|
Name |
Accession |
Description |
Interval |
E-value |
| HisF |
COG0107 |
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ... |
2-258 |
4.61e-164 |
|
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; Imidazole glycerol phosphate synthase subunit HisF is part of the Pathway/BioSystem: Histidine biosynthesis
Pssm-ID: 439877 Cd Length: 251 Bit Score: 454.10 E-value: 4.61e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 2 LAKRVIPCLDVKDGRVVKGVNFVSLRDAGDPVELARAYDREGADEVVFLDITATSDNRATTIEMAAHAAEELVIPYTVGG 81
Cdd:COG0107 1 LAKRIIPCLDVKDGRVVKGVNFVNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRKTMLDVVRRVAEEVFIPLTVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 82 GFRDLAGMRTMVAAGADKVSLNSAAVRDPSLISQAAAAFGSQAVVVAIDAKRVGlpgqpdADKWEVFTAGGRNATGIDAV 161
Cdd:COG0107 81 GIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAIDAKRVP------DGGWEVYTHGGRKPTGLDAV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 162 AWAEEAARRGAGEILLTSMDRDGTKAGFDLALTRAVARAVPIPVIASGGVGTLEHFAEGVIEGEADAVLAASVFHFGTFS 241
Cdd:COG0107 155 EWAKEAEELGAGEILLTSMDRDGTKDGYDLELTRAVSEAVSIPVIASGGAGTLEHFVEVFTEGGADAALAASIFHFGEIT 234
|
250
....*....|....*..
gi 1221321412 242 IRQVKEYMASQGIPVRL 258
Cdd:COG0107 235 IAELKAYLAEAGIPVRL 251
|
|
| HisF |
cd04731 |
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ... |
4-252 |
8.59e-139 |
|
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria.
Pssm-ID: 240082 Cd Length: 243 Bit Score: 389.90 E-value: 8.59e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 4 KRVIPCLDVKDGRVVKGVNFVSLRDAGDPVELARAYDREGADEVVFLDITATSDNRATTIEMAAHAAEELVIPYTVGGGF 83
Cdd:cd04731 1 KRIIPCLDVKDGRVVKGVNFKNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRETMLDVVERVAEEVFIPLTVGGGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 84 RDLAGMRTMVAAGADKVSLNSAAVRDPSLISQAAAAFGSQAVVVAIDAKRVGLPGqpdadkWEVFTAGGRNATGIDAVAW 163
Cdd:cd04731 81 RSLEDARRLLRAGADKVSINSAAVENPELIREIAKRFGSQCVVVSIDAKRRGDGG------YEVYTHGGRKPTGLDAVEW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 164 AEEAARRGAGEILLTSMDRDGTKAGFDLALTRAVARAVPIPVIASGGVGTLEHFAEGVIEGEADAVLAASVFHFGTFSIR 243
Cdd:cd04731 155 AKEVEELGAGEILLTSMDRDGTKKGYDLELIRAVSSAVNIPVIASGGAGKPEHFVEAFEEGGADAALAASIFHFGEYTIA 234
|
....*....
gi 1221321412 244 QVKEYMASQ 252
Cdd:cd04731 235 ELKEYLAER 243
|
|
| hisF |
TIGR00735 |
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ... |
1-257 |
1.06e-132 |
|
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273241 Cd Length: 254 Bit Score: 374.78 E-value: 1.06e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 1 MLAKRVIPCLDVKDGRVVKGVNFVSLRDAGDPVELARAYDREGADEVVFLDITATSDNRATTIEMAAHAAEELVIPYTVG 80
Cdd:TIGR00735 1 MLAKRIIPCLDVRDGRVVKGVQFLNLRDAGDPVELAQRYDEEGADELVFLDITASSEGRTTMIDVVERTAETVFIPLTVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 81 GGFRDLAGMRTMVAAGADKVSLNSAAVRDPSLISQAAAAFGSQAVVVAIDAKRVGLPGQPdadKWEVFTAGGRNATGIDA 160
Cdd:TIGR00735 81 GGIKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFGSQCIVVAIDAKRVYVNSYC---WYEVYIYGGRESTGLDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 161 VAWAEEAARRGAGEILLTSMDRDGTKAGFDLALTRAVARAVPIPVIASGGVGTLEHFAEGVIEGEADAVLAASVFHFGTF 240
Cdd:TIGR00735 158 VEWAKEVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEAVKIPVIASGGAGKPEHFYEAFTKGKADAALAASVFHYREI 237
|
250
....*....|....*..
