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Conserved domains on  [gi|499270726|ref|WP_010968119|]
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formyltetrahydrofolate deformylase [Sinorhizobium meliloti]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PurU COG0788
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ...
8-285 3.73e-170

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: 471.84  E-value: 3.73e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726   8 FVLTLTCDDRAGIVAAVTSQLHVLGANIVESSQYWDRATNRFFMRIAFN-PSGETSADLIERGLAPVLGQFEMQGRLIDC 86
Cdd:COG0788    4 YILTLSCPDRPGIVAAVTGFLAEHGGNITEADQFVDPETGRFFMRVEFEaPGLDFDLEALRAAFAPLAERFGMDWRLHDS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726  87 RKPQKIVIMISRFDHAFLHLLYQIRVGWLDAEVVAVISNHDDSRETAAWAGIPYHFLPINRENKKKQEDRIFAIVQETEA 166
Cdd:COG0788   84 DRRKRVAILVSKEDHCLNDLLYRWRSGELPAEIPAVISNHPDLRPLAEWFGIPFHHIPVTKETKAEAEARLLELLEEYDI 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726 167 DLVVLARYMQVFSDDIAGRLFGKVINIHHSFLPSFKGARPYHQAHEHGVKLIGATAHYVTADLDEGPIIEQETERVSHAM 246
Cdd:COG0788  164 DLVVLARYMQILSPDFCARLPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVERVDHRD 243
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 499270726 247 SVEDFVAAGRDIESRVLARAVKRHLEARVMLNGRKTVVF 285
Cdd:COG0788  244 TPEDLVRKGRDVEKRVLARAVRWHLEDRVLVNGNKTVVF 282
 
Name Accession Description Interval E-value
PurU COG0788
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ...
8-285 3.73e-170

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: 471.84  E-value: 3.73e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726   8 FVLTLTCDDRAGIVAAVTSQLHVLGANIVESSQYWDRATNRFFMRIAFN-PSGETSADLIERGLAPVLGQFEMQGRLIDC 86
Cdd:COG0788    4 YILTLSCPDRPGIVAAVTGFLAEHGGNITEADQFVDPETGRFFMRVEFEaPGLDFDLEALRAAFAPLAERFGMDWRLHDS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726  87 RKPQKIVIMISRFDHAFLHLLYQIRVGWLDAEVVAVISNHDDSRETAAWAGIPYHFLPINRENKKKQEDRIFAIVQETEA 166
Cdd:COG0788   84 DRRKRVAILVSKEDHCLNDLLYRWRSGELPAEIPAVISNHPDLRPLAEWFGIPFHHIPVTKETKAEAEARLLELLEEYDI 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726 167 DLVVLARYMQVFSDDIAGRLFGKVINIHHSFLPSFKGARPYHQAHEHGVKLIGATAHYVTADLDEGPIIEQETERVSHAM 246
Cdd:COG0788  164 DLVVLARYMQILSPDFCARLPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVERVDHRD 243
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 499270726 247 SVEDFVAAGRDIESRVLARAVKRHLEARVMLNGRKTVVF 285
Cdd:COG0788  244 TPEDLVRKGRDVEKRVLARAVRWHLEDRVLVNGNKTVVF 282
purU PRK06027
formyltetrahydrofolate deformylase; Reviewed
5-286 7.42e-156

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 235676 [Multi-domain]  Cd Length: 286  Bit Score: 435.69  E-value: 7.42e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726   5 AQPFVLTLTCDDRAGIVAAVTSQLHVLGANIVESSQYWDRATNRFFMRIAFN-PSGETSADLIERGLAPVLGQFEMQGRL 83
Cdd:PRK06027   4 MQRYVLTLSCPDRPGIVAAVSNFLYEHGGNIVDADQFVDPETGRFFMRVEFEgDGLIFNLETLRADFAALAEEFEMDWRL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726  84 IDCRKPQKIVIMISRFDHAFLHLLYQIRVGWLDAEVVAVISNHDDSRETAAWAGIPYHFLPINRENKKKQEDRIFAIVQE 163
Cdd:PRK06027  84 LDSAERKRVVILVSKEDHCLGDLLWRWRSGELPVEIAAVISNHDDLRSLVERFGIPFHHVPVTKETKAEAEARLLELIDE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726 164 TEADLVVLARYMQVFSDDIAGRLFGKVINIHHSFLPSFKGARPYHQAHEHGVKLIGATAHYVTADLDEGPIIEQETERVS 243
Cdd:PRK06027 164 YQPDLVVLARYMQILSPDFVARFPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVIRVD 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 499270726 244 HAMSVEDFVAAGRDIESRVLARAVKRHLEARVMLNGRKTVVFA 286
Cdd:PRK06027 244 HRDTAEDLVRAGRDVEKQVLARAVRWHLEDRVLVYGNKTVVFR 286
FMT_core_Formyl-FH4-Hydrolase_C cd08648
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ...
90-285 3.95e-108

