|
Name |
Accession |
Description |
Interval |
E-value |
| PurH |
COG0138 |
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR ... |
173-525 |
3.40e-173 |
|
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR transformylase/IMP cyclohydrolase PurH is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439908 Cd Length: 512 Bit Score: 498.40 E-value: 3.40e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 173 AYPRAI-QWFAEDrveidweegtvaiegDDGGAYPERRLASDDRVRELRYGENPHQDAALYADRTcEEANVVDAPQLNdG 251
Cdd:COG0138 182 AYDAAIaNYLAEQ---------------LGEEEFPETLTLSFEKVQDLRYGENPHQKAAFYRDPG-AEGGLATAEQLQ-G 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 252 aKGMGYNNYNDTDAALNLVKEFDEPACAVIKHTNPAGCAVADSISEAYADALATDPKSAFGGIVALNRECDAATAEQIIE 331
Cdd:COG0138 245 -KELSYNNILDADAALELVKEFDEPAVVIVKHANPCGVAVGDTLAEAYEKAYACDPVSAFGGIIAFNRPVDAATAEAIAK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 332 SFKEVVVAPGYTDDALDVLFEKDNLRVLDVSNQYEPSETLTEKPIVGGRLVQDRDLQTVTEDDLEVVTEREPTDEQLEAM 411
Cdd:COG0138 324 IFLEVIIAPDFSPEALEILAKKKNLRLLELGGLDPPAPGLDVKSVSGGLLVQDRDLGLIDPADLKVVTKRAPTEEELADL 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 412 RFAWQTIKHVKSNAIVFAKGTETVGVGAGQVSRVDAVEIAKMKAdsdaeGKDADGAVMASDAFFPFPDGIDAADEAGIEA 491
Cdd:COG0138 404 LFAWKVVKHVKSNAIVLAKDGATVGIGAGQMSRVDSARIALEKA-----GERAKGSVLASDAFFPFRDGVEAAAKAGITA 478
|
330 340 350
....*....|....*....|....*....|....
gi 506268592 492 VIQPGGSVNDDDVIERADELDIAMVFTGSRAFRH 525
Cdd:COG0138 479 IIQPGGSIRDEEVIAAADEHGIAMVFTGMRHFRH 512
|
|
| purH |
PRK00881 |
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; ... |
173-525 |
1.60e-171 |
|
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Provisional
Pssm-ID: 234854 Cd Length: 513 Bit Score: 494.22 E-value: 1.60e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 173 AYPRAI-QWFAEDrveidweegtvaiegdDGGAYPERRLASDDRVRELRYGENPHQDAALYADRTcEEANVVDAPQLNdG 251
Cdd:PRK00881 183 AYDAAIaNYLTEQ----------------VGEEFPETLNLSFEKKQDLRYGENPHQKAAFYRDPN-AEGGVATAEQLQ-G 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 252 aKGMGYNNYNDTDAALNLVKEFDEPACAVIKHTNPAGCAVADSISEAYADALATDPKSAFGGIVALNRECDAATAEQIIE 331
Cdd:PRK00881 245 -KELSYNNIADADAALELVKEFDEPACVIVKHANPCGVAVGDTILEAYDKAYACDPVSAFGGIIAFNREVDAETAEAIHK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 332 SFKEVVVAPGYTDDALDVLFEKDNLRVLDVSNQYEPSETLteKPIVGGRLVQDRDLQTVTEDDLEVVTEREPTDEQLEAM 411
Cdd:PRK00881 324 IFLEVIIAPSFSEEALEILAKKKNLRLLECPFPGGWEGDF--KSVSGGLLVQDRDLGMVDPADLKVVTKRQPTEQELKDL 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 412 RFAWQTIKHVKSNAIVFAKGTETVGVGAGQVSRVDAVEIAKMKADSdaEGKDADGAVMASDAFFPFPDGIDAADEAGIEA 491
Cdd:PRK00881 402 LFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIAIEKAGD--AGLDLKGAVLASDAFFPFRDGVEAAAKAGITA 479
|
330 340 350
....*....|....*....|....*....|....
gi 506268592 492 VIQPGGSVNDDDVIERADELDIAMVFTGSRAFRH 525
Cdd:PRK00881 480 IIQPGGSIRDEEVIAAADEHGIAMVFTGVRHFRH 513
|
|
| AICARFT_IMPCHas |
pfam01808 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
202-454 |
1.12e-128 |
|
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two steps in de novo purine biosynthesis. The bifunctional enzyme is found in both prokaryotes and eukaryotes. The second last step is catalyzed by 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase EC:2.1.2.3 (AICARFT), this enzyme catalyzes the formylation of AICAR with 10-formyl-tetrahydrofolate to yield FAICAR and tetrahydrofolate. This is catalyzed by a pair of C-terminal deaminase fold domains in the protein, where the active site is formed by the dimeric interface of two monomeric units. The last step is catalyzed by the N-terminal IMP (Inosine monophosphate) cyclohydrolase domain EC:3.5.4.10 (IMPCHase), cyclizing FAICAR (5-formylaminoimidazole-4-carboxamide ribonucleotide) to IMP.
Pssm-ID: 460341 Cd Length: 308 Bit Score: 377.13 E-value: 1.12e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 202 GGAYPERRLASDDRVRELRYGENPHQDAALYADRTcEEANVVDAPQLNdGaKGMGYNNYNDTDAALNLVKEFDEPACAVI 281
Cdd:pfam01808 59 GKEFPETLTLSFEKVQDLRYGENPHQKAAFYRDPG-PAGGLATAEQLQ-G-KELSYNNILDADAALELVKEFDEPAAVIV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 282 KHTNPAGCAVADSISEAYADALATDPKSAFGGIVALNRECDAATAEQIIESFKEVVVAPGYTDDALDVLFEKDNLRVLDV 361
Cdd:pfam01808 136 KHANPCGVAVGDTLAEAYRRALAADPVSAFGGIIALNRPVDAATAEEISKIFLEVIIAPGFTPEALEILKKKKNLRLLEI 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 362 SNQYEPSETLTEKPIVGGRLVQDRDLQTVTEDDLEVVTEREPTDEQLEAMRFAWQTIKHVKSNAIVFAKGTETVGVGAGQ 441
Cdd:pfam01808 216 DPLYPPPPGLEFRSVSGGLLVQDRDDALIDPDDLKVVTKRAPTEEELRDLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQ 295
|
250
....*....|...
gi 506268592 442 VSRVDAVEIAKMK 454
Cdd:pfam01808 296 MSRVDSARIAIEK 308
|
|
| AICARFT_IMPCHas |
smart00798 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
170-455 |
4.71e-123 |
|
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two steps in de novo purine biosynthesis. The bifunctional enzyme is found in both prokaryotes and eukaryotes. The second last step is catalysed by 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase (AICARFT), this enzyme catalyses the formylation of AICAR with 10-formyl-tetrahydrofolate to yield FAICAR and tetrahydrofolate. The last step is catalysed by IMP (Inosine monophosphate) cyclohydrolase (IMPCHase), cyclizing FAICAR (5-formylaminoimidazole-4-carboxamide ribonucleotide) to IMP.
