|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13011 |
PRK13011 |
formyltetrahydrofolate deformylase; Reviewed |
1-285 |
0e+00 |
|
formyltetrahydrofolate deformylase; Reviewed
Pssm-ID: 237266 [Multi-domain] Cd Length: 286 Bit Score: 571.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 1 MSRAPDTWILTADCPSVLGTVDAVTRFLFEQGCYVTEHHSFDDRLSARFFIRVEFRQPENFNEQGLRDGLAERARAFDMN 80
Cdd:PRK13011 1 MSRRPDTFVLTLSCPSAAGIVAAVTGFLAEHGCYITELHSFDDRLSGRFFMRVEFHSEEGLDEDALRAGFAPIAARFGMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 81 VELTPPQHRPKVVIMVSKADHCLNDLLYRQRIGQLAMDVVAVVSNHPDLKPLADWHQIPYYHFPLDPNDKPSQERQVWQV 160
Cdd:PRK13011 81 WELHDPAARPKVLIMVSKFDHCLNDLLYRWRIGELPMDIVGVVSNHPDLEPLAAWHGIPFHHFPITPDTKPQQEAQVLDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 161 IEDSGAELVILARYMQVLSPELCRKLDGKAINIHHSLLPGFKGAKPYHQAYNKGVKLVGATAHYINNDLDEGPIIAQGVE 240
Cdd:PRK13011 161 VEESGAELVVLARYMQVLSPELCRKLAGRAINIHHSFLPGFKGAKPYHQAYERGVKLIGATAHYVTDDLDEGPIIEQDVE 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1329358581 241 VVDHSHYPEDLIAKGRDIEGLTLARAVGYHIERRVFLNANRTVVL 285
Cdd:PRK13011 241 RVDHAYSPEDLVAKGRDVECLTLARAVKAHIERRVFLNGNRTVVF 285
|
|
| PurU |
COG0788 |
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ... |
5-285 |
6.50e-176 |
|
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: 486.48 E-value: 6.50e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 5 PDTWILTADCPSVLGTVDAVTRFLFEQGCYVTEHHSFDDRLSARFFIRVEFRQPE-NFNEQGLRDGLAERARAFDMNVEL 83
Cdd:COG0788 1 MTTYILTLSCPDRPGIVAAVTGFLAEHGGNITEADQFVDPETGRFFMRVEFEAPGlDFDLEALRAAFAPLAERFGMDWRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 84 TPPQHRPKVVIMVSKADHCLNDLLYRQRIGQLAMDVVAVVSNHPDLKPLADWHQIPYYHFPLDPNDKPSQERQVWQVIED 163
Cdd:COG0788 81 HDSDRRKRVAILVSKEDHCLNDLLYRWRSGELPAEIPAVISNHPDLRPLAEWFGIPFHHIPVTKETKAEAEARLLELLEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 164 SGAELVILARYMQVLSPELCRKLDGKAINIHHSLLPGFKGAKPYHQAYNKGVKLVGATAHYINNDLDEGPIIAQGVEVVD 243
Cdd:COG0788 161 YDIDLVVLARYMQILSPDFCARLPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVERVD 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1329358581 244 HSHYPEDLIAKGRDIEGLTLARAVGYHIERRVFLNANRTVVL 285
Cdd:COG0788 241 HRDTPEDLVRKGRDVEKRVLARAVRWHLEDRVLVNGNKTVVF 282
|
|
| FMT_core_Formyl-FH4-Hydrolase_C |
cd08648 |
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ... |
90-285 |
1.53e-118 |
|
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: 338.00 E-value: 1.53e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 90 PKVVIMVSKADHCLNDLLYRQRIGQLAMDVVAVVSNHPDLKPLADWHQIPYYHFPLDPNDKPSQERQVWQVIEDSGAELV 169
Cdd:cd08648 1 KRVAIFVSKEDHCLYDLLHRWREGELPCEIPLVISNHPDLRPLAERFGIPFHHIPVTKDTKAEAEAEQLELLEEYGVDLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 170 ILARYMQVLSPELCRKLDGKAINIHHSLLPGFKGAKPYHQAYNKGVKLVGATAHYINNDLDEGPIIAQGVEVVDHSHYPE 249