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: 311.42  E-value: 3.95e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726  90 QKIVIMISRFDHAFLHLLYQIRVGWLDAEVVAVISNHDDSRETAAWAGIPYHFLPINRENKKKQEDRIFAIVQETEADLV 169
Cdd:cd08648    1 KRVAIFVSKEDHCLYDLLHRWREGELPCEIPLVISNHPDLRPLAERFGIPFHHIPVTKDTKAEAEAEQLELLEEYGVDLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726 170 VLARYMQVFSDDIAGRLFGKVINIHHSFLPSFKGARPYHQAHEHGVKLIGATAHYVTADLDEGPIIEQETERVSHAMSVE 249
Cdd:cd08648   81 VLARYMQILSPDFVERYPNRIINIHHSFLPAFKGAKPYHQAFERGVKLIGATAHYVTEELDEGPIIEQDVERVSHRDSVE 160
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 499270726 250 DFVAAGRDIESRVLARAVKRHLEARVMLNGRKTVVF 285
Cdd:cd08648  161 DLVRKGRDIEKQVLARAVKWHLEDRVLVYGNKTVVF 196
PurU TIGR00655
formyltetrahydrofolate deformylase; This model describes formyltetrahydrofolate deformylases. ...
8-285 8.42e-107

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: 311.29  E-value: 8.42e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726    8 FVLTLTCDDRAGIVAAVTSQLHVLGANIVESSQYWDRATNRFFMRIAFNPSGETSA-DLIERGLAPVLGQ-FEMQGRLID 85
Cdd:TIGR00655   1 GILLVSCPDQKGLVAAISTFIAKHGANIISNDQHTDPETGRFFMRVEFQLEGFRLEeSSLLAAFKSALAEkFEMTWELIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726   86 CRKPQKIVIMISRFDHAFLHLLYQIRVGWLDAEVVAVISNHDDSRETAAWAGIPYHFLPINRENKKKQEDRIFAIVQETE 165
Cdd:TIGR00655  81 ADKLKRVAILVSKEDHCLGDLLWRWYSGELDAEIALVISNHEDLRSLVERFGIPFHYIPATKDNRVEHEKRQLELLKQYQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726  166 ADLVVLARYMQVFSDDIAGRLFGKVINIHHSFLPSFKGARPYHQAHEHGVKLIGATAHYVTADLDEGPIIEQETERVSHA 245
Cdd:TIGR00655 161 VDLVVLAKYMQILSPDFVKRYPNKIINIHHSFLPAFIGANPYQRAYERGVKIIGATAHYVTEELDEGPIIEQDVVRVDHT 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 499270726  246 MSVEDFVAAGRDIESRVLARAVKRHLEARVMLNGRKTVVF 285
Cdd:TIGR00655 241 DNVEDLIRAGRDIEKVVLARAVKLHLEDRVFVYENKTVVF 280
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
91-267 2.65e-37

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: 130.49  E-value: 2.65e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726   91 KIVIMISRFDHAFLHLLYQIRVGWLDAEVVAVISNHDD--SRETAAWAGIPYH-FLPINRENKKKQEDRIFAIVQETEAD 167
Cdd:pfam00551   2 KIAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDKaaGLGRAEQAGIPTFvFEHKGLTPRSLFDQELADALRALAAD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726  168 LVVLARYMQVFSDDIAGRLFGKVINIHHSFLPSFKGARPYHQAHEHGVKLIGATAHYVTADLDEGPIIEQETERVSHAMS 247
Cdd:pfam00551  82 VIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDDT 161
                         170       180
                  ....*....|....*....|
gi 499270726  248 VEDFVAAGRDIESRVLARAV 267
Cdd:pfam00551 162 AETLYNRVADLEHKALPRVL 181
 
Name Accession Description Interval E-value
PurU COG0788
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ...
8-285 3.73e-170