Pssm-ID: 214822 Cd Length: 311 Bit Score: 362.97 E-value: 4.71e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 170 EFTA-YPRAI-QWFAEDrveidweegtvaiegdDGGAYPERRLASDDRVRELRYGENPHQDAALYADRTcEEANVVDAPQ 247
Cdd:smart00798 44 AHTAaYDAAIsNYLAKQ----------------LASEFPETLTLSFEKKQDLRYGENPHQKAAFYTDPD-ALGGIATAKQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 248 LNdgAKGMGYNNYNDTDAALNLVKEFDEPACAVIKHTNPAGCAVADSISEAYADALATDPKSAFGGIVALNRECDAATAE 327
Cdd:smart00798 107 LQ--GKELSYNNILDADAALELVKEFDEPACVIVKHANPCGVAVGDTLAEAYRKAYAADPVSAFGGIIAFNRPVDEETAE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 328 QIIESFKEVVVAPGYTDDALDVLFEKDNLRVLDVSNQYEPSETLTeKPIVGGRLVQDRDLQTVTEDDLEVVTEREPTDEQ 407
Cdd:smart00798 185 AINKIFLEVIIAPDFDEEALEILSKKKNLRLLECGPLPDPDGLEF-KSVSGGLLVQDRDNGGIDPEDLKVVTKRQPTEEE 263
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 506268592 408 LEAMRFAWQTIKHVKSNAIVFAKGTETVGVGAGQVSRVDAVEIAKMKA 455
Cdd:smart00798 264 LADLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIAAEKA 311
|
|
| purH |
TIGR00355 |
phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; PurH is ... |
219-525 |
3.96e-120 |
|
phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; PurH is bifunctional: IMP cyclohydrolase (EC 3.5.4.10); phosphoribosylaminoimidazolecarboxamide formyltransferase (EC 2.1.2.3) Involved in purine ribonucleotide biosynthesis. The IMP cyclohydrolase activity is in the N-terminal region. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273032 Cd Length: 511 Bit Score: 362.99 E-value: 3.96e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 219 LRYGENPHQDAALYADRTCEEANVVDAPQLNdgAKGMGYNNYNDTDAALNLVKEFDEPACAVIKHTNPAGCAVADSISEA 298
Cdd:TIGR00355 209 LRYGENPHQKAAFYVTQNVKEGSVATAEQLQ--GKELSYNNIADADAALEIVKEFDEPAAVIVKHANPCGVALGKTILDA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 299 YADALATDPKSAFGGIVALNRECDAATAEQIIESFKEVVVAPGYTDDALDVLFEKDNLRVLDVSNQYEPSETLTEKPIVG 378
Cdd:TIGR00355 287 YDRAFGADPTSAFGGIIALNRELDVPTAKAIVRQFLEVIIAPGYSAEALEILAKKKNLRVLILGIWANRVPELDFKRVNG 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 379 GRLVQDRDLQTVTEDDLEVVTEREPTDEQLEAMRFAWQTIKHVKSNAIVFAKGTETVGVGAGQVSRVDAVEIAKMKAdsD 458
Cdd:TIGR00355 367 GLLVQDRDDGMVDQSTLKVVTKRQPTEQELIDLLFAWKVAKHVKSNAIVYAKNNMTVGVGAGQMSRVGSAKIAGIKA--D 444
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506268592 459 AEGKDADGAVMASDAFFPFPDGIDAADEAGIEAVIQPGGSVNDDDVIERADELDIAMVFTGSRAFRH 525
Cdd:TIGR00355 445 DEGLEAKGSSLASDAFFPFRDGVEEAAAAGITCIIQPGGSMRDEDSIWAADEHGIVMVFTGMRHFRH 511
|
|
| PurN |
COG0299 |
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ... |
1-200 |
3.10e-80 |
|
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: 249.18 E-value: 3.10e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 1 MKVAGMASNRGRNLMNLADRTPGG---AELSVVLTNDADAPVLEKAEERGIPTEVVEHEASESREAHEQRVLDALADYEF 77
Cdd:COG0299 2 KRIAVLISGRGSNLQALIDAIEAGdlpAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYGP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 78 DLVALDGYMRILTETFLEE-TPTTLNVHPALLPAFKGMDVHEDVLEAGVRMTGCTVHVVDESVDDGPIVTQEPVPVREGD 156
Cdd:COG0299 82 DLVVLAGFMRILTPEFVRAfPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 506268592 157 TVEDLKERVLyEGEFTAYPRAIQWFAEDRVEIDweEGTVAIEGD 200
Cdd:COG0299 162 TEETLAARIL-EQEHRLYPEAIRLLAEGRLTLD--GRRVRLDGE 202
|
|
| FMT_core_GART |
cd08645 |
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ... |
2-181 |
3.38e-76 |
|
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: 238.06 E-value: 3.38e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 2 KVAGMASNRGRNLMNLADRTPGG---AELSVVLTNDADAPVLEKAEERGIPTEVVEHEASESREAHEQRVLDALADYEFD 78
Cdd:cd08645 1 RIAVLASGSGSNLQALIDAIKSGklnAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 79 LVALDGYMRILTETFLEETPT-TLNVHPALLPAFKGMDVHEDVLEAGVRMTGCTVHVVDESVDDGPIVTQEPVPVREGDT 157
Cdd:cd08645 81 LIVLAGFMRILSPEFLEAFPGrIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDT 160
|
170 180
....*....|....*....|....
gi 506268592 158 VEDLKERVLyEGEFTAYPRAIQWF 181
Cdd:cd08645 161 PETLAERIH-ALEHRLYPEAIKLL 183
|
|
| PurN |
TIGR00639 |
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ... |
1-186 |
1.13e-57 |
|
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: 190.27 E-value: 1.13e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 1 MKVAGMASNRGRNLMNLADRTPGG---AELSVVLTNDADAPVLEKAEERGIPTEVVEHEASESREAHEQRVLDALADYEF 77
Cdd:TIGR00639 1 KRIVVLISGNGSNLQAIIDACKEGkipASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 78 DLVALDGYMRILTETFLEETPT-TLNVHPALLPAFKGMDVHEDVLEAGVRMTGCTVHVVDESVDDGPIVTQEPVPVREGD 156
Cdd:TIGR00639 81 DLVVLAGFMRILGPTFLSRFAGrILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPED 160
|
170 180 190
....*....|....*....|....*....|
gi 506268592 157 TVEDLKERVLyEGEFTAYPRAIQWFAEDRV 186
Cdd:TIGR00639 161 TEETLEQRIH-KQEHRIYPLAIAWFAQGRL 189
|
|
| Formyl_trans_N |
pfam00551 |
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ... |
1-178 |
2.05e-44 |
|
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: 154.76 E-value: 2.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 1 MKVAGMASNRGRNLMNLADRT---PGGAELSVVLTNDADAPVLEKAEERGIPTEVVEHEASESREAHEQRVLDALADYEF 77
Cdd:pfam00551 1 MKIAVLISGTGSNLQALIDALrkgGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 78 DLVALDGYMRILTETFLEETP-TTLNVHPALLPAFKGMDVHEDVLEAGVRMTGCTVHVVDESVDDGPIVTQEPVPVREGD 156
Cdd:pfam00551 81 DVIVLAGYMRILPPEFLQAPPgGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160
|
170 180
....*....|....*....|..
