMKNFDGSLDVEIAAVVGNYDILQSLTERFDIPYHHVSHEGLNREEHEKKMLEVID 154
Cdd:PRK06027  83 LLDSAERKRVVILVSKEDHCLGDLLWRWRSGELPVEIAAVISNHDDLRSLVERFGIPFHHVPVTKETKAEAEARLLELID 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712 155 QYEADYLVLAKYMRVLTPGFVERYNHKIINIHHSFLPAFIGAKPYQQAYERGVKIIGATAHFVTNDLDEGPIIKQDVIPV 234
Cdd:PRK06027 163 EYQPDLVVLARYMQILSPDFVARFPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVIRV 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 880808712 235 DHNFSAKDMAQAGRDVEKNVLSKALNKVINDHVFVYGNKTVIL 277
Cdd:PRK06027 243 DHRDTAEDLVRAGRDVEKQVLARAVRWHLEDRVLVYGNKTVVF 285
PurU COG0788
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ...
 1-277 1.19e-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: 1.19e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712   1 MERKTLLTHCTDAPGLISKITNICYKHQLNIIHNNEFVDNTSGHFFMRTELEGY---FNDETLLADLDQALPQ-NTKRKL 76
Cdd:COG0788    1 MTTYILTLSCPDRPGIVAAVTGFLAEHGGNITEADQFVDPETGRFFMRVEFEAPgldFDLEALRAAFAPLAERfGMDWRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712  77 VDSS-RKRVVILVTKEAHCLGDILMKNFDGSLDVEIAAVVGNYDILQSLTERFDIPYHHVSHEGLNREEHEKKMLEVIDQ 155
Cdd:COG0788   81 HDSDrRKRVAILVSKEDHCLNDLLYRWRSGELPAEIPAVISNHPDLRPLAEWFGIPFHHIPVTKETKAEAEARLLELLEE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712 156 YEADYLVLAKYMRVLTPGFVERYNHKIINIHHSFLPAFIGAKPYQQAYERGVKIIGATAHFVTNDLDEGPIIKQDVIPVD 235
Cdd:COG0788  161 YDIDLVVLARYMQILSPDFCARLPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVERVD 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 880808712 236 HNFSAKDMAQAGRDVEKNVLSKALNKVINDHVFVYGNKTVIL 277
Cdd:COG0788  241 HRDTPEDLVRKGRDVEKRVLARAVRWHLEDRVLVNGNKTVVF 282
PurU TIGR00655
formyltetrahydrofolate deformylase; This model describes formyltetrahydrofolate deformylases. ...
 4-277 7.00e-151

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: 422.61  E-value: 7.00e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712    4 KTLLTHCTDAPGLISKITNICYKHQLNIIHNNEFVDNTSGHFFMRTELEGYFN---DETLLADLDQALPQ--NTKRKLVD 78
Cdd:TIGR00655   1 GILLVSCPDQKGLVAAISTFIAKHGANIISNDQHTDPETGRFFMRVEFQLEGFrleESSLLAAFKSALAEkfEMTWELIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712   79 SSR-KRVVILVTKEAHCLGDILMKNFDGSLDVEIAAVVGNYDILQSLTERFDIPYHHVSHEGLNREEHEKKMLEVIDQYE 157
Cdd:TIGR00655  81 ADKlKRVAILVSKEDHCLGDLLWRWYSGELDAEIALVISNHEDLRSLVERFGIPFHYIPATKDNRVEHEKRQLELLKQYQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712  158 ADYLVLAKYMRVLTPGFVERYNHKIINIHHSFLPAFIGAKPYQQAYERGVKIIGATAHFVTNDLDEGPIIKQDVIPVDHN 237
Cdd:TIGR00655 161 VDLVVLAKYMQILSPDFVKRYPNKIINIHHSFLPAFIGANPYQRAYERGVKIIGATAHYVTEELDEGPIIEQDVVRVDHT 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 880808712  238 FSAKDMAQAGRDVEKNVLSKALNKVINDHVFVYGNKTVIL 277
Cdd:TIGR00655 241 DNVEDLIRAGRDIEKVVLARAVKLHLEDRVFVYENKTVVF 280
FMT_core_Formyl-FH4-Hydrolase_C cd08648
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ...
 82-277 2.23e-112