Cdd:cd08648 81 VLARYMQILSPDFVERYPNRIINIHHSFLPAFKGAKPYHQAFERGVKLIGATAHYVTEELDEGPIIEQDVERVSHRDSVE 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1329358581 250 DLIAKGRDIEGLTLARAVGYHIERRVFLNANRTVVL 285
Cdd:cd08648 161 DLVRKGRDIEKQVLARAVKWHLEDRVLVYGNKTVVF 196
|
|
| PurU |
TIGR00655 |
formyltetrahydrofolate deformylase; This model describes formyltetrahydrofolate deformylases. ... |
9-285 |
1.16e-99 |
|
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: 293.18 E-value: 1.16e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 9 ILTADCPSVLGTVDAVTRFLFEQGCYVTEHHSFDDRLSARFFIRVEFRQPEN-FNEQGLRDGLAER-ARAFDMNVELTPP 86
Cdd:TIGR00655 2 ILLVSCPDQKGLVAAISTFIAKHGANIISNDQHTDPETGRFFMRVEFQLEGFrLEESSLLAAFKSAlAEKFEMTWELILA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 87 QHRPKVVIMVSKADHCLNDLLYRQRIGQLAMDVVAVVSNHPDLKPLADWHQIPYYHFPLDPNDKPSQERQVWQVIEDSGA 166
Cdd:TIGR00655 82 DKLKRVAILVSKEDHCLGDLLWRWYSGELDAEIALVISNHEDLRSLVERFGIPFHYIPATKDNRVEHEKRQLELLKQYQV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 167 ELVILARYMQVLSPELCRKLDGKAINIHHSLLPGFKGAKPYHQAYNKGVKLVGATAHYINNDLDEGPIIAQGVEVVDHSH 246
Cdd:TIGR00655 162 DLVVLAKYMQILSPDFVKRYPNKIINIHHSFLPAFIGANPYQRAYERGVKIIGATAHYVTEELDEGPIIEQDVVRVDHTD 241
|
250 260 270
....*....|....*....|....*....|....*....
gi 1329358581 247 YPEDLIAKGRDIEGLTLARAVGYHIERRVFLNANRTVVL 285
Cdd:TIGR00655 242 NVEDLIRAGRDIEKVVLARAVKLHLEDRVFVYENKTVVF 280
|
|
| Formyl_trans_N |
pfam00551 |
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ... |
91-267 |
2.39e-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: 2.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 91 KVVIMVSKADHCLNDLLYRQRIGQLAMDVVAVVSNHPDLKPL--ADWHQIPYYHFPLDPNDKPSQ-ERQVWQVIEDSGAE 167
Cdd:pfam00551 2 KIAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLgrAEQAGIPTFVFEHKGLTPRSLfDQELADALRALAAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 168 LVILARYMQVLSPELCRKLDGKAINIHHSLLPGFKGAKPYHQAYNKGVKLVGATAHYINNDLDEGPIIAQGVEVVDHSHY 247
Cdd:pfam00551 82 VIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDDT 161
|
170 180
....*....|....*....|
gi 1329358581 248 PEDLIAKGRDIEGLTLARAV 267
Cdd:pfam00551 162 AETLYNRVADLEHKALPRVL 181
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13011 |
PRK13011 |
formyltetrahydrofolate deformylase; Reviewed |
1-285 |
0e+00 |
|
formyltetrahydrofolate deformylase; Reviewed
Pssm-ID: 237266 [Multi-domain] Cd Length: 286 Bit Score: 571.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 1 MSRAPDTWILTADCPSVLGTVDAVTRFLFEQGCYVTEHHSFDDRLSARFFIRVEFRQPENFNEQGLRDGLAERARAFDMN 80
Cdd:PRK13011 1 MSRRPDTFVLTLSCPSAAGIVAAVTGFLAEHGCYITELHSFDDRLSGRFFMRVEFHSEEGLDEDALRAGFAPIAARFGMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 81 VELTPPQHRPKVVIMVSKADHCLNDLLYRQRIGQLAMDVVAVVSNHPDLKPLADWHQIPYYHFPLDPNDKPSQERQVWQV 160