gi 506268592 157 TVEDLKERVLyEGEFTAYPRAI 178
Cdd:pfam00551 161 TAETLYNRVA-DLEHKALPRVL 181
|
|
| PLN02331 |
PLN02331 |
phosphoribosylglycinamide formyltransferase |
2-197 |
6.10e-35 |
|
phosphoribosylglycinamide formyltransferase
Pssm-ID: 177965 [Multi-domain] Cd Length: 207 Bit Score: 130.20 E-value: 6.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 2 KVAGMASNRGRNLMNLADRTPGG---AELSVVLTNDADAPVLEKAEERGIPTEVVEHEASESREAHEQRVLDALADYEFD 78
Cdd:PLN02331 1 KLAVFVSGGGSNFRAIHDACLDGrvnGDVVVVVTNKPGCGGAEYARENGIPVLVYPKTKGEPDGLSPDELVDALRGAGVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 79 LVALDGYMRILTETFLEETP-TTLNVHPALLPAFKG-----MDVHEDVLEAGVRMTGCTVHVVDESVDDGPIVTQEPVPV 152
Cdd:PLN02331 81 FVLLAGYLKLIPVELVRAYPrSILNIHPALLPAFGGkgyygIKVHKAVIASGARYSGPTVHFVDEHYDTGRILAQRVVPV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 506268592 153 REGDTVEDLKERVLYEgEFTAYPRAIQWFAEDRveIDWEEGTVAI 197
Cdd:PLN02331 161 LATDTPEELAARVLHE-EHQLYVEVVAALCEER--IVWREDGVPL 202
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PurH |
COG0138 |
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR ... |
173-525 |
3.40e-173 |
|
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR transformylase/IMP cyclohydrolase PurH is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439908 Cd Length: 512 Bit Score: 498.40 E-value: 3.40e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 173 AYPRAI-QWFAEDrveidweegtvaiegDDGGAYPERRLASDDRVRELRYGENPHQDAALYADRTcEEANVVDAPQLNdG 251
Cdd:COG0138 182 AYDAAIaNYLAEQ---------------LGEEEFPETLTLSFEKVQDLRYGENPHQKAAFYRDPG-AEGGLATAEQLQ-G 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 252 aKGMGYNNYNDTDAALNLVKEFDEPACAVIKHTNPAGCAVADSISEAYADALATDPKSAFGGIVALNRECDAATAEQIIE 331
Cdd:COG0138 245 -KELSYNNILDADAALELVKEFDEPAVVIVKHANPCGVAVGDTLAEAYEKAYACDPVSAFGGIIAFNRPVDAATAEAIAK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 332 SFKEVVVAPGYTDDALDVLFEKDNLRVLDVSNQYEPSETLTEKPIVGGRLVQDRDLQTVTEDDLEVVTEREPTDEQLEAM 411
Cdd:COG0138 324 IFLEVIIAPDFSPEALEILAKKKNLRLLELGGLDPPAPGLDVKSVSGGLLVQDRDLGLIDPADLKVVTKRAPTEEELADL 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 412 RFAWQTIKHVKSNAIVFAKGTETVGVGAGQVSRVDAVEIAKMKAdsdaeGKDADGAVMASDAFFPFPDGIDAADEAGIEA 491
Cdd:COG0138 404 LFAWKVVKHVKSNAIVLAKDGATVGIGAGQMSRVDSARIALEKA-----GERAKGSVLASDAFFPFRDGVEAAAKAGITA 478
|
330 340 350
....*....|....*....|....*....|....
gi 506268592 492 VIQPGGSVNDDDVIERADELDIAMVFTGSRAFRH 525
Cdd:COG0138 479 IIQPGGSIRDEEVIAAADEHGIAMVFTGMRHFRH 512
|
|
| purH |
PRK00881 |
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; ... |
173-525 |
1.60e-171 |
|
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Provisional
Pssm-ID: 234854 Cd Length: 513 Bit Score: 494.22 E-value: 1.60e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 173 AYPRAI-QWFAEDrveidweegtvaiegdDGGAYPERRLASDDRVRELRYGENPHQDAALYADRTcEEANVVDAPQLNdG 251
Cdd:PRK00881 183 AYDAAIaNYLTEQ----------------VGEEFPETLNLSFEKKQDLRYGENPHQKAAFYRDPN-AEGGVATAEQLQ-G 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 252 aKGMGYNNYNDTDAALNLVKEFDEPACAVIKHTNPAGCAVADSISEAYADALATDPKSAFGGIVALNRECDAATAEQIIE 331
Cdd:PRK00881 245 -KELSYNNIADADAALELVKEFDEPACVIVKHANPCGVAVGDTILEAYDKAYACDPVSAFGGIIAFNREVDAETAEAIHK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 332 SFKEVVVAPGYTDDALDVLFEKDNLRVLDVSNQYEPSETLteKPIVGGRLVQDRDLQTVTEDDLEVVTEREPTDEQLEAM 411
Cdd:PRK00881 324 IFLEVIIAPSFSEEALEILAKKKNLRLLECPFPGGWEGDF--KSVSGGLLVQDRDLGMVDPADLKVVTKRQPTEQELKDL 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 412 RFAWQTIKHVKSNAIVFAKGTETVGVGAGQVSRVDAVEIAKMKADSdaEGKDADGAVMASDAFFPFPDGIDAADEAGIEA 491
Cdd:PRK00881 402 LFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIAIEKAGD--AGLDLKGAVLASDAFFPFRDGVEAAAKAGITA 479
|
330 340 350
....*....|....*....|....*....|....
gi 506268592 492 VIQPGGSVNDDDVIERADELDIAMVFTGSRAFRH 525
Cdd:PRK00881 480 IIQPGGSIRDEEVIAAADEHGIAMVFTGVRHFRH 513
|
|
| AICARFT_IMPCHas |
pfam01808 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
202-454 |
1.12e-128 |
|
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two steps in de novo purine biosynthesis. The bifunctional enzyme is found in both prokaryotes and eukaryotes. The second last step is catalyzed by 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase EC:2.1.2.3 (AICARFT), this enzyme catalyzes the formylation of AICAR with 10-formyl-tetrahydrofolate to yield FAICAR and tetrahydrofolate. This is catalyzed by a pair of C-terminal deaminase fold domains in the protein, where the active site is formed by the dimeric interface of two monomeric units. The last step is catalyzed by the N-terminal IMP (Inosine monophosphate) cyclohydrolase domain EC:3.5.4.10 (IMPCHase), cyclizing FAICAR (5-formylaminoimidazole-4-carboxamide ribonucleotide) to IMP.