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: 321.82  E-value: 2.23e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712  82 KRVVILVTKEAHCLGDILMKNFDGSLDVEIAAVVGNYDILQSLTERFDIPYHHVSHEGLNREEHEKKMLEVIDQYEADYL 161
Cdd:cd08648    1 KRVAIFVSKEDHCLYDLLHRWREGELPCEIPLVISNHPDLRPLAERFGIPFHHIPVTKDTKAEAEAEQLELLEEYGVDLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712 162 VLAKYMRVLTPGFVERYNHKIINIHHSFLPAFIGAKPYQQAYERGVKIIGATAHFVTNDLDEGPIIKQDVIPVDHNFSAK 241
Cdd:cd08648   81 VLARYMQILSPDFVERYPNRIINIHHSFLPAFKGAKPYHQAFERGVKLIGATAHYVTEELDEGPIIEQDVERVSHRDSVE 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 880808712 242 DMAQAGRDVEKNVLSKALNKVINDHVFVYGNKTVIL 277
Cdd:cd08648  161 DLVRKGRDIEKQVLARAVKWHLEDRVLVYGNKTVVF 196
PRK13011 PRK13011
formyltetrahydrofolate deformylase; Reviewed
 1-277 3.56e-96

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 237266 [Multi-domain]  Cd Length: 286  Bit Score: 284.18  E-value: 3.56e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712   1 MERKTLLTHCTDAPGLISKITNICYKHQLNIIHNNEFVDNTSGHFFMRTE--LEGYFNDETLLADLDQ-ALPQNTKRKLV 77
Cdd:PRK13011   5 PDTFVLTLSCPSAAGIVAAVTGFLAEHGCYITELHSFDDRLSGRFFMRVEfhSEEGLDEDALRAGFAPiAARFGMQWELH 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712  78 DSS-RKRVVILVTKEAHCLGDILMKNFDGSLDVEIAAVVGNYDILQSLTERFDIPYHHVSHEGLNREEHEKKMLEVIDQY 156
Cdd:PRK13011  85 DPAaRPKVLIMVSKFDHCLNDLLYRWRIGELPMDIVGVVSNHPDLEPLAAWHGIPFHHFPITPDTKPQQEAQVLDVVEES 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712 157 EADYLVLAKYMRVLTPGFVERYNHKIINIHHSFLPAFIGAKPYQQAYERGVKIIGATAHFVTNDLDEGPIIKQDVIPVDH 236
Cdd:PRK13011 165 GAELVVLARYMQVLSPELCRKLAGRAINIHHSFLPGFKGAKPYHQAYERGVKLIGATAHYVTDDLDEGPIIEQDVERVDH 244

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 880808712 237 NFSAKDMAQAGRDVEKNVLSKALNKVINDHVFVYGNKTVIL 277
Cdd:PRK13011 245 AYSPEDLVAKGRDVECLTLARAVKAHIERRVFLNGNRTVVF 285
purU PRK13010
formyltetrahydrofolate deformylase; Reviewed
 10-277 8.22e-85