Cdd:PRK13011 81 WELHDPAARPKVLIMVSKFDHCLNDLLYRWRIGELPMDIVGVVSNHPDLEPLAAWHGIPFHHFPITPDTKPQQEAQVLDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 161 IEDSGAELVILARYMQVLSPELCRKLDGKAINIHHSLLPGFKGAKPYHQAYNKGVKLVGATAHYINNDLDEGPIIAQGVE 240
Cdd:PRK13011 161 VEESGAELVVLARYMQVLSPELCRKLAGRAINIHHSFLPGFKGAKPYHQAYERGVKLIGATAHYVTDDLDEGPIIEQDVE 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1329358581 241 VVDHSHYPEDLIAKGRDIEGLTLARAVGYHIERRVFLNANRTVVL 285
Cdd:PRK13011 241 RVDHAYSPEDLVAKGRDVECLTLARAVKAHIERRVFLNGNRTVVF 285
|
|
| PurU |
COG0788 |
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ... |
5-285 |
6.50e-176 |
|
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: 486.48 E-value: 6.50e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 5 PDTWILTADCPSVLGTVDAVTRFLFEQGCYVTEHHSFDDRLSARFFIRVEFRQPE-NFNEQGLRDGLAERARAFDMNVEL 83
Cdd:COG0788 1 MTTYILTLSCPDRPGIVAAVTGFLAEHGGNITEADQFVDPETGRFFMRVEFEAPGlDFDLEALRAAFAPLAERFGMDWRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 84 TPPQHRPKVVIMVSKADHCLNDLLYRQRIGQLAMDVVAVVSNHPDLKPLADWHQIPYYHFPLDPNDKPSQERQVWQVIED 163
Cdd:COG0788 81 HDSDRRKRVAILVSKEDHCLNDLLYRWRSGELPAEIPAVISNHPDLRPLAEWFGIPFHHIPVTKETKAEAEARLLELLEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 164 SGAELVILARYMQVLSPELCRKLDGKAINIHHSLLPGFKGAKPYHQAYNKGVKLVGATAHYINNDLDEGPIIAQGVEVVD 243
Cdd:COG0788 161 YDIDLVVLARYMQILSPDFCARLPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVERVD 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1329358581 244 HSHYPEDLIAKGRDIEGLTLARAVGYHIERRVFLNANRTVVL 285
Cdd:COG0788 241 HRDTPEDLVRKGRDVEKRVLARAVRWHLEDRVLVNGNKTVVF 282
|
|
| purU |
PRK06027 |
formyltetrahydrofolate deformylase; Reviewed |
6-285 |
6.02e-159 |
|
formyltetrahydrofolate deformylase; Reviewed
Pssm-ID: 235676 [Multi-domain] Cd Length: 286 Bit Score: 443.78 E-value: 6.02e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 6 DTWILTADCPSVLGTVDAVTRFLFEQGCYVTEHHSFDDRLSARFFIRVEFRQPE-NFNEQGLRDGLAERARAFDMNVELT 84
Cdd:PRK06027 5 QRYVLTLSCPDRPGIVAAVSNFLYEHGGNIVDADQFVDPETGRFFMRVEFEGDGlIFNLETLRADFAALAEEFEMDWRLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 85 PPQHRPKVVIMVSKADHCLNDLLYRQRIGQLAMDVVAVVSNHPDLKPLADWHQIPYYHFPLDPNDKPSQERQVWQVIEDS 164
Cdd:PRK06027 85 DSAERKRVVILVSKEDHCLGDLLWRWRSGELPVEIAAVISNHDDLRSLVERFGIPFHHVPVTKETKAEAEARLLELIDEY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 165 GAELVILARYMQVLSPELCRKLDGKAINIHHSLLPGFKGAKPYHQAYNKGVKLVGATAHYINNDLDEGPIIAQGVEVVDH 244
Cdd:PRK06027 165 QPDLVVLARYMQILSPDFVARFPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVIRVDH 244
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1329358581 245 SHYPEDLIAKGRDIEGLTLARAVGYHIERRVFLNANRTVVL 285
Cdd:PRK06027 245 RDTAEDLVRAGRDVEKQVLARAVRWHLEDRVLVYGNKTVVF 285
|
|
| purU |
PRK13010 |
formyltetrahydrofolate deformylase; Reviewed |
1-285 |
1.16e-154 |
|
formyltetrahydrofolate deformylase; Reviewed