Pssm-ID: 460341 Cd Length: 308 Bit Score: 377.13 E-value: 1.12e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 202 GGAYPERRLASDDRVRELRYGENPHQDAALYADRTcEEANVVDAPQLNdGaKGMGYNNYNDTDAALNLVKEFDEPACAVI 281
Cdd:pfam01808 59 GKEFPETLTLSFEKVQDLRYGENPHQKAAFYRDPG-PAGGLATAEQLQ-G-KELSYNNILDADAALELVKEFDEPAAVIV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 282 KHTNPAGCAVADSISEAYADALATDPKSAFGGIVALNRECDAATAEQIIESFKEVVVAPGYTDDALDVLFEKDNLRVLDV 361
Cdd:pfam01808 136 KHANPCGVAVGDTLAEAYRRALAADPVSAFGGIIALNRPVDAATAEEISKIFLEVIIAPGFTPEALEILKKKKNLRLLEI 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 362 SNQYEPSETLTEKPIVGGRLVQDRDLQTVTEDDLEVVTEREPTDEQLEAMRFAWQTIKHVKSNAIVFAKGTETVGVGAGQ 441
Cdd:pfam01808 216 DPLYPPPPGLEFRSVSGGLLVQDRDDALIDPDDLKVVTKRAPTEEELRDLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQ 295
|
250
....*....|...
gi 506268592 442 VSRVDAVEIAKMK 454
Cdd:pfam01808 296 MSRVDSARIAIEK 308
|
|
| AICARFT_IMPCHas |
smart00798 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
170-455 |
4.71e-123 |
|
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two steps in de novo purine biosynthesis. The bifunctional enzyme is found in both prokaryotes and eukaryotes. The second last step is catalysed by 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase (AICARFT), this enzyme catalyses the formylation of AICAR with 10-formyl-tetrahydrofolate to yield FAICAR and tetrahydrofolate. The last step is catalysed by IMP (Inosine monophosphate) cyclohydrolase (IMPCHase), cyclizing FAICAR (5-formylaminoimidazole-4-carboxamide ribonucleotide) to IMP.
Pssm-ID: 214822 Cd Length: 311 Bit Score: 362.97 E-value: 4.71e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 170 EFTA-YPRAI-QWFAEDrveidweegtvaiegdDGGAYPERRLASDDRVRELRYGENPHQDAALYADRTcEEANVVDAPQ 247
Cdd:smart00798 44 AHTAaYDAAIsNYLAKQ----------------LASEFPETLTLSFEKKQDLRYGENPHQKAAFYTDPD-ALGGIATAKQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 248 LNdgAKGMGYNNYNDTDAALNLVKEFDEPACAVIKHTNPAGCAVADSISEAYADALATDPKSAFGGIVALNRECDAATAE 327
Cdd:smart00798 107 LQ--GKELSYNNILDADAALELVKEFDEPACVIVKHANPCGVAVGDTLAEAYRKAYAADPVSAFGGIIAFNRPVDEETAE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 328 QIIESFKEVVVAPGYTDDALDVLFEKDNLRVLDVSNQYEPSETLTeKPIVGGRLVQDRDLQTVTEDDLEVVTEREPTDEQ 407
Cdd:smart00798 185 AINKIFLEVIIAPDFDEEALEILSKKKNLRLLECGPLPDPDGLEF-KSVSGGLLVQDRDNGGIDPEDLKVVTKRQPTEEE 263
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 506268592 408 LEAMRFAWQTIKHVKSNAIVFAKGTETVGVGAGQVSRVDAVEIAKMKA 455
Cdd:smart00798 264 LADLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIAAEKA 311
|
|
| purH |
TIGR00355 |
phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; PurH is ... |
219-525 |
3.96e-120 |
|
phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; PurH is bifunctional: IMP cyclohydrolase (EC 3.5.4.10); phosphoribosylaminoimidazolecarboxamide formyltransferase (EC 2.1.2.3) Involved in purine ribonucleotide biosynthesis. The IMP cyclohydrolase activity is in the N-terminal region. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273032 Cd Length: 511 Bit Score: 362.99 E-value: 3.96e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 219 LRYGENPHQDAALYADRTCEEANVVDAPQLNdgAKGMGYNNYNDTDAALNLVKEFDEPACAVIKHTNPAGCAVADSISEA 298
Cdd:TIGR00355 209 LRYGENPHQKAAFYVTQNVKEGSVATAEQLQ--GKELSYNNIADADAALEIVKEFDEPAAVIVKHANPCGVALGKTILDA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 299 YADALATDPKSAFGGIVALNRECDAATAEQIIESFKEVVVAPGYTDDALDVLFEKDNLRVLDVSNQYEPSETLTEKPIVG 378
Cdd:TIGR00355 287 YDRAFGADPTSAFGGIIALNRELDVPTAKAIVRQFLEVIIAPGYSAEALEILAKKKNLRVLILGIWANRVPELDFKRVNG 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 379 GRLVQDRDLQTVTEDDLEVVTEREPTDEQLEAMRFAWQTIKHVKSNAIVFAKGTETVGVGAGQVSRVDAVEIAKMKAdsD 458
Cdd:TIGR00355 367 GLLVQDRDDGMVDQSTLKVVTKRQPTEQELIDLLFAWKVAKHVKSNAIVYAKNNMTVGVGAGQMSRVGSAKIAGIKA--D 444
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506268592 459 AEGKDADGAVMASDAFFPFPDGIDAADEAGIEAVIQPGGSVNDDDVIERADELDIAMVFTGSRAFRH 525
Cdd:TIGR00355 445 DEGLEAKGSSLASDAFFPFRDGVEEAAAAGITCIIQPGGSMRDEDSIWAADEHGIVMVFTGMRHFRH 511
|
|
| PLN02891 |
PLN02891 |
IMP cyclohydrolase |
219-525 |
1.44e-95 |
|
IMP cyclohydrolase
Pssm-ID: 178479 [Multi-domain] Cd Length: 547 Bit Score: 300.55 E-value: 1.44e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 219 LRYGENPHQDAALYADRTCEEAN---VVDAPQLNdgAKGMGYNNYNDTDAALNLVKEFDEPACAVIKHTNPAGCAVADSI 295
Cdd:PLN02891 234 LRYGENPHQKAAFYVDKSLSEVNaggIATAIQHH--GKEMSYNNYLDADAAWNCVSEFSNPTCVVVKHTNPCGVASRGDI 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 296 SEAYADALATDPKSAFGGIVALNRECDAATAEQIIE----------SFKEVVVAPGYTDDALDVLFEKD-NLRVLDVsnq 364
Cdd:PLN02891 312 LEAYRLAVRADPVSAFGGIVAFNCEVDEDLAREIREfrsptdgetrMFYEIVVAPKYTEKGLEVLKGKSkTLRILEA--- 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 365 yEPSE--TLTEKPIVGGRLVQDRDLQTVTEDDLEVVTEREPTDEQLEAMRFAWQTIKHVKSNAIVFAKGTETVGVGAGQV 442
Cdd:PLN02891 389 -KPRKkgRLSLRQVGGGWLAQDSDDLTPEDITFTVVSEKVPTESELEDAKFAWLCVKHVKSNAIVVAKNNRMLGMGSGQP 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 443 SRVDAVEIAKMKAdsdaeGKDADGAVMASDAFFPFP--DGIDAADEAGIEAVIQPGGSVNDDDVIERADELDIAMVFTGS 520
Cdd:PLN02891 468 NRVESLRIALEKA-----GEEAKGAALASDAFFPFAwnDAVEEACQAGVKVIAEPGGSMRDQDAIDCCNKYGVALLFTGV 542
|
....*
gi 506268592 521 RAFRH 525
Cdd:PLN02891 543 RHFRH 547
|
|
| PurN |
COG0299 |
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ... |
1-200 |
3.10e-80 |
|
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: 249.18 E-value: 3.10e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 1 MKVAGMASNRGRNLMNLADRTPGG---AELSVVLTNDADAPVLEKAEERGIPTEVVEHEASESREAHEQRVLDALADYEF 77
Cdd:COG0299 2 KRIAVLISGRGSNLQALIDAIEAGdlpAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYGP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 78 DLVALDGYMRILTETFLEE-TPTTLNVHPALLPAFKGMDVHEDVLEAGVRMTGCTVHVVDESVDDGPIVTQEPVPVREGD 156
Cdd:COG0299 82 DLVVLAGFMRILTPEFVRAfPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 506268592 157 TVEDLKERVLyEGEFTAYPRAIQWFAEDRVEIDweEGTVAIEGD 200
Cdd:COG0299 162 TEETLAARIL-EQEHRLYPEAIRLLAEGRLTLD--GRRVRLDGE 202
|
|
| FMT_core_GART |
cd08645 |
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ... |
2-181 |
3.38e-76 |
|
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: 238.06 E-value: 3.38e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 2 KVAGMASNRGRNLMNLADRTPGG---AELSVVLTNDADAPVLEKAEERGIPTEVVEHEASESREAHEQRVLDALADYEFD 78
Cdd:cd08645 1 RIAVLASGSGSNLQALIDAIKSGklnAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 79 LVALDGYMRILTETFLEETPT-TLNVHPALLPAFKGMDVHEDVLEAGVRMTGCTVHVVDESVDDGPIVTQEPVPVREGDT 157
Cdd:cd08645 81 LIVLAGFMRILSPEFLEAFPGrIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDT 160
|
170 180
....*....|....*....|....