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 139334 [Multi-domain]  Cd Length: 289  Bit Score: 255.49  E-value: 8.22e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712  10 CTDAPGLISKITNICYKHQLNIIHNNEFVDNTSGHFFMRTELEGYFNDETLLADLDQALPQ-----NTKRKLVDSS-RKR 83
Cdd:PRK13010  16 CPSAPGIVAAVSGFLAEKGCYIVELTQFDDDESGRFFMRVSFHAQSAEAASVDTFRQEFQPvaekfDMQWAIHPDGqRPK 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712  84 VVILVTKEAHCLGDILMKNFDGSLDVEIAAVVGNYDILQSLTERFDIPYHHVSHEGLNREEHEKKMLEVIDQYEADYLVL 163
Cdd:PRK13010  96 VVIMVSKFDHCLNDLLYRWRMGELDMDIVGIISNHPDLQPLAVQHDIPFHHLPVTPDTKAQQEAQILDLIETSGAELVVL 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712 164 AKYMRVLTPGFVERYNHKIINIHHSFLPAFIGAKPYQQAYERGVKIIGATAHFVTNDLDEGPIIKQDVIPVDHNFSAKDM 243
Cdd:PRK13010 176 ARYMQVLSDDLSRKLSGRAINIHHSFLPGFKGARPYHQAHARGVKLIGATAHFVTDDLDEGPIIEQDVERVDHSYSPEDL 255

                        250       260       270
                 ....*....|....*....|....*....|....
gi 880808712 244 AQAGRDVEKNVLSKALNKVINDHVFVYGNKTVIL 277
Cdd:PRK13010 256 VAKGRDVECLTLARAVKAFIEHRVFINGDRTVVF 289
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 82-259 1.88e-60

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: 189.42  E-value: 1.88e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712   82 KRVVILVTKEAHCLGDILMKNFDGSLDVEIAAVVGNYDILQSLT--ERFDIPYHHVSHEGL-NREEHEKKMLEVIDQYEA 158
Cdd:pfam00551   1 MKIAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGraEQAGIPTFVFEHKGLtPRSLFDQELADALRALAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712  159 DYLVLAKYMRVLTPGFVERYNHKIINIHHSFLPAFIGAKPYQQAYERGVKIIGATAHFVTNDLDEGPIIKQDVIPVDHNF 238
Cdd:pfam00551  81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160

                         170       180
                  ....*....|....*....|.
gi 880808712  239 SAKDMAQAGRDVEKNVLSKAL 259
Cdd:pfam00551 161 TAETLYNRVADLEHKALPRVL 181
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 104-276 2.37e-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: 166.75  E-value: 2.37e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712 104 DGSLDVEIAAVVGNYDILQSLT--ERFDIPYHHVSHEGL-NREEHEKKMLEVIDQYEADYLVLAKYMRVLTPGFVERYNH 180
Cdd:COG0299   24 AGDLPAEIVLVISNRPDAYGLEraRAAGIPTFVLDHKDFpSREAFDAALLEALDAYGPDLVVLAGFMRILTPEFVRAFPG 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712 181 KIINIHHSFLPAFIGAKPYQQAYERGVKIIGATAHFVTNDLDEGPIIKQDVIPVDHNFSAKDMAQAGRDVEKNVLSKALN 260
Cdd:COG0299  104 RIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDDTEETLAARILEQEHRLYPEAIR 183

                        170
                 ....*....|....*.
gi 880808712 261 KVINDHVFVYGNKTVI 276
Cdd:COG0299  184 LLAEGRLTLDGRRVRL 199
PLN02828 PLN02828
formyltetrahydrofolate deformylase
 30-277 8.23e-51