gi 1221321412 241 SIRQVKEYMASQGIPVR 257
Cdd:TIGR00735 238 TIGEVKEYLAERGIPVR 254
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
5-241 |
4.00e-100 |
|
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine biosynthesis pathway are contained in this family. Histidine is formed by several complex and distinct biochemical reactions catalyzed by eight enzymes. The enzymes in this Pfam entry are called His6 and His7 in eukaryotes and HisA and HisF in prokaryotes. The structure of HisA is known to be a TIM barrel fold. In some archaeal HisA proteins the TIM barrel is composed of two tandem repeats of a half barrel. This family belong to the common phosphate binding site TIM barrel family.
Pssm-ID: 425971 Cd Length: 228 Bit Score: 291.30 E-value: 4.00e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 5 RVIPCLDVKDGRVV---KGVNFVSLRDAGDPVELARAYDREGADEVVFLDITATSDNRATTIEMAAHAAEELVIPYTVGG 81
Cdd:pfam00977 1 RIIPAIDLKDGRVVrlvKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 82 GFRDLAGMRTMVAAGADKVSLNSAAVRDPSLISQAAAAFGSQAVVVAIDAKRVglpgqpdadkwEVFTAGGRNATGIDAV 161
Cdd:pfam00977 81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAIDARRG-----------KVAINGWREDTGIDAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 162 AWAEEAARRGAGEILLTSMDRDGTKAGFDLALTRAVARAVPIPVIASGGVGTLEHFAEGVIEGeADAVLAASVFHFGTFS 241
Cdd:pfam00977 150 EWAKELEELGAGEILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELFTEG-VDGVIAGSALYEGEIT 228
|
|
| AglZ_HisF2_fam |
NF038364 |
AglZ/HisF2 family acetamidino modification protein; |
2-237 |
3.32e-82 |
|
AglZ/HisF2 family acetamidino modification protein;
Pssm-ID: 439657 Cd Length: 248 Bit Score: 246.62 E-value: 3.32e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 2 LAKRVIPCLDVKDGRVVKGVNFVSLRDAGDPVELARAYDREGADEVVFLDITATSDNRATTIEMAAHAAEELVIPYTVGG 81
Cdd:NF038364 1 LRPRIIPCLLLHNGGLVKTVKFKDPKYVGDPINAVRIFNEKEVDELIVLDIDATKEGREPDYELIEDLASECFMPLCYGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 82 GFRDLAGMRTMVAAGADKVSLNSAAVRDPSLISQAAAAFGSQAVVVAIDAKRvGLPGqpdadKWEVFTAGGRNATGIDAV 161
Cdd:NF038364 81 GIKTLEQARRIFSLGVEKVALNSAALENPELITEAAEEFGSQSVVVSIDVKK-NLFG-----GYEVYTHNGTKKTKLDPV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1221321412 162 AWAEEAARRGAGEILLTSMDRDGTKAGFDLALTRAVARAVPIPVIASGGVGTLEHFAEGVIEGEADAVLAASVFHF 237
Cdd:NF038364 155 EFAKELEALGAGEIVLNSIDRDGTMKGYDLELIKKVSSAVSIPVIALGGAGSLEDLKEAIKQAGASAVAAGSLFVF 230
|
|
| PLN02617 |
PLN02617 |
imidazole glycerol phosphate synthase hisHF |
2-258 |
2.59e-58 |