gi 506268592 158 VEDLKERVLyEGEFTAYPRAIQWF 181
Cdd:cd08645 161 PETLAERIH-ALEHRLYPEAIKLL 183
|
|
| PurN |
TIGR00639 |
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ... |
1-186 |
1.13e-57 |
|
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: 190.27 E-value: 1.13e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 1 MKVAGMASNRGRNLMNLADRTPGG---AELSVVLTNDADAPVLEKAEERGIPTEVVEHEASESREAHEQRVLDALADYEF 77
Cdd:TIGR00639 1 KRIVVLISGNGSNLQAIIDACKEGkipASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 78 DLVALDGYMRILTETFLEETPT-TLNVHPALLPAFKGMDVHEDVLEAGVRMTGCTVHVVDESVDDGPIVTQEPVPVREGD 156
Cdd:TIGR00639 81 DLVVLAGFMRILGPTFLSRFAGrILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPED 160
|
170 180 190
....*....|....*....|....*....|
gi 506268592 157 TVEDLKERVLyEGEFTAYPRAIQWFAEDRV 186
Cdd:TIGR00639 161 TEETLEQRIH-KQEHRIYPLAIAWFAQGRL 189
|
|
| PRK07106 |
PRK07106 |
phosphoribosylaminoimidazolecarboxamide formyltransferase; |
218-525 |
1.80e-55 |
|
phosphoribosylaminoimidazolecarboxamide formyltransferase;
Pssm-ID: 180841 Cd Length: 390 Bit Score: 191.03 E-value: 1.80e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 218 ELRYGENPHQdaalyadrtcEEANVvdapQLNDGAKGM-------GYNNYNDTDAALNLVKEFDE----PACAVIKHTNP 286
Cdd:PRK07106 5 ELKYGCNPNQ----------KPARI----FMKEGELPIevlngrpGYINFLDALNSWQLVKELKEatglPAAASFKHVSP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 287 AGCAVADSISE------------------AYADALATDPKSAFGGIVALNRECDAATAEQIIESFKEVVVAPGYTDDALD 348
Cdd:PRK07106 71 AGAAVGLPLSDtlkkiyfvddmelsplacAYARARGADRMSSYGDFAALSDVCDVETAKLLKREVSDGIIAPGYTPEALE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 349 VLFEKD--NLRVLDVSNQYEPSEtLTEKPIVGGRLVQDRDLQTVTEDDLE-VVTE-REPTDEQLEAMRFAWQTIKHVKSN 424
Cdd:PRK07106 151 ILKAKKkgNYNIIKIDPNYEPAP-IETKDVFGITFEQGRNELKIDEDLLKnIVTEnKELPDEAKRDLIIALITLKYTQSN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 425 AIVFAKGTETVGVGAGQVSRVDAVEIAKMKAD--------------------------------SD-------------- 458
Cdd:PRK07106 230 SVCYAKDGQAIGIGAGQQSRIHCTRLAGNKADiwylrqhpkvlnlpfkegirrpdrdnaidvylSDdymdvladgvwqqf 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 459 ---------AEGKDA-----DGAVMASDAFFPFPDGIDAADEAGIEAVIQPGGSVNDDDVIERADELDIAMVFTGSRAFR 524
Cdd:PRK07106 310 ftekpepltREEKRAwlatlTGVALGSDAFFPFGDNIERAAKSGVKYIAQPGGSIRDDNVIETCNKYGMTMAFTGVRLFH 389
|
.
gi 506268592 525 H 525
Cdd:PRK07106 390 H 390
|
|
| Formyl_trans_N |
pfam00551 |
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ... |
1-178 |
2.05e-44 |
|
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: 154.76 E-value: 2.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 1 MKVAGMASNRGRNLMNLADRT---PGGAELSVVLTNDADAPVLEKAEERGIPTEVVEHEASESREAHEQRVLDALADYEF 77
Cdd:pfam00551 1 MKIAVLISGTGSNLQALIDALrkgGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 78 DLVALDGYMRILTETFLEETP-TTLNVHPALLPAFKGMDVHEDVLEAGVRMTGCTVHVVDESVDDGPIVTQEPVPVREGD 156
Cdd:pfam00551 81 DVIVLAGYMRILPPEFLQAPPgGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160
|
170 180
....*....|....*....|..