formyltetrahydrofolate deformylase


Pssm-ID: 178422  Cd Length: 268  Bit Score: 167.62  E-value: 8.23e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712  30 NIIHNNEFVDNTSGHFFMRTELegYFN---------DETLLADLDQALPQNTKRKLVDSSRK-RVVILVTKEAHCLGDIL 99
Cdd:PLN02828  11 NILGVDVFVPENKNVFYSRSEF--IFDpvkwpraqmDEDFQEISKHFKALKSVVRVPGLDPKyKIAVLASKQDHCLIDLL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712 100 MKNFDGSLDVEIAAVVGNYDILQS-----LTERFDIPYHHVSHEGLNREEHEkkMLEVIDqyEADYLVLAKYMRVLTPGF 174
Cdd:PLN02828  89 HRWQDGRLPVDITCVISNHERGPNthvmrFLERHGIPYHYLPTTKENKREDE--ILELVK--GTDFLVLARYMQILSGNF 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712 175 VERYNHKIINIHHSFLPAFIGAKPYQQAYERGVKIIGATAHFVTNDLDEGPIIKQDVIPVDHNFSAKDMAQAGRDVEKNV 254
Cdd:PLN02828 165 LKGYGKDIINIHHGLLPSFKGGNPSKQAFDAGVKLIGATSHFVTEELDAGPIIEQMVERVSHRDNLRSFVQKSENLEKQC 244

                        250       260
                 ....*....|....*....|....
gi 880808712 255 LSKALNKVINDHVFVYG-NKTVIL 277
Cdd:PLN02828 245 LAKAIKSYCELRVLPYGtNKTVVF 268
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 104-262 9.81e-45

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: 149.46  E-value: 9.81e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712 104 DGSLDVEIAAVVGNYDILQSLT--ERFDIPYHHVSH-EGLNREEHEKKMLEVIDQYEADYLVLAKYMRVLTPGFVERYNH 180
Cdd:cd08645   22 SGKLNAEIVLVISNNPDAYGLEraKKAGIPTFVINRkDFPSREEFDEALLELLKEYKVDLIVLAGFMRILSPEFLEAFPG 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712 181 KIINIHHSFLPAFIGAKPYQQAYERGVKIIGATAHFVTNDLDEGPIIKQDVIPVDHNFSAKDMAQAGRDVEKNVLSKALN 260
Cdd:cd08645  102 RIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDTPETLAERIHALEHRLYPEAIK 181


                 ..
gi 880808712 261 KV 262
Cdd:cd08645  182 LL 183
FMT_core cd08369
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...
 84-261 2.01e-35

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: 125.09  E-value: 2.01e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712  84 VVILVTKEahcLGDILMKNFDGSLDVEIAAVVGNYDILQSLTERFDIPYHHVSHegLNREEHEKKMLEVIDQYEADYLVL 163
Cdd:cd08369    1 IVILGSGN---IGQRVLKALLSKEGHEIVGVVTHPDSPRGTAQLSLELVGGKVY--LDSNINTPELLELLKEFAPDLIVS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712 164 AKYMRVLTPGFVERYNHKIINIHHSFLPAFIGAKPYQQAYERGVKIIGATAHFVTNDLDEGPIIKQDVIPVDHNFSAKDM 243
Cdd:cd08369   76 INFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTAGTL 155

                        170
                 ....*....|....*...
gi 880808712 244 AQAGRDVEKNVLSKALNK 261
Cdd:cd08369  156 YQRLIELGPKLLKEALQK 173
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 82-265 7.25e-32

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: 116.32  E-value: 7.25e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712   82 KRVVILVTKEAHCLGDILMKNFDGSLDVEIAAVVGNYDILQSLT--ERFDIPYHHVSHEGL-NREEHEKKMLEVIDQYEA 158
Cdd:TIGR00639   1 KRIVVLISGNGSNLQAIIDACKEGKIPASVVLVISNKPDAYGLEraAQAGIPTFVLSLKDFpSREAFDQAIIEELRAHEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712  159 DYLVLAKYMRVLTPGFVERYNHKIINIHHSFLPAFIGAKPYQQAYERGVKIIGATAHFVTNDLDEGPIIKQDVIPVDHNF 238
Cdd:TIGR00639  81 DLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPED 160

                         170       180
                  ....*....|....*....|....*..
gi 880808712  239 SAKDMAQAGRDVEKNVLSKALNKVIND 265
Cdd:TIGR00639 161 TEETLEQRIHKQEHRIYPLAIAWFAQG 187
ACT_F4HF-DF cd04875
N-terminal ACT domain of formyltetrahydrofolate deformylase (F4HF-DF; formyltetrahydrofolate ...
 5-70 5.23e-17