|
imidazole glycerol phosphate synthase hisHF
Pssm-ID: 178226 [Multi-domain] Cd Length: 538 Bit Score: 193.77 E-value: 2.59e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 2 LAKRVIPCLDVK-----DGRVVKGVNF--------VSLRDAGDPVELARAYDREGADEVVFLDITATSD---NRATTIEM 65
Cdd:PLN02617 226 LAKRVIACLDVRsndkgDLVVTKGDQYdvrehsegREVRNLGKPVELAGQYYKDGADEVAFLNITGFRDfplGDLPMLEV 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 66 AAHAAEELVIPYTVGGGFRDL--AGMRTMVA---------AGADKVSLNSAAVR------------DPSLISQAAAAFGS 122
Cdd:PLN02617 306 LRRASENVFVPLTVGGGIRDFtdANGRYYSSlevaseyfrSGADKISIGSDAVYaaeeyiasgvktGKTSIEQISRVYGN 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 123 QAVVVAIDAKRVGLPGQPDADKWEVFTA-----------------GGRNATGIDAVAWAEEAARRGAGEILLTSMDRDGT 185
Cdd:PLN02617 386 QAVVVSIDPRRVYVKDPSDVPFKTVKVTnpgpngeeyawyqctvkGGREGRPIGAYELAKAVEELGAGEILLNCIDCDGQ 465
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1221321412 186 KAGFDLALTRAVARAVPIPVIASGGVGTLEHFAEGVIEGEADAVLAASVFHFGTFSIRQVKEYMASQGIPVRL 258
Cdd:PLN02617 466 GKGFDIELVKLVSDAVTIPVIASSGAGTPEHFSDVFSKTNASAALAAGIFHRKEVPISSVKEHLLEEGIETRI 538
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HisF |
COG0107 |
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ... |
2-258 |
4.61e-164 |
|
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; Imidazole glycerol phosphate synthase subunit HisF is part of the Pathway/BioSystem: Histidine biosynthesis
Pssm-ID: 439877 Cd Length: 251 Bit Score: 454.10 E-value: 4.61e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 2 LAKRVIPCLDVKDGRVVKGVNFVSLRDAGDPVELARAYDREGADEVVFLDITATSDNRATTIEMAAHAAEELVIPYTVGG 81
Cdd:COG0107 1 LAKRIIPCLDVKDGRVVKGVNFVNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRKTMLDVVRRVAEEVFIPLTVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 82 GFRDLAGMRTMVAAGADKVSLNSAAVRDPSLISQAAAAFGSQAVVVAIDAKRVGlpgqpdADKWEVFTAGGRNATGIDAV 161
Cdd:COG0107 81 GIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAIDAKRVP------DGGWEVYTHGGRKPTGLDAV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 162 AWAEEAARRGAGEILLTSMDRDGTKAGFDLALTRAVARAVPIPVIASGGVGTLEHFAEGVIEGEADAVLAASVFHFGTFS 241
Cdd:COG0107 155 EWAKEAEELGAGEILLTSMDRDGTKDGYDLELTRAVSEAVSIPVIASGGAGTLEHFVEVFTEGGADAALAASIFHFGEIT 234
|
250
....*....|....*..
gi 1221321412 242 IRQVKEYMASQGIPVRL 258
Cdd:COG0107 235 IAELKAYLAEAGIPVRL 251
|
|
| HisF |
cd04731 |
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ... |
4-252 |
8.59e-139 |
|
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria.