gi 506268592 157 TVEDLKERVLyEGEFTAYPRAI 178
Cdd:pfam00551 161 TAETLYNRVA-DLEHKALPRVL 181
|
|
| PLN02331 |
PLN02331 |
phosphoribosylglycinamide formyltransferase |
2-197 |
6.10e-35 |
|
phosphoribosylglycinamide formyltransferase
Pssm-ID: 177965 [Multi-domain] Cd Length: 207 Bit Score: 130.20 E-value: 6.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 2 KVAGMASNRGRNLMNLADRTPGG---AELSVVLTNDADAPVLEKAEERGIPTEVVEHEASESREAHEQRVLDALADYEFD 78
Cdd:PLN02331 1 KLAVFVSGGGSNFRAIHDACLDGrvnGDVVVVVTNKPGCGGAEYARENGIPVLVYPKTKGEPDGLSPDELVDALRGAGVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 79 LVALDGYMRILTETFLEETP-TTLNVHPALLPAFKG-----MDVHEDVLEAGVRMTGCTVHVVDESVDDGPIVTQEPVPV 152
Cdd:PLN02331 81 FVLLAGYLKLIPVELVRAYPrSILNIHPALLPAFGGkgyygIKVHKAVIASGARYSGPTVHFVDEHYDTGRILAQRVVPV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 506268592 153 REGDTVEDLKERVLYEgEFTAYPRAIQWFAEDRveIDWEEGTVAI 197
Cdd:PLN02331 161 LATDTPEELAARVLHE-EHQLYVEVVAALCEER--IVWREDGVPL 202
|
|
| PurU |
COG0788 |
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ... |
1-190 |
3.55e-30 |
|
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: 119.00 E-value: 3.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 1 MKVAGMASNRGRNLMNLADRTPGG---AELSVVLTNDADapvLEK-AEERGIPTEVVEHEAsESREAHEQRVLDALADYE 76
Cdd:COG0788 87 KRVAILVSKEDHCLNDLLYRWRSGelpAEIPAVISNHPD---LRPlAEWFGIPFHHIPVTK-ETKAEAEARLLELLEEYD 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 77 FDLVALDGYMRILTETFLEETPT-TLNVHPALLPAFKGMDVHEDVLEAGVRMTGCTVHVVDESVDDGPIVTQEPVPVREG 155
Cdd:COG0788 163 IDLVVLARYMQILSPDFCARLPGrIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVERVDHR 242
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 506268592 156 DTVEDLKE-------RVLYegeftaypRAIQWFAEDRVEIDW 190
Cdd:COG0788 243 DTPEDLVRkgrdvekRVLA--------RAVRWHLEDRVLVNG 276
|
|
| FMT_core_Formyl-FH4-Hydrolase_C |
cd08648 |
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ... |
1-186 |
9.63e-30 |
|
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: 115.35 E-value: 9.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 1 MKVAGMASNRGRNLMNLADRTPGG---AELSVVLTNDadaPVLEKAEER-GIPTEVVEHEAsESREAHEQRVLDALADYE 76
Cdd:cd08648 1 KRVAIFVSKEDHCLYDLLHRWREGelpCEIPLVISNH---PDLRPLAERfGIPFHHIPVTK-DTKAEAEAEQLELLEEYG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 77 FDLVALDGYMRILTETFLEETPT-TLNVHPALLPAFKGMDVHEDVLEAGVRMTGCTVHVVDESVDDGPIVTQEPVPVREG 155
Cdd:cd08648 77 VDLVVLARYMQILSPDFVERYPNrIINIHHSFLPAFKGAKPYHQAFERGVKLIGATAHYVTEELDEGPIIEQDVERVSHR 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 506268592 156 DTVEDLKE-------RVLyegeftayPRAIQWFAEDRV 186
Cdd:cd08648 157 DSVEDLVRkgrdiekQVL--------ARAVKWHLEDRV 186
|
|
| FMT_core |
cd08369 |
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ... |
20-180 |
1.44e-25 |
|
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: 103.14 E-value: 1.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 20 RTPGGAELSVVLTNDADAPVLEKAEERGIPTEVVEHeasesREAHEQRVLDALADYEFDLVALDGYMRILTETFLEETP- 98
Cdd:cd08369 18 LSKEGHEIVGVVTHPDSPRGTAQLSLELVGGKVYLD-----SNINTPELLELLKEFAPDLIVSINFRQIIPPEILKLPPg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 99 TTLNVHPALLPAFKGMDVHEDVLEAGVRMTGCTVHVVDESVDDGPIVTQEPVPVREGDTVEDLKERvLYEGEFTAYPRAI 178
Cdd:cd08369 93 GAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTAGTLYQR-LIELGPKLLKEAL 171
|
..
gi 506268592 179 QW 180
Cdd:cd08369 172 QK 173
|
|
| purU |
PRK06027 |
formyltetrahydrofolate deformylase; Reviewed |
1-186 |
2.26e-23 |
|
formyltetrahydrofolate deformylase; Reviewed
Pssm-ID: 235676 [Multi-domain] Cd Length: 286 Bit Score: 99.80 E-value: 2.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 1 MKVAGMASNRGRNLMNLADRTPGG---AELSVVLTNDADapvLEKAEER-GIPTEVVEHEAsESREAHEQRVLDALADYE 76
Cdd:PRK06027 90 KRVVILVSKEDHCLGDLLWRWRSGelpVEIAAVISNHDD---LRSLVERfGIPFHHVPVTK-ETKAEAEARLLELIDEYQ 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 77 FDLVALDGYMRILTETFLEETPT-TLNVHPALLPAFKGMDVHEDVLEAGVRMTGCTVHVVDESVDDGPIVTQEPVPVREG 155
Cdd:PRK06027 166 PDLVVLARYMQILSPDFVARFPGrIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVIRVDHR 245
|
170 180 190
....*....|....*....|....*....|....*...