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: 73.75  E-value: 5.23e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 880808712   5 TLLTHCTDAPGLISKITNICYKHQLNIIHNNEFVDNTSGHFFMRTELEG---YFNDETLLADLDQALPQ 70
Cdd:cd04875    1 ILTLSCPDRPGIVAAVSGFLAEHGGNIVESDQFVDPDSGRFFMRVEFELegfDLSREALEAAFAPVAAE 69
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 138-244 8.92e-17

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 76.66  E-value: 8.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712 138 EGLNREEhekkMLEVIDQYEADYLVLAKYMRVLTPGFVERYNHKIINIHHSFLPAF-----IGAKPYQQAYERGVKIIGA 212
Cdd:PLN02331  63 DGLSPDE----LVDALRGAGVDFVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFggkgyYGIKVHKAVIASGARYSGP 138

                         90       100       110
                 ....*....|....*....|....*....|..
gi 880808712 213 TAHFVTNDLDEGPIIKQDVIPVDHNFSAKDMA 244
Cdd:PLN02331 139 TVHFVDEHYDTGRILAQRVVPVLATDTPEELA 170
PLN02285 PLN02285
methionyl-tRNA formyltransferase
 79-243 4.51e-12

methionyl-tRNA formyltransferase


Pssm-ID: 215159 [Multi-domain]  Cd Length: 334  Bit Score: 65.10  E-value: 4.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712  79 SSRKRVVILVTKE--AHCLGDILMKNFDGSLDVEIAAVV---------GNYDI---LQSLTERFDIPYHHVSHEGLNREE 144
Cdd:PLN02285   4 GRKKRLVFLGTPEvaATVLDALLDASQAPDSAFEVAAVVtqpparrgrGRKLMpspVAQLALDRGFPPDLIFTPEKAGEE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712 145 hekKMLEVIDQYEADYLVLAKYMRVLTPGFVERYNHKIINIHHSFLPAFIGAKPYQQAYERGVKIIGATAHFVTNDLDEG 224
Cdd:PLN02285  84 ---DFLSALRELQPDLCITAAYGNILPQKFLDIPKLGTVNIHPSLLPLYRGAAPVQRALQDGVNETGVSVAFTVRALDAG 160

                        170
                 ....*....|....*....
gi 880808712 225 PIIKQDVIPVDHNFSAKDM 243
Cdd:PLN02285 161 PVIAQERVEVDEDIKAPEL 179
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
108-264 2.84e-11

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


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 62.43  E-value: 2.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712 108 DVEIAAVV-------GNYDILQS-----LTERFDIPYHHvsHEGLNREEHekkmLEVIDQYEADYLVLAKYMRVLTPGFV 175
Cdd:COG0223   23 GHEVVAVVtqpdrpaGRGRKLTPspvkeLALEHGIPVLQ--PESLKDPEF----LEELRALNPDLIVVVAYGQILPKEVL 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712 176 ERYNHKIINIHHSFLPAFIGAKPYQQAYERGVKIIGATAHFVTNDLDEGPIIKQDVIPVDHNFSAKD----MAQAGRDve 251
Cdd:COG0223   97 DIPRLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDTGDILLQEEVPIGPDDTAGSlhdkLAELGAE-- 174

                        170
                 ....*....|...
gi 880808712 252 knVLSKALNKVIN 264
Cdd:COG0223  175 --LLLETLDALEA 185
FMT_core_Met-tRNA-FMT_N cd08646
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ...
 126-264 3.72e-10