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: 471.84  E-value: 3.73e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726   8 FVLTLTCDDRAGIVAAVTSQLHVLGANIVESSQYWDRATNRFFMRIAFN-PSGETSADLIERGLAPVLGQFEMQGRLIDC 86
Cdd:COG0788    4 YILTLSCPDRPGIVAAVTGFLAEHGGNITEADQFVDPETGRFFMRVEFEaPGLDFDLEALRAAFAPLAERFGMDWRLHDS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726  87 RKPQKIVIMISRFDHAFLHLLYQIRVGWLDAEVVAVISNHDDSRETAAWAGIPYHFLPINRENKKKQEDRIFAIVQETEA 166
Cdd:COG0788   84 DRRKRVAILVSKEDHCLNDLLYRWRSGELPAEIPAVISNHPDLRPLAEWFGIPFHHIPVTKETKAEAEARLLELLEEYDI 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726 167 DLVVLARYMQVFSDDIAGRLFGKVINIHHSFLPSFKGARPYHQAHEHGVKLIGATAHYVTADLDEGPIIEQETERVSHAM 246
Cdd:COG0788  164 DLVVLARYMQILSPDFCARLPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVERVDHRD 243
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 499270726 247 SVEDFVAAGRDIESRVLARAVKRHLEARVMLNGRKTVVF 285
Cdd:COG0788  244 TPEDLVRKGRDVEKRVLARAVRWHLEDRVLVNGNKTVVF 282
purU PRK06027
formyltetrahydrofolate deformylase; Reviewed
5-286 7.42e-156

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 235676 [Multi-domain]  Cd Length: 286  Bit Score: 435.69  E-value: 7.42e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726   5 AQPFVLTLTCDDRAGIVAAVTSQLHVLGANIVESSQYWDRATNRFFMRIAFN-PSGETSADLIERGLAPVLGQFEMQGRL 83
Cdd:PRK06027   4 MQRYVLTLSCPDRPGIVAAVSNFLYEHGGNIVDADQFVDPETGRFFMRVEFEgDGLIFNLETLRADFAALAEEFEMDWRL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726  84 IDCRKPQKIVIMISRFDHAFLHLLYQIRVGWLDAEVVAVISNHDDSRETAAWAGIPYHFLPINRENKKKQEDRIFAIVQE 163
Cdd:PRK06027  84 LDSAERKRVVILVSKEDHCLGDLLWRWRSGELPVEIAAVISNHDDLRSLVERFGIPFHHVPVTKETKAEAEARLLELIDE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726 164 TEADLVVLARYMQVFSDDIAGRLFGKVINIHHSFLPSFKGARPYHQAHEHGVKLIGATAHYVTADLDEGPIIEQETERVS 243
Cdd:PRK06027 164 YQPDLVVLARYMQILSPDFVARFPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVIRVD 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 499270726 244 HAMSVEDFVAAGRDIESRVLARAVKRHLEARVMLNGRKTVVFA 286
Cdd:PRK06027 244 HRDTAEDLVRAGRDVEKQVLARAVRWHLEDRVLVYGNKTVVFR 286
PRK13011 PRK13011
formyltetrahydrofolate deformylase; Reviewed
1-286 1.16e-141

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 237266 [Multi-domain]  Cd Length: 286  Bit Score: 400.13  E-value: 1.16e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726   1 MTNVAQPFVLTLTCDDRAGIVAAVTSQLHVLGANIVESSQYWDRATNRFFMRIAFNPSGETSADLIERGLAPVLGQFEMQ 80
Cdd:PRK13011   1 MSRRPDTFVLTLSCPSAAGIVAAVTGFLAEHGCYITELHSFDDRLSGRFFMRVEFHSEEGLDEDALRAGFAPIAARFGMQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726  81 GRLIDCRKPQKIVIMISRFDHAFLHLLYQIRVGWLDAEVVAVISNHDDSRETAAWAGIPYHFLPINRENKKKQEDRIFAI 160
Cdd:PRK13011  81 WELHDPAARPKVLIMVSKFDHCLNDLLYRWRIGELPMDIVGVVSNHPDLEPLAAWHGIPFHHFPITPDTKPQQEAQVLDV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726 161 VQETEADLVVLARYMQVFSDDIAGRLFGKVINIHHSFLPSFKGARPYHQAHEHGVKLIGATAHYVTADLDEGPIIEQETE 240
Cdd:PRK13011 161 VEESGAELVVLARYMQVLSPELCRKLAGRAINIHHSFLPGFKGAKPYHQAYERGVKLIGATAHYVTDDLDEGPIIEQDVE 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 499270726 241 RVSHAMSVEDFVAAGRDIESRVLARAVKRHLEARVMLNGRKTVVFA 286
Cdd:PRK13011 241 RVDHAYSPEDLVAKGRDVECLTLARAVKAHIERRVFLNGNRTVVFP 286
purU PRK13010
formyltetrahydrofolate deformylase; Reviewed
2-285 1.24e-127