gi 506268592 156 DTVEDLK------ER-VLyegeftayPRAIQWFAEDRV 186
Cdd:PRK06027 246 DTAEDLVragrdvEKqVL--------ARAVRWHLEDRV 275
|
|
| PLN02828 |
PLN02828 |
formyltetrahydrofolate deformylase |
1-197 |
2.13e-17 |
|
formyltetrahydrofolate deformylase
Pssm-ID: 178422 Cd Length: 268 Bit Score: 82.10 E-value: 2.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 1 MKVAGMASNRGRNLMNLADRTPGG---AELSVVLTNDADAP---VLEKAEERGIPTevveHEASESRE-AHEQRVLDALA 73
Cdd:PLN02828 71 YKIAVLASKQDHCLIDLLHRWQDGrlpVDITCVISNHERGPnthVMRFLERHGIPY----HYLPTTKEnKREDEILELVK 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 74 DYEFdlVALDGYMRILTETFLEE-TPTTLNVHPALLPAFKGMDVHEDVLEAGVRMTGCTVHVVDESVDDGPIVTQEPVPV 152
Cdd:PLN02828 147 GTDF--LVLARYMQILSGNFLKGyGKDIINIHHGLLPSFKGGNPSKQAFDAGVKLIGATSHFVTEELDAGPIIEQMVERV 224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 506268592 153 REGDTV-------EDLKERVLyegeftayPRAIQWFAEDRVEIDWEEGTVAI 197
Cdd:PLN02828 225 SHRDNLrsfvqksENLEKQCL--------AKAIKSYCELRVLPYGTNKTVVF 268
|
|
| Fmt |
COG0223 |
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis]; |
38-165 |
8.71e-16 |
|
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439993 [Multi-domain] Cd Length: 308 Bit Score: 78.22 E-value: 8.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 38 PVLEKAEERGIPteVVEHEasesrEAHEQRVLDALADYEFDLVALDGYMRILTETFLEeTPT--TLNVHPALLPAFKG-M 114
Cdd:COG0223 47 PVKELALEHGIP--VLQPE-----SLKDPEFLEELRALNPDLIVVVAYGQILPKEVLD-IPRlgCINLHASLLPRYRGaA 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 506268592 115 DVHEdVLEAGVRMTGCTVHVVDESVDDGPIVTQEPVPVREGDTVEDLKERV 165
Cdd:COG0223 119 PIQW-AILNGDTETGVTIMQMDEGLDTGDILLQEEVPIGPDDTAGSLHDKL 168
|
|
| PLN02285 |
PLN02285 |
methionyl-tRNA formyltransferase |
38-169 |
2.08e-15 |
|
methionyl-tRNA formyltransferase
Pssm-ID: 215159 [Multi-domain] Cd Length: 334 Bit Score: 77.43 E-value: 2.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 38 PVLEKAEERGIPTEVVEHEAsesrEAHEQRVLDALADYEFDLVALDGYMRILTETFLEeTPT--TLNVHPALLPAFKGMD 115
Cdd:PLN02285 59 PVAQLALDRGFPPDLIFTPE----KAGEEDFLSALRELQPDLCITAAYGNILPQKFLD-IPKlgTVNIHPSLLPLYRGAA 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 506268592 116 VHEDVLEAGVRMTGCTVHVVDESVDDGPIVTQEPVPVREGDTVEDLKERVLYEG 169
Cdd:PLN02285 134 PVQRALQDGVNETGVSVAFTVRALDAGPVIAQERVEVDEDIKAPELLPLLFELG 187
|
|
| PRK13011 |
PRK13011 |
formyltetrahydrofolate deformylase; Reviewed |
1-186 |
5.90e-15 |
|
formyltetrahydrofolate deformylase; Reviewed
Pssm-ID: 237266 [Multi-domain] Cd Length: 286 Bit Score: 75.40 E-value: 5.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 1 MKVAGMASNRGRNLMNLADRTPGGA---ELSVVLTNDADapvLEK-AEERGIPTEVVEHEAsESREAHEQRVLDALADYE 76
Cdd:PRK13011 90 PKVLIMVSKFDHCLNDLLYRWRIGElpmDIVGVVSNHPD---LEPlAAWHGIPFHHFPITP-DTKPQQEAQVLDVVEESG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 77 FDLVALDGYMRILTETFLEETP-TTLNVHPALLPAFKGMDVHEDVLEAGVRMTGCTVHVVDESVDDGPIVTQEPVPVREG 155
Cdd:PRK13011 166 AELVVLARYMQVLSPELCRKLAgRAINIHHSFLPGFKGAKPYHQAYERGVKLIGATAHYVTDDLDEGPIIEQDVERVDHA 245
|
170 180 190
....*....|....*....|....*....|...
gi 506268592 156 DTVEDL--KERvlyEGEFTAYPRAIQWFAEDRV 186
Cdd:PRK13011 246 YSPEDLvaKGR---DVECLTLARAVKAHIERRV 275
|
|
| FMT_core_like_3 |
cd08653 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
64-178 |
1.62e-14 |
|
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: 71.09 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 64 HEQRVLDALADYEFDLVALDGyMRILTETFLEETP-TTLNVHPALLPAFKGMDVH-EDVLEAGVRMTGCTVHVVDESVDD 141
Cdd:cd08653 35 NGPEVVAALRALAPDVVSVYG-CGIIKDALLAIPPlGVLNLHGGILPDYRGVHTGfWALANGDPDNVGVTVHLVDAGIDT 113
|
90 100 110
....*....|....*....|....*....|....*..
gi 506268592 142 GPIVTQEPVPVREGDTVEDLKERvLYEGEFTAYPRAI 178
Cdd:cd08653 114 GDVLAQARPPLAAGDTLLSLYLR-LYRAGVELMVEAI 149
|
|
| purU |
PRK13010 |
formyltetrahydrofolate deformylase; Reviewed |
1-195 |
1.82e-14 |
|
formyltetrahydrofolate deformylase; Reviewed
Pssm-ID: 139334 [Multi-domain] Cd Length: 289 Bit Score: 74.06 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 1 MKVAGMASNRGRNLMNLADRTPGGA---ELSVVLTNDADApvLEKAEERGIPTEVVEhEASESREAHEQRVLDALADYEF 77
Cdd:PRK13010 94 PKVVIMVSKFDHCLNDLLYRWRMGEldmDIVGIISNHPDL--QPLAVQHDIPFHHLP-VTPDTKAQQEAQILDLIETSGA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 78 DLVALDGYMRILT-ETFLEETPTTLNVHPALLPAFKGMDVHEDVLEAGVRMTGCTVHVVDESVDDGPIVTQEPVPVREGD 156
Cdd:PRK13010 171 ELVVLARYMQVLSdDLSRKLSGRAINIHHSFLPGFKGARPYHQAHARGVKLIGATAHFVTDDLDEGPIIEQDVERVDHSY 250
|
170 180 190
....*....|....*....|....*....|....*....
gi 506268592 157 TVEDLKeRVLYEGEFTAYPRAIQWFAEDRVEIDWEEGTV 195
Cdd:PRK13010 251 SPEDLV-AKGRDVECLTLARAVKAFIEHRVFINGDRTVV 288
|
|
| FMT_core_Met-tRNA-FMT_N |
cd08646 |
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ... |
38-164 |
7.15e-14 |
|
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: 70.55 E-value: 7.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 38 PVLEKAEERGIPteVVEHEASESREAheqrvLDALADYEFDL---VAldgYMRILTETFLEETP-TTLNVHPALLPAFKG 113
Cdd:cd08646 47 PVKELALELGLP--VLQPEKLKDEEF-----LEELKALKPDLivvVA---YGQILPKEILDLPPyGCINVHPSLLPKYRG 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 506268592 114 MD-VHEdVLEAGVRMTGCTVHVVDESVDDGPIVTQEPVPVREGDTVEDLKER 164
Cdd:cd08646 117 AApIQR-AILNGDKETGVTIMKMDEGLDTGDILAQEEVPIDPDDTAGELLDK 167
|
|
| fmt |
TIGR00460 |
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ... |
38-165 |
1.51e-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: 71.66 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 38 PVLEKAEERGIPteVVEHEASESREaheqrVLDALADYEFDLVALDGYMRILTETFLEETP-TTLNVHPALLPAFKG-MD 115
Cdd:TIGR00460 47 PVKVLAEEKGIP--VFQPEKQRQLE-----ELPLVRELKPDVIVVVSFGKILPKEFLDLFPyGCINVHPSLLPRWRGgAP 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 506268592 116 VHEDVLEaGVRMTGCTVHVVDESVDDGPIVTQEPVPVREGDTVEDLKERV 165
Cdd:TIGR00460 120 IQRAILN-GDKKTGVTIMQMVPKMDAGDILKQETFPIEEEDNSGTLSDKL 168
|
|
| FMT_core_ArnA_N |