Pssm-ID: 139334 [Multi-domain] Cd Length: 289 Bit Score: 433.07 E-value: 1.16e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 1 MSRAPdTWILTADCPSVLGTVDAVTRFLFEQGCYVTEHHSFDDRLSARFFIRVEFRQP--ENFNEQGLRDGLAERARAFD 78
Cdd:PRK13010 4 KPRSP-SYVLTLACPSAPGIVAAVSGFLAEKGCYIVELTQFDDDESGRFFMRVSFHAQsaEAASVDTFRQEFQPVAEKFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 79 MNVELTPPQHRPKVVIMVSKADHCLNDLLYRQRIGQLAMDVVAVVSNHPDLKPLADWHQIPYYHFPLDPNDKPSQERQVW 158
Cdd:PRK13010 83 MQWAIHPDGQRPKVVIMVSKFDHCLNDLLYRWRMGELDMDIVGIISNHPDLQPLAVQHDIPFHHLPVTPDTKAQQEAQIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 159 QVIEDSGAELVILARYMQVLSPELCRKLDGKAINIHHSLLPGFKGAKPYHQAYNKGVKLVGATAHYINNDLDEGPIIAQG 238
Cdd:PRK13010 163 DLIETSGAELVVLARYMQVLSDDLSRKLSGRAINIHHSFLPGFKGARPYHQAHARGVKLIGATAHFVTDDLDEGPIIEQD 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1329358581 239 VEVVDHSHYPEDLIAKGRDIEGLTLARAVGYHIERRVFLNANRTVVL 285
Cdd:PRK13010 243 VERVDHSYSPEDLVAKGRDVECLTLARAVKAFIEHRVFINGDRTVVF 289
|
|
| FMT_core_Formyl-FH4-Hydrolase_C |
cd08648 |
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ... |
90-285 |
1.53e-118 |
|
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: 338.00 E-value: 1.53e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 90 PKVVIMVSKADHCLNDLLYRQRIGQLAMDVVAVVSNHPDLKPLADWHQIPYYHFPLDPNDKPSQERQVWQVIEDSGAELV 169
Cdd:cd08648 1 KRVAIFVSKEDHCLYDLLHRWREGELPCEIPLVISNHPDLRPLAERFGIPFHHIPVTKDTKAEAEAEQLELLEEYGVDLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 170 ILARYMQVLSPELCRKLDGKAINIHHSLLPGFKGAKPYHQAYNKGVKLVGATAHYINNDLDEGPIIAQGVEVVDHSHYPE 249
Cdd:cd08648 81 VLARYMQILSPDFVERYPNRIINIHHSFLPAFKGAKPYHQAFERGVKLIGATAHYVTEELDEGPIIEQDVERVSHRDSVE 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1329358581 250 DLIAKGRDIEGLTLARAVGYHIERRVFLNANRTVVL 285
Cdd:cd08648 161 DLVRKGRDIEKQVLARAVKWHLEDRVLVYGNKTVVF 196
|
|
| PurU |
TIGR00655 |
formyltetrahydrofolate deformylase; This model describes formyltetrahydrofolate deformylases. ... |
9-285 |
1.16e-99 |
|
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: 293.18 E-value: 1.16e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 9 ILTADCPSVLGTVDAVTRFLFEQGCYVTEHHSFDDRLSARFFIRVEFRQPEN-FNEQGLRDGLAER-ARAFDMNVELTPP 86
Cdd:TIGR00655 2 ILLVSCPDQKGLVAAISTFIAKHGANIISNDQHTDPETGRFFMRVEFQLEGFrLEESSLLAAFKSAlAEKFEMTWELILA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 87 QHRPKVVIMVSKADHCLNDLLYRQRIGQLAMDVVAVVSNHPDLKPLADWHQIPYYHFPLDPNDKPSQERQVWQVIEDSGA 166
Cdd:TIGR00655 82 DKLKRVAILVSKEDHCLGDLLWRWYSGELDAEIALVISNHEDLRSLVERFGIPFHYIPATKDNRVEHEKRQLELLKQYQV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 167 ELVILARYMQVLSPELCRKLDGKAINIHHSLLPGFKGAKPYHQAYNKGVKLVGATAHYINNDLDEGPIIAQGVEVVDHSH 246
Cdd:TIGR00655 162 DLVVLAKYMQILSPDFVKRYPNKIINIHHSFLPAFIGANPYQRAYERGVKIIGATAHYVTEELDEGPIIEQDVVRVDHTD 241
|
250 260 270
....*....|....*....|....*....|....*....