Pssm-ID: 240082 Cd Length: 243 Bit Score: 389.90 E-value: 8.59e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 4 KRVIPCLDVKDGRVVKGVNFVSLRDAGDPVELARAYDREGADEVVFLDITATSDNRATTIEMAAHAAEELVIPYTVGGGF 83
Cdd:cd04731 1 KRIIPCLDVKDGRVVKGVNFKNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRETMLDVVERVAEEVFIPLTVGGGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 84 RDLAGMRTMVAAGADKVSLNSAAVRDPSLISQAAAAFGSQAVVVAIDAKRVGLPGqpdadkWEVFTAGGRNATGIDAVAW 163
Cdd:cd04731 81 RSLEDARRLLRAGADKVSINSAAVENPELIREIAKRFGSQCVVVSIDAKRRGDGG------YEVYTHGGRKPTGLDAVEW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 164 AEEAARRGAGEILLTSMDRDGTKAGFDLALTRAVARAVPIPVIASGGVGTLEHFAEGVIEGEADAVLAASVFHFGTFSIR 243
Cdd:cd04731 155 AKEVEELGAGEILLTSMDRDGTKKGYDLELIRAVSSAVNIPVIASGGAGKPEHFVEAFEEGGADAALAASIFHFGEYTIA 234
|
....*....
gi 1221321412 244 QVKEYMASQ 252
Cdd:cd04731 235 ELKEYLAER 243
|
|
| hisF |
TIGR00735 |
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ... |
1-257 |
1.06e-132 |
|
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273241 Cd Length: 254 Bit Score: 374.78 E-value: 1.06e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 1 MLAKRVIPCLDVKDGRVVKGVNFVSLRDAGDPVELARAYDREGADEVVFLDITATSDNRATTIEMAAHAAEELVIPYTVG 80
Cdd:TIGR00735 1 MLAKRIIPCLDVRDGRVVKGVQFLNLRDAGDPVELAQRYDEEGADELVFLDITASSEGRTTMIDVVERTAETVFIPLTVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 81 GGFRDLAGMRTMVAAGADKVSLNSAAVRDPSLISQAAAAFGSQAVVVAIDAKRVGLPGQPdadKWEVFTAGGRNATGIDA 160
Cdd:TIGR00735 81 GGIKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFGSQCIVVAIDAKRVYVNSYC---WYEVYIYGGRESTGLDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 161 VAWAEEAARRGAGEILLTSMDRDGTKAGFDLALTRAVARAVPIPVIASGGVGTLEHFAEGVIEGEADAVLAASVFHFGTF 240
Cdd:TIGR00735 158 VEWAKEVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEAVKIPVIASGGAGKPEHFYEAFTKGKADAALAASVFHYREI 237
|
250
....*....|....*..
gi 1221321412 241 SIRQVKEYMASQGIPVR 257
Cdd:TIGR00735 238 TIGEVKEYLAERGIPVR 254
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
5-241 |
4.00e-100 |
|
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine biosynthesis pathway are contained in this family. Histidine is formed by several complex and distinct biochemical reactions catalyzed by eight enzymes. The enzymes in this Pfam entry are called His6 and His7 in eukaryotes and HisA and HisF in prokaryotes. The structure of HisA is known to be a TIM barrel fold. In some archaeal HisA proteins the TIM barrel is composed of two tandem repeats of a half barrel. This family belong to the common phosphate binding site TIM barrel family.