cd08644 |
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ... |
24-167 |
1.21e-11 |
|
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: 63.90 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 24 GAELSVVLTNdADAP--------VLEKAEERGIPteVVEHEASESREaheqrVLDALADYEFDLVALDGYMRILTETFLE 95
Cdd:cd08644 23 GFEVVAVFTH-TDNPgeniwfgsVAQLAREHGIP--VFTPDDINHPE-----WVERLRALKPDLIFSFYYRHMISEDILE 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506268592 96 ETPT-TLNVHPALLPAFKGMDVHEDVLEAGVRMTGCTVHVVDESVDDGPIVTQEPVPVREGDTVEDLKERVLY 167
Cdd:cd08644 95 IARLgAFNLHGSLLPKYRGRAPLNWALINGETETGVTLHRMTKKPDAGAIVDQEKVPILPDDTAKSLFHKLCV 167
|
|
| FMT_core_like_4 |
cd08651 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
24-167 |
6.38e-10 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187720 [Multi-domain] Cd Length: 180 Bit Score: 58.43 E-value: 6.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 24 GAELSVVLT--------NDADAPVLEKAEERGIPteVVEHEASESREaheqrVLDALADYEFDLVALDGYMRILTETFLE 95
Cdd:cd08651 22 GGEVVGVITlddsssnnDSDYLDLDSFARKNGIP--YYKFTDINDEE-----IIEWIKEANPDIIFVFGWSQLLKPEILA 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506268592 96 ETPT-TLNVHPALLPAFKGMDVHEDVLEAGVRMTGCTVHVVDESVDDGPIVTQEPVPVREGDTVEDLKERVLY 167
Cdd:cd08651 95 IPRLgVIGFHPTKLPKNRGRAPIPWAILLGLKETASTFFWMDEGADSGDILSQEPFPIDKDDTANSLYDKIME 167
|
|
| FMT_core_like_2 |
cd08822 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
104-184 |
6.37e-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: 187724 [Multi-domain] Cd Length: 192 Bit Score: 55.93 E-value: 6.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 104 HPALLPAFKGMDVHEDVLEAGVRMTGCTVHVVDESVDDGPIVTQEPVPVREGDTVEDLKERVLYEGEFTAYPRAIQWFAE 183
Cdd:cd08822 95 HPSLLPRHRGRDAVEWTIRMRDPITGGTVYHLDDGVDGGPIAAQDWCHVRPGDTAAELWRRALAPMGVKLLTQVIDALLR 174
|
.
gi 506268592 184 D 184
Cdd:cd08822 175 G 175
|
|
| PRK06988 |
PRK06988 |
formyltransferase; |
12-194 |
4.87e-08 |
|
formyltransferase;
Pssm-ID: 235902 [Multi-domain] Cd Length: 312 Bit Score: 54.70 E-value: 4.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 12 RNLMNLADRtpgGAELSVVLTNDaDAP--------VLEKAEERGIPteVVEHEASESREAHEqRVLDALADYEFDLvald 83
Cdd:PRK06988 16 RCLQVLLAR---GVDVALVVTHE-DNPteniwfgsVAAVAAEHGIP--VITPADPNDPELRA-AVAAAAPDFIFSF---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 84 gYMRILTETFLEETPT--TLNVHPALLPAFKG-MDVHEDVLEaGVRMTGCTVHVVDESVDDGPIVTQEPVPVREGDTVED 160
Cdd:PRK06988 85 -YYRHMIPVDLLALAPrgAYNMHGSLLPKYRGrVPVNWAVLN-GETETGATLHEMVAKPDAGAIVDQTAVPILPDDTAAQ 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 506268592 161 LKERVLYEGEFT---AYPRAIQWFAeDRVEIDWEEGT 194
Cdd:PRK06988 163 VFDKVTVAAEQTlwrVLPALLAGEA-PHLPNDLAQGS 198
|
|
| FMT_core_like_5 |
cd08823 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
102-169 |
1.06e-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: 48.98 E-value: 1.06e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506268592 102 NVHPALLPAFKGMDVHEDVLEAGVRMTGCTVHVVDESVDDGPIVTQEPVPVREGDTVEDLKERVLYEG 169
Cdd:cd08823 98 NLHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMTAEIDRGPIVLEQFTPIHPDDTYGLLCSRLAMLA 165
|
|
| FMT_core_FDH_N |
cd08647 |
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ... |
104-183 |
9.11e-06 |
|
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family represents the N-terminal hydrolase domain of the bifunctional protein 10-formyltetrahydrofolate dehydrogenase (FDH). This domain contains a 10-formyl-tetrahydrofolate (10-formyl-THF) binding site and shares sequence homology and structural topology with other enzymes utilizing this substrate. This domain functions as a hydrolase, catalyzing the conversion of 10-formyl-THF, a precursor for nucleotide biosynthesis, to tetrahydrofolate (THF). The overall FDH reaction mechanism is a coupling of two sequential reactions, a hydrolase and a formyl dehydrogenase, bridged by a substrate transfer step. The N-terminal hydrolase domain removes the formyl group from 10-formyl-THF and the C-terminal NADP-dependent dehydrogenase domain then reduces the formyl group to carbon dioxide. The two catalytic domains are connected by a third intermediate linker domain that transfers the formyl group, covalently attached to the sulfhydryl group of the phosphopantetheine arm, from the N-terminal domain to the C-terminal domain.
Pssm-ID: 187716 [Multi-domain] Cd Length: 203 Bit Score: 46.67 E-value: 9.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 104 HPALLPAFKGMDVHEDVLEAGVRMTGCTVHVVDESVDDGPIVTQEPVPVREGDTVEDLKERVLYEGEFTAYPRAIQWFAE 183
Cdd:cd08647 106 HPSILPRHRGASAINWTLIHGDKKAGFTIFWADDGLDTGPILLQKECDVLPNDTVDTLYNRFLYPEGIKAMVEAVRLIAE 185
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|
| PRK08125 |
PRK08125 |
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ... |
24-167 |
2.13e-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: 44.20 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268592 24 GAELSVVLTNdADAP--------VLEKAEERGIPT---EVVEHEASESReaheqrvLDALA-DYEFDLValdgYMRILTE 91
Cdd:PRK08125 23 GYEIAAVFTH-TDNPgenhffgsVARLAAELGIPVyapEDVNHPLWVER-------IRELApDVIFSFY----YRNLLSD 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506268592 92 TFLEETPT-TLNVHPALLPAFKGMDVHEDVLEAGVRMTGCTVHVVDESVDDGPIVTQEPVPVREGDTVEDLKERVLY 167
Cdd:PRK08125 91 EILQLAPAgAFNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQQRVAIAPDDTALTLHHKLCH 167
|
|
| PRK07579 |
PRK07579 |
dTDP-4-amino-4,6-dideoxyglucose formyltransferase; |
101-166 |
7.70e-04 |
|
dTDP-4-amino-4,6-dideoxyglucose formyltransferase;
Pssm-ID: 236058 [Multi-domain] Cd Length: 245 Bit Score: 41.43 E-value: 7.70e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506268592 101 LNVHPALLPAFKGMDVHEDVLEAGVRMtGCTVHVVDESVDDGPIVTQEPVPVREGDTVEDLKERVL 166
Cdd:PRK07579 89 INIHPGFNPYNRGWFPQVFSIINGLKI-GATIHEMDEQLDHGPIIAQREVEIESWDSSGSVYARVM 153
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