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 139334 [Multi-domain]  Cd Length: 289  Bit Score: 364.50  E-value: 1.24e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726   2 TNVAQPFVLTLTCDDRAGIVAAVTSQLHVLGANIVESSQYWDRATNRFFMRIAFNPSGET--SADLIERGLAPVLGQFEM 79
Cdd:PRK13010   4 KPRSPSYVLTLACPSAPGIVAAVSGFLAEKGCYIVELTQFDDDESGRFFMRVSFHAQSAEaaSVDTFRQEFQPVAEKFDM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726  80 QGRLIDCRKPQKIVIMISRFDHAFLHLLYQIRVGWLDAEVVAVISNHDDSRETAAWAGIPYHFLPINRENKKKQEDRIFA 159
Cdd:PRK13010  84 QWAIHPDGQRPKVVIMVSKFDHCLNDLLYRWRMGELDMDIVGIISNHPDLQPLAVQHDIPFHHLPVTPDTKAQQEAQILD 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726 160 IVQETEADLVVLARYMQVFSDDIAGRLFGKVINIHHSFLPSFKGARPYHQAHEHGVKLIGATAHYVTADLDEGPIIEQET 239
Cdd:PRK13010 164 LIETSGAELVVLARYMQVLSDDLSRKLSGRAINIHHSFLPGFKGARPYHQAHARGVKLIGATAHFVTDDLDEGPIIEQDV 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 499270726 240 ERVSHAMSVEDFVAAGRDIESRVLARAVKRHLEARVMLNGRKTVVF 285
Cdd:PRK13010 244 ERVDHSYSPEDLVAKGRDVECLTLARAVKAFIEHRVFINGDRTVVF 289
FMT_core_Formyl-FH4-Hydrolase_C cd08648
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ...
90-285 3.95e-108

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: 311.42  E-value: 3.95e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726  90 QKIVIMISRFDHAFLHLLYQIRVGWLDAEVVAVISNHDDSRETAAWAGIPYHFLPINRENKKKQEDRIFAIVQETEADLV 169
Cdd:cd08648    1 KRVAIFVSKEDHCLYDLLHRWREGELPCEIPLVISNHPDLRPLAERFGIPFHHIPVTKDTKAEAEAEQLELLEEYGVDLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726 170 VLARYMQVFSDDIAGRLFGKVINIHHSFLPSFKGARPYHQAHEHGVKLIGATAHYVTADLDEGPIIEQETERVSHAMSVE 249
Cdd:cd08648   81 VLARYMQILSPDFVERYPNRIINIHHSFLPAFKGAKPYHQAFERGVKLIGATAHYVTEELDEGPIIEQDVERVSHRDSVE 160
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 499270726 250 DFVAAGRDIESRVLARAVKRHLEARVMLNGRKTVVF 285
Cdd:cd08648  161 DLVRKGRDIEKQVLARAVKWHLEDRVLVYGNKTVVF 196
PurU TIGR00655
formyltetrahydrofolate deformylase; This model describes formyltetrahydrofolate deformylases. ...
8-285 8.42e-107

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: 311.29  E-value: 8.42e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726    8 FVLTLTCDDRAGIVAAVTSQLHVLGANIVESSQYWDRATNRFFMRIAFNPSGETSA-DLIERGLAPVLGQ-FEMQGRLID 85
Cdd:TIGR00655   1 GILLVSCPDQKGLVAAISTFIAKHGANIISNDQHTDPETGRFFMRVEFQLEGFRLEeSSLLAAFKSALAEkFEMTWELIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726   86 CRKPQKIVIMISRFDHAFLHLLYQIRVGWLDAEVVAVISNHDDSRETAAWAGIPYHFLPINRENKKKQEDRIFAIVQETE 165
Cdd:TIGR00655  81 ADKLKRVAILVSKEDHCLGDLLWRWYSGELDAEIALVISNHEDLRSLVERFGIPFHYIPATKDNRVEHEKRQLELLKQYQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726  166 ADLVVLARYMQVFSDDIAGRLFGKVINIHHSFLPSFKGARPYHQAHEHGVKLIGATAHYVTADLDEGPIIEQETERVSHA 245
Cdd:TIGR00655 161 VDLVVLAKYMQILSPDFVKRYPNKIINIHHSFLPAFIGANPYQRAYERGVKIIGATAHYVTEELDEGPIIEQDVVRVDHT 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 499270726  246 MSVEDFVAAGRDIESRVLARAVKRHLEARVMLNGRKTVVF 285
Cdd:TIGR00655 241 DNVEDLIRAGRDIEKVVLARAVKLHLEDRVFVYENKTVVF 280
PLN02828 PLN02828
formyltetrahydrofolate deformylase
32-285 4.42e-64