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: 58.22  E-value: 3.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712 126 ERFDIPYHHVshEGLNREEhekkMLEVIDQYEADYLVLAKYMRVLTPGFVERYNHKIINIHHSFLPAFIGAKPYQQAYER 205
Cdd:cd08646   53 LELGLPVLQP--EKLKDEE----FLEELKALKPDLIVVVAYGQILPKEILDLPPYGCINVHPSLLPKYRGAAPIQRAILN 126

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 880808712 206 GVKIIGATAHFVTNDLDEGPIIKQDVIPVDHNFSAKD----MAQAGRDveknVLSKALNKVIN 264
Cdd:cd08646  127 GDKETGVTIMKMDEGLDTGDILAQEEVPIDPDDTAGElldkLAELGAD----LLLEVLDDIEA 185
FMT_core_like_5 cd08823
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 147-234 9.25e-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: 9.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712 147 KKMLEVIDQYEADYLVLAKYMRVLTPGFVERYNHKIINIHHSFLPAFIGAKP-YQQAYERGVKiIGATAHFVTNDLDEGP 225
Cdd:cd08823   61 EQLAEWLRALAADTVVVFTFPYRIPQHILDLPPLGFYNLHPGLLPAYRGPDPlFWQIRNQEQE-TAITVHKMTAEIDRGP 139


                 ....*....
gi 880808712 226 IIKQDVIPV 234
Cdd:cd08823  140 IVLEQFTPI 148
FMT_core_like_6 cd08820
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 83-243 2.64e-07

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: 49.36  E-value: 2.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712  83 RVVILVTKEA--HCLGDILMKNFDGslDVEIAAVVGNYDILQSltERFDIPYHHVSHEGLNREehekKMLEVIDQYEADY 160
Cdd:cd08820    1 RIVFLGQKPIgeECLRTLLRLQDRG--SFEIIAVLTNTSPADV--WEGSEPLYDIGSTERNLH----KLLEILENKGVDI 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712 161 LVLAKYMRVLTPGFVERYNHKIINIHHSFLPAFIGAKPYQQAYERGVKIIGATAHFVTNDLDEGPIIKQDVIPVDHNFSA 240
Cdd:cd08820   73 LISVQYHWILPGSILEKAKEIAFNLHNAPLPEYRGCNQFSHAILNGDDQFGTTIHWMAEGIDSGDIIFEKRFPIPSDCTV 152


                 ...
gi 880808712 241 KDM 243
Cdd:cd08820  153 ISL 155
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 5-68 5.50e-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: 46.15  E-value: 5.50e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 880808712    5 TLLTHCTDAPGLISKITNICYKHQLNIIHNNEFVDNTSGHFFMRTELEGYFNDETLLADLDQAL 68
Cdd:pfam01842   2 VLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGGIVFVVIVVDEEDLEEVLEALKKLE 65
FMT_core_like_3 cd08653
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 150-235 1.20e-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: 187721 [Multi-domain]  Cd Length: 152  Bit Score: 44.12  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712 150 LEVIDQYEADyLVLAKYMRVLTPGFVERYNHKIINIHHSFLPAFIGAKP-YQQAYERGVKIIGATAHFVTNDLDEGPIIK 228
Cdd:cd08653   40 VAALRALAPD-VVSVYGCGIIKDALLAIPPLGVLNLHGGILPDYRGVHTgFWALANGDPDNVGVTVHLVDAGIDTGDVLA 118


                 ....*..
gi 880808712 229 QDVIPVD 235
Cdd:cd08653  119 QARPPLA 125
FMT_core_ArnA_N cd08644
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ...
 184-243 2.82e-05