gi 1329358581 247 YPEDLIAKGRDIEGLTLARAVGYHIERRVFLNANRTVVL 285
Cdd:TIGR00655 242 NVEDLIRAGRDIEKVVLARAVKLHLEDRVFVYENKTVVF 280
|
|
| PLN02828 |
PLN02828 |
formyltetrahydrofolate deformylase |
91-285 |
1.14e-52 |
|
formyltetrahydrofolate deformylase
Pssm-ID: 178422 Cd Length: 268 Bit Score: 173.01 E-value: 1.14e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 91 KVVIMVSKADHCLNDLLYRQRIGQLAMDVVAVVSNH---PD--LKPLADWHQIPYYHFPLDPNDKpsQERQVWQVIedSG 165
Cdd:PLN02828 72 KIAVLASKQDHCLIDLLHRWQDGRLPVDITCVISNHergPNthVMRFLERHGIPYHYLPTTKENK--REDEILELV--KG 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 166 AELVILARYMQVLSPELCRKLDGKAINIHHSLLPGFKGAKPYHQAYNKGVKLVGATAHYINNDLDEGPIIAQGVEVVDHS 245
Cdd:PLN02828 148 TDFLVLARYMQILSGNFLKGYGKDIINIHHGLLPSFKGGNPSKQAFDAGVKLIGATSHFVTEELDAGPIIEQMVERVSHR 227
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1329358581 246 HYPEDLIAKGRDIEGLTLARAVGYHIERRVFLNA-NRTVVL 285
Cdd:PLN02828 228 DNLRSFVQKSENLEKQCLAKAIKSYCELRVLPYGtNKTVVF 268
|
|
| Formyl_trans_N |
pfam00551 |
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ... |
91-267 |
2.39e-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: 2.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 91 KVVIMVSKADHCLNDLLYRQRIGQLAMDVVAVVSNHPDLKPL--ADWHQIPYYHFPLDPNDKPSQ-ERQVWQVIEDSGAE 167
Cdd:pfam00551 2 KIAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLgrAEQAGIPTFVFEHKGLTPRSLfDQELADALRALAAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 168 LVILARYMQVLSPELCRKLDGKAINIHHSLLPGFKGAKPYHQAYNKGVKLVGATAHYINNDLDEGPIIAQGVEVVDHSHY 247
Cdd:pfam00551 82 VIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDDT 161
|
170 180
....*....|....*....|
gi 1329358581 248 PEDLIAKGRDIEGLTLARAV 267
Cdd:pfam00551 162 AETLYNRVADLEHKALPRVL 181
|
|
| PurN |
COG0299 |
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ... |
89-284 |
2.23e-36 |
|
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: 128.61 E-value: 2.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 89 RPKVVIMVS------KAdhclndLLYRQRIGQLAMDVVAVVSNHPDLKPL--ADWHQIPYYHfpLDPNDKPSQE---RQV 157
Cdd:COG0299 1 MKRIAVLISgrgsnlQA------LIDAIEAGDLPAEIVLVISNRPDAYGLerARAAGIPTFV--LDHKDFPSREafdAAL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 158 WQVIEDSGAELVILARYMQVLSPELCRKLDGKAINIHHSLLPGFKGAKPYHQAYNKGVKLVGATAHYINNDLDEGPIIAQ 237
Cdd:COG0299 73 LEALDAYGPDLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQ 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1329358581 238 GVEVVDHSHYPEDLIAKGRDIEGLTLARAVGYHIERRVFLNANRTVV 284
Cdd:COG0299 153 AAVPVLPDDTEETLAARILEQEHRLYPEAIRLLAEGRLTLDGRRVRL 199
|
|
| FMT_core_GART |
cd08645 |
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ... |
91-249 |
1.58e-35 |
|
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: 125.96 E-value: 1.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 91 KVVIMVS------KAdhclndLLYRQRIGQLAMDVVAVVSNHPDLKPL--ADWHQIPYYHFPL-DPNDKPSQERQVWQVI 161
Cdd:cd08645 1 RIAVLASgsgsnlQA------LIDAIKSGKLNAEIVLVISNNPDAYGLerAKKAGIPTFVINRkDFPSREEFDEALLELL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 162 EDSGAELVILARYMQVLSPELCRKLDGKAINIHHSLLPGFKGAKPYHQAYNKGVKLVGATAHYINNDLDEGPIIAQG-VE 240
Cdd:cd08645 75 KEYKVDLIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAaVP 154
|
170 180
....*....|....*....|....
gi 1329358581 241 VVD---------------HSHYPE 249
Cdd:cd08645 155 VLPgdtpetlaerihaleHRLYPE 178
|
|
| FMT_core |
cd08369 |
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ... |
118-267 |
2.52e-28 |
|
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The proteins of this superfamily contain a formyltransferase domain that hydrolyzes the removal of a formyl group from its substrate as part of a multistep transfer mechanism, and this alignment model represents the catalytic core of the formyltransferase domain. This family includes the following known members; Glycinamide Ribonucleotide Transformylase (GART), Formyl-FH4 Hydrolase, Methionyl-tRNA Formyltransferase, ArnA, and 10-Formyltetrahydrofolate Dehydrogenase (FDH). Glycinamide Ribonucleotide Transformylase (GART) catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyl-FH4 Hydrolase catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate. Methionyl-tRNA Formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA, which plays important role in translation initiation. ArnA is required for the modification of lipid A with 4-amino-4-deoxy-l-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. 10-formyltetrahydrofolate dehydrogenase (FDH) catalyzes the conversion of 10-formyltetrahydrofolate, a precursor for nucleotide biosynthesis, to tetrahydrofolate. Members of this family are multidomain proteins. The formyltransferase domain is located at the N-terminus of FDH, Methionyl-tRNA Formyltransferase and ArnA, and at the C-terminus of Formyl-FH4 Hydrolase. Prokaryotic Glycinamide Ribonucleotide Transformylase (GART) is a single domain protein while eukaryotic GART is a trifunctional protein that catalyzes the second, third and fifth steps in de novo purine biosynthesis.