formyltetrahydrofolate deformylase


Pssm-ID: 178422  Cd Length: 268  Bit Score: 202.28  E-value: 4.42e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726  32 GANIVESSQYWDRATNRFFMR--IAFNPSGETSAdLIERGLAPVLGQFEMQG---RLIDCRKPQKIVIMISRFDHAFLHL 106
Cdd:PLN02828   9 GGNILGVDVFVPENKNVFYSRseFIFDPVKWPRA-QMDEDFQEISKHFKALKsvvRVPGLDPKYKIAVLASKQDHCLIDL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726 107 LYQIRVGWLDAEVVAVISNHDDSRETAAWA-----GIPYHFLPINRENKKkqEDRIFAIVQETeaDLVVLARYMQVFSDD 181
Cdd:PLN02828  88 LHRWQDGRLPVDITCVISNHERGPNTHVMRflerhGIPYHYLPTTKENKR--EDEILELVKGT--DFLVLARYMQILSGN 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726 182 IAGRLFGKVINIHHSFLPSFKGARPYHQAHEHGVKLIGATAHYVTADLDEGPIIEQETERVSHAMSVEDFVAAGRDIESR 261
Cdd:PLN02828 164 FLKGYGKDIINIHHGLLPSFKGGNPSKQAFDAGVKLIGATSHFVTEELDAGPIIEQMVERVSHRDNLRSFVQKSENLEKQ 243
                        250       260
                 ....*....|....*....|....*
gi 499270726 262 VLARAVKRHLEARVMLNGR-KTVVF 285
Cdd:PLN02828 244 CLAKAIKSYCELRVLPYGTnKTVVF 268
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
89-284 1.08e-44

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: 150.18  E-value: 1.08e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726  89 PQKIVIMISRFDHAFLHLLYQIRVGWLDAEVVAVISNHDDSR--ETAAWAGIPYHFLPINR-ENKKKQEDRIFAIVQETE 165
Cdd:COG0299    1 MKRIAVLISGRGSNLQALIDAIEAGDLPAEIVLVISNRPDAYglERARAAGIPTFVLDHKDfPSREAFDAALLEALDAYG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726 166 ADLVVLARYMQVFSDDIAGRLFGKVINIHHSFLPSFKGARPYHQAHEHGVKLIGATAHYVTADLDEGPIIEQETERVSHA 245
Cdd:COG0299   81 PDLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPD 160
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 499270726 246 MSVEDFVAAGRDIESRVLARAVKRHLEARVMLNGRKTVV 284
Cdd:COG0299  161 DTEETLAARILEQEHRLYPEAIRLLAEGRLTLDGRRVRL 199
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
91-267 2.65e-37

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: 130.49  E-value: 2.65e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726   91 KIVIMISRFDHAFLHLLYQIRVGWLDAEVVAVISNHDD--SRETAAWAGIPYH-FLPINRENKKKQEDRIFAIVQETEAD 167
Cdd:pfam00551   2 KIAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDKaaGLGRAEQAGIPTFvFEHKGLTPRSLFDQELADALRALAAD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726  168 LVVLARYMQVFSDDIAGRLFGKVINIHHSFLPSFKGARPYHQAHEHGVKLIGATAHYVTADLDEGPIIEQETERVSHAMS 247
Cdd:pfam00551  82 VIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDDT 161
                         170       180
                  ....*....|....*....|
gi 499270726  248 VEDFVAAGRDIESRVLARAV 267
Cdd:pfam00551 162 AETLYNRVADLEHKALPRVL 181
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
91-269 5.49e-37