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: 43.87  E-value: 2.82e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712 184 NIHHSFLPAFIGAKPYQQAYERGVKIIGATAHFVTNDLDEGPIIKQDVIPVDHNFSAKDM 243
Cdd:cd08644  102 NLHGSLLPKYRGRAPLNWALINGETETGVTLHRMTKKPDAGAIVDQEKVPILPDDTAKSL 161
FMT_core_like_4 cd08651
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 106-262 4.44e-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: 187720 [Multi-domain]  Cd Length: 180  Bit Score: 43.02  E-value: 4.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808712 106 SLDVEIAAVVGNYDILQSLTERFDIPYHHVSHegLNREEhekkMLEVIDQYEADYLVLAKYMRVLTPGFVERYNHKIINI 185
Cdd:cd08651   30 TLDDSSSNNDSDYLDLDSFARKNGIPYYKFTD--INDEE----IIEWIKEANPDIIFVFGWSQLLKPEILAIPRLGVIGF 103

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 880808712 186 HHSFLPAFIGAKPYQQAYERGVKIIGATAHFVTNDLDEGPIIKQDVIPVDHNFSAKDMAQAGRDVEKNVLSKALNKV 262
Cdd:cd08651  104 HPTKLPKNRGRAPIPWAILLGLKETASTFFWMDEGADSGDILSQEPFPIDKDDTANSLYDKIMEAAKQQIDKFLPRL 180
ACT_Af1403 cd04874
N-terminal ACT domain of the yet uncharacterized, small (~133 a.a.), putative amino acid ...
 6-64 6.88e-04

N-terminal ACT domain of the yet uncharacterized, small (~133 a.a.), putative amino acid binding protein, Af1403, and related domains; This CD includes the N-terminal ACT domain of the yet uncharacterized, small (~133 a.a.), putative amino acid binding protein, Af1403, from Archaeoglobus fulgidus and other related archeal ACT domains. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153146 [Multi-domain]  Cd Length: 72  Bit Score: 37.28  E-value: 6.88e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 880808712   6 LLTHCTDAPGLISKITNICYKHQLNIIHNNEFVdNTSGHFFMRTELEGYFNDETLLADL 64
Cdd:cd04874    3 LSIIAEDKPGVLRDLTGVIAEHGGNITYTQQFI-EREGKARIYMELEGVGDIEELVEEL 60
PRK08125 PRK08125
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ...
 184-259 2.85e-03

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


Pssm-ID: 236156 [Multi-domain]  Cd Length: 660  Bit Score: 38.81  E-value: 2.85e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 880808712 184 NIHHSFLPAFIGAKPYQQAYERGVKIIGATAHFVTNDLDEGPIIKQDVIPVDHNFSAKDMAQAGRDVEKNVLSKAL 259
Cdd:PRK08125 102 NLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQQRVAIAPDDTALTLHHKLCHAARQLLEQTL 177
ACT_LSD cd04903
C-terminal ACT domain of the L-serine dehydratase (LSD), iron-sulfur-dependent, beta subunit; ...
 5-33 3.79e-03

C-terminal ACT domain of the L-serine dehydratase (LSD), iron-sulfur-dependent, beta subunit; The C-terminal ACT domain of the L-serine dehydratase (LSD), iron-sulfur-dependent, beta subunit, found in various bacterial anaerobes such as Clostridium, Bacillis, and Treponema species. These enzymes catalyze the deamination of L-serine, producing pyruvate and ammonia. Unlike the eukaryotic L-serine dehydratase, which requires the pyridoxal-5'-phosphate (PLP) cofactor, the prokaryotic L-serine dehydratase contains an [4Fe-4S] cluster instead of a PLP active site. The LSD alpha and beta subunits of the 'clostridial' enzyme are encoded by the sdhA and sdhB genes. The single subunit bacterial homologs of L-serine dehydratase (LSD1, LSD2, TdcG) present in Escherichia coli, and other enterobacterials, lack the ACT domain described here. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153175  Cd Length: 71  Bit Score: 35.20  E-value: 3.79e-03
                         10        20
                 ....*....|....*....|....*....
gi 880808712   5 TLLTHCTDAPGLISKITNICYKHQLNIIH 33
Cdd:cd04903    1 TLIVVHKDKPGAIAKVTSVLADHEINIAF 29
 
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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