Pssm-ID: 187712 [Multi-domain] Cd Length: 173 Bit Score: 106.60 E-value: 2.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 118 DVVAVVSNHPDLKPLADWHQIPYYHFPLDPNDKPSQErqVWQVIEDSGAELVILARYMQVLSPELCRKLDGKAINIHHSL 197
Cdd:cd08369 24 EIVGVVTHPDSPRGTAQLSLELVGGKVYLDSNINTPE--LLELLKEFAPDLIVSINFRQIIPPEILKLPPGGAINIHPSL 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 198 LPGFKGAKPYHQAYNKGVKLVGATAHYINNDLDEGPIIAQGVEVVDHSHYPEDLIAKGRDIEGLTLARAV 267
Cdd:cd08369 102 LPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTAGTLYQRLIELGPKLLKEAL 171
|
|
| PurN |
TIGR00639 |
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ... |
91-244 |
3.46e-27 |
|
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: 104.38 E-value: 3.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 91 KVVIMVSKADHCLNDLLYRQRIGQLAMDVVAVVSNHPDLKPL--ADWHQIPyyHFPLDPNDKPSqeRQVWQV-----IED 163
Cdd:TIGR00639 2 RIVVLISGNGSNLQAIIDACKEGKIPASVVLVISNKPDAYGLerAAQAGIP--TFVLSLKDFPS--REAFDQaiieeLRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 164 SGAELVILARYMQVLSPELCRKLDGKAINIHHSLLPGFKGAKPYHQAYNKGVKLVGATAHYINNDLDEGPIIAQG-VEVV 242
Cdd:TIGR00639 78 HEVDLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAkVPIL 157
|
..
gi 1329358581 243 DH 244
Cdd:TIGR00639 158 PE 159
|
|
| ACT_F4HF-DF |
cd04875 |
N-terminal ACT domain of formyltetrahydrofolate deformylase (F4HF-DF; formyltetrahydrofolate ... |
9-81 |
1.05e-24 |
|
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: 94.16 E-value: 1.05e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1329358581 9 ILTADCPSVLGTVDAVTRFLFEQGCYVTEHHSFDDRLSARFFIRVEFRQPE-NFNEQGLRDGLAERARAFDMNV 81
Cdd:cd04875 1 ILTLSCPDRPGIVAAVSGFLAEHGGNIVESDQFVDPDSGRFFMRVEFELEGfDLSREALEAAFAPVAAEFDMDW 74
|
|
| PLN02331 |
PLN02331 |
phosphoribosylglycinamide formyltransferase |
118-276 |
1.87e-19 |
|
phosphoribosylglycinamide formyltransferase
Pssm-ID: 177965 [Multi-domain] Cd Length: 207 Bit Score: 83.97 E-value: 1.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 118 DVVAVVSNHPDLKPlADW---HQIPYYHFP--------LDPNDKPSQERqvwqvieDSGAELVILARYMQVLSPELCRKL 186
Cdd:PLN02331 28 DVVVVVTNKPGCGG-AEYareNGIPVLVYPktkgepdgLSPDELVDALR-------GAGVDFVLLAGYLKLIPVELVRAY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 187 DGKAINIHHSLLPGFKGAKPY----HQAY-NKGVKLVGATAHYINNDLDEGPIIAQGVEVVDHSHYPEDLIAKGRDIEGL 261
Cdd:PLN02331 100 PRSILNIHPALLPAFGGKGYYgikvHKAViASGARYSGPTVHFVDEHYDTGRILAQRVVPVLATDTPEELAARVLHEEHQ 179
|
170
....*....|....*
gi 1329358581 262 TLARAVGYHIERRVF 276
Cdd:PLN02331 180 LYVEVVAALCEERIV 194
|
|
| fmt |
TIGR00460 |
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ... |
99-254 |
1.71e-13 |
|
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than methionyl-tRNA formyltransferase (fmt) itself are formyltetrahydrofolate dehydrogenases. The mitochondrial methionyl-tRNA formyltransferases are so divergent that, in a multiple alignment of bacterial fmt, mitochondrial fmt, and formyltetrahydrofolate dehydrogenases, the mitochondrial fmt appears the most different. However, because both bacterial and mitochondrial fmt are included in the seed alignment, all credible fmt sequences score higher than any non-fmt sequence. This enzyme modifies Met on initiator tRNA to f-Met. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273088 [Multi-domain] Cd Length: 313 Bit Score: 69.35 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 99 ADHCLNDLLYRQrigqlaMDVVAVVSN------------HPDLKPLADWHQIPYYhfpldpndKPSQERQ--VWQVIEDS 164
Cdd:TIGR00460 12 SLPVLEELREDN------FEVVGVVTQpdkpagrgkkltPPPVKVLAEEKGIPVF--------QPEKQRQleELPLVREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 165 GAELVILARYMQVLSPELCRKLDGKAINIHHSLLPGFKGAKPYHQAYNKGVKLVGATAHYINNDLDEGPIIAQ---GVEV 241
Cdd:TIGR00460 78 KPDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVPKMDAGDILKQetfPIEE 157
|
170
....*....|...