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: 129.43  E-value: 5.49e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726  91 KIVIMISrfdHA---FLHLLYQIRVGWLDAEVVAVISNHDDSR--ETAAWAGIPYHFLP-INRENKKKQEDRIFAIVQET 164
Cdd:cd08645    1 RIAVLAS---GSgsnLQALIDAIKSGKLNAEIVLVISNNPDAYglERAKKAGIPTFVINrKDFPSREEFDEALLELLKEY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726 165 EADLVVLARYMQVFSDDIAGRLFGKVINIHHSFLPSFKGARPYHQAHEHGVKLIGATAHYVTADLDEGPIIEQETERVSH 244
Cdd:cd08645   78 KVDLIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLP 157
                        170       180
                 ....*....|....*....|....*
gi 499270726 245 AMSVEDFVAAGRDIESRVLARAVKR 269
Cdd:cd08645  158 GDTPETLAERIHALEHRLYPEAIKL 182
FMT_core cd08369
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...
101-269 2.78e-32

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: 117.00  E-value: 2.78e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726 101 HAFLHLLYQIrvgwLDAEVVAVISNHDDSRETAAWAGIPYHFLPinRENKKKQEDRIFAIVQETEADLVVLARYMQVFSD 180
Cdd:cd08369   11 QRVLKALLSK----EGHEIVGVVTHPDSPRGTAQLSLELVGGKV--YLDSNINTPELLELLKEFAPDLIVSINFRQIIPP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726 181 DIAGRLFGKVINIHHSFLPSFKGARPYHQAHEHGVKLIGATAHYVTADLDEGPIIEQETERVSHAMSVEDFVAAGRDIES 260
Cdd:cd08369   85 EILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTAGTLYQRLIELGP 164

                 ....*....
gi 499270726 261 RVLARAVKR 269
Cdd:cd08369  165 KLLKEALQK 173
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
91-275 3.04e-31

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: 114.78  E-value: 3.04e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726   91 KIVIMISRFDHAFLHLLYQIRVGWLDAEVVAVISNHDDSR--ETAAWAGIPYH-FLPINRENKKKQEDRIFAIVQETEAD 167
Cdd:TIGR00639   2 RIVVLISGNGSNLQAIIDACKEGKIPASVVLVISNKPDAYglERAAQAGIPTFvLSLKDFPSREAFDQAIIEELRAHEVD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726  168 LVVLARYMQVFSDDIAGRLFGKVINIHHSFLPSFKGARPYHQAHEHGVKLIGATAHYVTADLDEGPIIEQETERVSHAMS 247
Cdd:TIGR00639  82 LVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPEDT 161
                         170       180
                  ....*....|....*....|....*...
gi 499270726  248 VEDFVAAGRDIESRVLARAVKRHLEARV 275
Cdd:TIGR00639 162 EETLEQRIHKQEHRIYPLAIAWFAQGRL 189
ACT_F4HF-DF cd04875
N-terminal ACT domain of formyltetrahydrofolate deformylase (F4HF-DF; formyltetrahydrofolate ...
9-80 5.01e-27

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: 100.33  E-value: 5.01e-27
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499270726   9 VLTLTCDDRAGIVAAVTSQLHVLGANIVESSQYWDRATNRFFMRIAFNPSGET-SADLIERGLAPVLGQFEMQ 80
Cdd:cd04875    1 ILTLSCPDRPGIVAAVSGFLAEHGGNIVESDQFVDPDSGRFFMRVEFELEGFDlSREALEAAFAPVAAEFDMD 73
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
113-275 5.80e-11

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 60.48  E-value: 5.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726 113 GWLDAEVVAVISNHDDSReTAAWA---GIPYHFLPinrenKKKQE------DRIFAIVQETEADLVVLARYMQVFSDDIA 183
Cdd:PLN02331  23 GRVNGDVVVVVTNKPGCG-GAEYArenGIPVLVYP-----KTKGEpdglspDELVDALRGAGVDFVLLAGYLKLIPVELV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726 184 GRLFGKVINIHHSFLPSFkGARPYHQAHEH------GVKLIGATAHYVTADLDEGPIIEQETERVSHAMSVEDFVAAGRD 257
Cdd:PLN02331  97 RAYPRSILNIHPALLPAF-GGKGYYGIKVHkaviasGARYSGPTVHFVDEHYDTGRILAQRVVPVLATDTPEELAARVLH 175
                        170
                 ....*....|....*...
gi 499270726 258 IESRVLARAVKRHLEARV 275
Cdd:PLN02331 176 EEHQLYVEVVAALCEERI 193
FMT_core_like_3 cd08653
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
159-266 5.84e-11

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


Pssm-ID: 187721 [Multi-domain]  Cd Length: 152  Bit Score: 59.53  E-value: 5.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726 159 AIVQETEADLVVLaRYMQVFSDDIAGRLFGKVINIHHSFLPSFKGARP-YHQAHEHGVKLIGATAHYVTADLDEGPIIEQ 237
Cdd:cd08653   41 AALRALAPDVVSV-YGCGIIKDALLAIPPLGVLNLHGGILPDYRGVHTgFWALANGDPDNVGVTVHLVDAGIDTGDVLAQ 119
                         90       100       110
                 ....*....|....*....|....*....|...
gi 499270726 238 ETERVSHAMSVEDF----VAAGRDIESRVLARA 266
Cdd:cd08653  120 ARPPLAAGDTLLSLylrlYRAGVELMVEAIADL 152
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
118-250 7.93e-10

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


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 58.58  E-value: 7.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726 118 EVVAVISNHDDSR------------ETAAWAGIPYhFLPinrENKKKQEdrIFAIVQETEADLVVLARYMQVFSDDI--A 183
Cdd:COG0223   25 EVVAVVTQPDRPAgrgrkltpspvkELALEHGIPV-LQP---ESLKDPE--FLEELRALNPDLIVVVAYGQILPKEVldI 98
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499270726 184 GRLfgKVINIHHSFLPSFKGARPYHQAHEHGVKLIGATAHYVTADLDEGPIIEQETERVSHAMSVED 250
Cdd:COG0223   99 PRL--GCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDTGDILLQEEVPIGPDDTAGS 163
FMT_core_ArnA_N cd08644
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ...
115-238 2.44e-09

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: 55.81  E-value: 2.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726 115 LDAEVVAVISNHDDSRE---------TAAWAGIPYhFLPINrENKKKQEDRIfaivQETEADLVVLARYMQVFSDDI--A 183
Cdd:cd08644   22 AGFEVVAVFTHTDNPGEniwfgsvaqLAREHGIPV-FTPDD-INHPEWVERL----RALKPDLIFSFYYRHMISEDIleI 95
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 499270726 184 GRLfgKVINIHHSFLPSFKGARPYHQAHEHGVKLIGATAHYVTADLDEGPIIEQE 238
Cdd:cd08644   96 ARL--GAFNLHGSLLPKYRGRAPLNWALINGETETGVTLHRMTKKPDAGAIVDQE 148
PLN02285 PLN02285
methionyl-tRNA formyltransferase
118-242 5.51e-08

methionyl-tRNA formyltransferase


Pssm-ID: 215159 [Multi-domain]  Cd Length: 334  Bit Score: 53.16  E-value: 5.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726 118 EVVAVISNHDDSR------------ETAAWAGIPYH--FLPinrenKKKQEDRIFAIVQETEADLVVLARYMQVFSD--- 180
Cdd:PLN02285  37 EVAAVVTQPPARRgrgrklmpspvaQLALDRGFPPDliFTP-----EKAGEEDFLSALRELQPDLCITAAYGNILPQkfl 111
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499270726 181 DIAGrlFGKViNIHHSFLPSFKGARPYHQAHEHGVKLIGATAHYVTADLDEGPIIEQETERV 242
Cdd:PLN02285 112 DIPK--LGTV-NIHPSLLPLYRGAAPVQRALQDGVNETGVSVAFTVRALDAGPVIAQERVEV 170
FMT_core_Met-tRNA-FMT_N cd08646
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ...
118-239 2.11e-07

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: 50.13  E-value: 2.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726 118 EVVAVISNHDDSR---------ETAAWA---GIPYHflpinRENKKKQEDrIFAIVQETEADLVVLARYmqvfsddiaGR 185
Cdd:cd08646   25 EVVAVVTQPDKPRgrgkkltpsPVKELAlelGLPVL-----QPEKLKDEE-FLEELKALKPDLIVVVAY---------GQ 89
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499270726 186 LFGK---------VINIHHSFLPSFKGARPYHQAHEHGVKLIGATAHYVTADLDEGPIIEQET 239
Cdd:cd08646   90 ILPKeildlppygCINVHPSLLPKYRGAAPIQRAILNGDKETGVTIMKMDEGLDTGDILAQEE 152
PRK06988 PRK06988
formyltransferase;
117-238 1.06e-06

formyltransferase;


Pssm-ID: 235902 [Multi-domain]  Cd Length: 312  Bit Score: 49.31  E-value: 1.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726 117 AEVVAVISnHDDS----------RETAAWAGIPYhflpINRENKKKQEDRifAIVQETEADLVVLARYMQVFSDDIAGRL 186
Cdd:PRK06988  26 VDVALVVT-HEDNpteniwfgsvAAVAAEHGIPV----ITPADPNDPELR--AAVAAAAPDFIFSFYYRHMIPVDLLALA 98
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 499270726 187 FGKVINIHHSFLPSFKGARPYHQAHEHGVKLIGATAHYVTADLDEGPIIEQE 238
Cdd:PRK06988  99 PRGAYNMHGSLLPKYRGRVPVNWAVLNGETETGATLHEMVAKPDAGAIVDQT 150
FMT_core_like_5 cd08823
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
120-239 3.39e-06