gi 1329358581 242 VDHSHYPEDLIAK 254
Cdd:TIGR00460 158 EDNSGTLSDKLSE 170
|
|
| Fmt |
COG0223 |
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis]; |
118-237 |
2.05e-13 |
|
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439993 [Multi-domain] Cd Length: 308 Bit Score: 68.98 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 118 DVVAVVSnHPD-------------LKPLADWHQIPYYHfPLDPNDKPSQERqvwqvIEDSGAELVILARYMQVLSPELcr 184
Cdd:COG0223 25 EVVAVVT-QPDrpagrgrkltpspVKELALEHGIPVLQ-PESLKDPEFLEE-----LRALNPDLIVVVAYGQILPKEV-- 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1329358581 185 kLD---GKAINIHHSLLPGFKGAKPYHQAYNKGVKLVGATAHYINNDLDEGPIIAQ 237
Cdd:COG0223 96 -LDiprLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDTGDILLQ 150
|
|
| FMT_core_like_3 |
cd08653 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
169-258 |
2.31e-09 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187721 [Multi-domain] Cd Length: 152 Bit Score: 54.91 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 169 VILARYMQVLSPELCRKLDGKAINIHHSLLPGFKGAKP-YHQAYNKGVKLVGATAHYINNDLDEGPIIAQGVEVV----D 243
Cdd:cd08653 50 VVSVYGCGIIKDALLAIPPLGVLNLHGGILPDYRGVHTgFWALANGDPDNVGVTVHLVDAGIDTGDVLAQARPPLaagdT 129
|
90
....*....|....*
gi 1329358581 244 HSHYPEDLIAKGRDI 258
Cdd:cd08653 130 LLSLYLRLYRAGVEL 144
|
|
| FMT_core_ArnA_N |
cd08644 |
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ... |
102-237 |
3.38e-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: 55.43 E-value: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 102 CLNDLLyrqrigQLAMDVVAVVSnHPD----------LKPLADWHQIPYYhFPLDPNDKPSQERqvwqvIEDSGAELVIL 171
Cdd:cd08644 15 CLEALL------AAGFEVVAVFT-HTDnpgeniwfgsVAQLAREHGIPVF-TPDDINHPEWVER-----LRALKPDLIFS 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1329358581 172 ARYMQVLSPEL--CRKLDgkAINIHHSLLPGFKGAKPYHQAYNKGVKLVGATAHYINNDLDEGPIIAQ 237
Cdd:cd08644 82 FYYRHMISEDIleIARLG--AFNLHGSLLPKYRGRAPLNWALINGETETGVTLHRMTKKPDAGAIVDQ 147
|
|
| FMT_core_Met-tRNA-FMT_N |
cd08646 |
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ... |
118-237 |
5.58e-09 |
|
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: 54.76 E-value: 5.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 118 DVVAVVSNhPDlKP--------------LADWHQIPYYHfPLDPNDKPSQERqvwqvIEDSGAELVILARYMQVLSPELC 183
Cdd:cd08646 25 EVVAVVTQ-PD-KPrgrgkkltpspvkeLALELGLPVLQ-PEKLKDEEFLEE-----LKALKPDLIVVVAYGQILPKEIL 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1329358581 184 RKLDGKAINIHHSLLPGFKGAKPYHQAYNKGVKLVGATAHYINNDLDEGPIIAQ 237
Cdd:cd08646 97 DLPPYGCINVHPSLLPKYRGAAPIQRAILNGDKETGVTIMKMDEGLDTGDILAQ 150
|
|
| PLN02285 |
PLN02285 |
methionyl-tRNA formyltransferase |
167-243 |
1.65e-07 |
|
methionyl-tRNA formyltransferase
Pssm-ID: 215159 [Multi-domain] Cd Length: 334 Bit Score: 51.62 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 167 ELVILARYMQVLsPElcRKLD----GkAINIHHSLLPGFKGAKPYHQAYNKGVKLVGATAHYINNDLDEGPIIAQGVEVV 242
Cdd:PLN02285 95 DLCITAAYGNIL-PQ--KFLDipklG-TVNIHPSLLPLYRGAAPVQRALQDGVNETGVSVAFTVRALDAGPVIAQERVEV 170
|
.
gi 1329358581 243 D 243
Cdd:PLN02285 171 D 171
|
|
| FMT_core_like_5 |
cd08823 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
106-237 |
1.94e-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: 187725 [Multi-domain] Cd Length: 177 Bit Score: 50.14 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 106 LLYRQRIGQLAmdVVAVVSNHPDLKPLADWHQIPYYHFPLDPNDKPSQERQVWQVIEDSGAELVILARYMQVLSPELCRK 185
Cdd:cd08823 14 LGQLLSEGRLA--GIAVPAHNASYFPQIFVFTGIRRLVSKQRVDTANLKEQLAEWLRALAADTVVVFTFPYRIPQHILDL 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1329358581 186 LDGKAINIHHSLLPGFKGAKP-YHQAYNKGVKLvGATAHYINNDLDEGPIIAQ 237
Cdd:cd08823 92 PPLGFYNLHPGLLPAYRGPDPlFWQIRNQEQET-AITVHKMTAEIDRGPIVLE 143
|
|
| PRK06988 |
PRK06988 |
formyltransferase; |
100-237 |
3.84e-07 |
|
formyltransferase;
Pssm-ID: 235902 [Multi-domain] Cd Length: 312 Bit Score: 50.46 E-value: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 100 DHCLNDLLYRqrigqlAMDVVAVVSnHPD----------LKPLADWHQIPYYhFPLDPNDKPSQERqvwqvIEDSGAELV 169
Cdd:PRK06988 15 VRCLQVLLAR------GVDVALVVT-HEDnpteniwfgsVAAVAAEHGIPVI-TPADPNDPELRAA-----VAAAAPDFI 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1329358581 170 ILARYMQVLSPELCRKLDGKAINIHHSLLPGFKGAKPYHQAYNKGVKLVGATAHYINNDLDEGPIIAQ 237
Cdd:PRK06988 82 FSFYYRHMIPVDLLALAPRGAYNMHGSLLPKYRGRVPVNWAVLNGETETGATLHEMVAKPDAGAIVDQ 149
|
|
| FMT_core_like_4 |
cd08651 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
117-237 |
7.35e-06 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187720 [Multi-domain] Cd Length: 180 Bit Score: 45.33 E-value: 7.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 117 MDVVAVVS-------NHPD---LKPLADWHQIPYYHFpldpNDKPSQErqVWQVIEDSGAELVILARYMQVLSPELCRKL 186
Cdd:cd08651 23 GEVVGVITlddsssnNDSDyldLDSFARKNGIPYYKF----TDINDEE--IIEWIKEANPDIIFVFGWSQLLKPEILAIP 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1329358581 187 DGKAINIHHSLLPGFKGAKPYHQAYNKGVKLVGATAHYINNDLDEGPIIAQ 237
Cdd:cd08651 97 RLGVIGFHPTKLPKNRGRAPIPWAILLGLKETASTFFWMDEGADSGDILSQ 147
|
|
| FMT_core_like_6 |
cd08820 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
91-238 |
9.89e-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: 187722 [Multi-domain] Cd Length: 173 Bit Score: 45.12 E-value: 9.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 91 KVVIMVSK--ADHCLNDLLYRQRIGQLamDVVAVVSNHPDLKplADWHQIPYYhfplDPNDKPSQERQVWQVIEDSGAEL 168
Cdd:cd08820 1 RIVFLGQKpiGEECLRTLLRLQDRGSF--EIIAVLTNTSPAD--VWEGSEPLY----DIGSTERNLHKLLEILENKGVDI 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1329358581 169 VILARYMQVLSPELCRKLDGKAINIHHSLLPGFKGAKPYHQAYNKGVKLVGATAHYINNDLDEGPIIAQG 238
Cdd:cd08820 73 LISVQYHWILPGSILEKAKEIAFNLHNAPLPEYRGCNQFSHAILNGDDQFGTTIHWMAEGIDSGDIIFEK 142
|
|
| PRK08125 |
PRK08125 |
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ... |
174-237 |
4.25e-04 |
|
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ArnA;
Pssm-ID: 236156 [Multi-domain] Cd Length: 660 Bit Score: 41.51 E-value: 4.25e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1329358581 174 YMQVLSPELCRKLDGKAINIHHSLLPGFKGAKPYHQAYNKGVKLVGATAHYINNDLDEGPIIAQ 237
Cdd:PRK08125 84 YRNLLSDEILQLAPAGAFNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQ 147
|
|
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