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


Pssm-ID: 187725 [Multi-domain]  Cd Length: 177  Bit Score: 46.28  E-value: 3.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726 120 VAVISNHDDSretaawagIPYHFL---PINRENK--------KKQedrIFAIVQETEADLVVLARYMQVFSDDIAGRLFG 188
Cdd:cd08823   26 IAVPAHNASY--------FPQIFVftgIRRLVSKqrvdtanlKEQ---LAEWLRALAADTVVVFTFPYRIPQHILDLPPL 94
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 499270726 189 KVINIHHSFLPSFKGARPYHQAHEHGVKLIGATAHYVTADLDEGPIIEQET 239
Cdd:cd08823   95 GFYNLHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMTAEIDRGPIVLEQF 145
PRK08125 PRK08125
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ...
118-238 3.98e-05

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


Pssm-ID: 236156 [Multi-domain]  Cd Length: 660  Bit Score: 44.97  E-value: 3.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726 118 EVVAVISNHDDSRE---------TAAWAGIPYhFLPINrENKKKQEDRIfaivQETEADLVVLARYMQVFSDDIAGRLFG 188
Cdd:PRK08125  25 EIAAVFTHTDNPGEnhffgsvarLAAELGIPV-YAPED-VNHPLWVERI----RELAPDVIFSFYYRNLLSDEILQLAPA 98
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 499270726 189 KVINIHHSFLPSFKGARPYHQAHEHGVKLIGATAHYVTADLDEGPIIEQE 238
Cdd:PRK08125  99 GAFNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQQ 148
GcvR COG2716
Glycine cleavage system regulator GcvR [Amino acid transport and metabolism];
8-40 5.59e-05

Glycine cleavage system regulator GcvR [Amino acid transport and metabolism];


Pssm-ID: 442029 [Multi-domain]  Cd Length: 174  Bit Score: 42.90  E-value: 5.59e-05
                         10        20        30
                 ....*....|....*....|....*....|...
gi 499270726   8 FVLTLTCDDRAGIVAAVTSQLHVLGANIVESSQ 40
Cdd:COG2716    4 LVITAIGPDRPGIVAALARAVSEHGCNILDSRM 36
GcvR COG2716
Glycine cleavage system regulator GcvR [Amino acid transport and metabolism];
5-67 8.79e-05

Glycine cleavage system regulator GcvR [Amino acid transport and metabolism];


Pssm-ID: 442029 [Multi-domain]  Cd Length: 174  Bit Score: 42.13  E-value: 8.79e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499270726   5 AQPFVLTLTCDDRAGIVAAVTSQLHVLGANIVE------SSQYWDraTNRFFMRIAFN-PSGETSADLIE 67
Cdd:COG2716   88 GLPYVVEVVGNDRPGIVAEVTQFLAERGINIEDlstktyPAPMSG--TPLFSAQITVHvPAGLDIDALRD 155
ACT_6 pfam13740
ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains.
6-40 2.94e-03

ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains.


Pssm-ID: 433446 [Multi-domain]  Cd Length: 76  Bit Score: 35.61  E-value: 2.94e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 499270726    6 QPFVLTLTCDDRAGIVAAVTSQLHVLGANIVESSQ 40
Cdd:pfam13740   1 EILLITATGPDRPGLTASLTAVLAEHGCNILDSGQ 35
ACT cd02116
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
10-53 7.19e-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: 34.19  E-value: 7.19e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 499270726  10 LTLTCDDRAGIVAAVTSQLHVLGANIVESSQY--WDRATNRFFMRI 53
Cdd:cd02116    1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRtsGDGGEADIFIVV 46
PRK00194 PRK00194
ACT domain-containing protein;
8-40 9.74e-03

ACT domain-containing protein;


Pssm-ID: 178923 [Multi-domain]  Cd Length: 90  Bit Score: 34.79  E-value: 9.74e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 499270726   8 FVLTLTCDDRAGIVAAVTSQLHVLGANIVESSQ 40
Cdd:PRK00194   4 AIITVIGKDKVGIIAGVSTVLAELNVNILDISQ 36
 
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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