Pssm-ID: 425971 Cd Length: 228 Bit Score: 291.30 E-value: 4.00e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 5 RVIPCLDVKDGRVV---KGVNFVSLRDAGDPVELARAYDREGADEVVFLDITATSDNRATTIEMAAHAAEELVIPYTVGG 81
Cdd:pfam00977 1 RIIPAIDLKDGRVVrlvKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 82 GFRDLAGMRTMVAAGADKVSLNSAAVRDPSLISQAAAAFGSQAVVVAIDAKRVglpgqpdadkwEVFTAGGRNATGIDAV 161
Cdd:pfam00977 81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAIDARRG-----------KVAINGWREDTGIDAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 162 AWAEEAARRGAGEILLTSMDRDGTKAGFDLALTRAVARAVPIPVIASGGVGTLEHFAEGVIEGeADAVLAASVFHFGTFS 241
Cdd:pfam00977 150 EWAKELEELGAGEILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELFTEG-VDGVIAGSALYEGEIT 228
|
|
| WbuZ |
TIGR03572 |
glycosyl amidation-associated protein WbuZ; This clade of sequences is highly similar to the ... |
1-237 |
1.30e-95 |
|
glycosyl amidation-associated protein WbuZ; This clade of sequences is highly similar to the HisF protein, but generally represents the second HisF homolog in the genome where the other is an authentic HisF observed in the context of a complete histidine biosynthesis operon. The similarity between these WbuZ sequences and true HisFs is such that often the closest match by BLAST of a WbuZ is a HisF. Only by making a multiple sequence alignment is the homology relationship among the WbuZ sequences made apparent. WbuZ genes are invariably observed in the presence of a homolog of the HisH protein (designated WbuY) and a proposed N-acetyl sugar amidotransferase designated in WbuX in E. coli, IfnA in P. aeriginosa and PseA in C. jejuni. Similarly, this trio of genes is invariably found in the context of saccharide biosynthesis loci. It has been shown that the WbuYZ homologs are not essential components of the activity expressed by WbuX, leading to the proposal that these to proteins provide ammonium ions to the amidotransferase when these are in low concentration. WbuY (like HisH) is proposed to act as a glutaminase to release ammonium. In histidine biosynthesis this is also dispensible in the presence of exogenous ammonium ion. HisH and HisF form a complex such that the ammonium ion is passed directly to HisF where it is used in an amidation reaction causing a subsequent cleavage and cyclization. In the case of WbuYZ, the ammonium ion would be passed from WbuY to WbuZ. WbuZ, being non-essential and so similar to HisF that a sugar substrate is unlikely, would function instead as a amoonium channel to the WbuX protein which does the enzymatic work.
Pssm-ID: 132611 [Multi-domain] Cd Length: 232 Bit Score: 280.31 E-value: 1.30e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 1 MLAKRVIPCLDVKDGRVVKGVNFVSLRDAGDPVELARAYDREGADEVVFLDITATSDNRATTIEMAAHAAEELVIPYTVG 80
Cdd:TIGR03572 1 MLKKRIIPCLLLKDGRLVKTVQFKDPRYIGDPVNAARIYNAKGADELIVLDIDASKRGREPLFELISNLAEECFMPLTVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 81 GGFRDLAGMRTMVAAGADKVSLNSAAVRDPSLISQAAAAFGSQAVVVAIDAKRVGLPGQpdadkWEVFTAGGRNATGIDA 160
Cdd:TIGR03572 81 GGIRSLEDAKKLLSLGADKVSINTAALENPDLIEEAARRFGSQCVVVSIDVKKELDGSD-----YKVYSDNGRRATGRDP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1221321412 161 VAWAEEAARRGAGEILLTSMDRDGTKAGFDLALTRAVARAVPIPVIASGGVGTLEHFAEGVIEGEADAVLAASVFHF 237
Cdd:TIGR03572 156 VEWAREAEQLGAGEILLNSIDRDGTMKGYDLELIKTVSDAVSIPVIALGGAGSLDDLVEVALEAGASAVAAASLFHF 232
|
|
| AglZ_HisF2_fam |
NF038364 |
AglZ/HisF2 family acetamidino modification protein; |
2-237 |
3.32e-82 |
|
AglZ/HisF2 family acetamidino modification protein;
Pssm-ID: 439657 Cd Length: 248 Bit Score: 246.62 E-value: 3.32e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 2 LAKRVIPCLDVKDGRVVKGVNFVSLRDAGDPVELARAYDREGADEVVFLDITATSDNRATTIEMAAHAAEELVIPYTVGG 81
Cdd:NF038364 1 LRPRIIPCLLLHNGGLVKTVKFKDPKYVGDPINAVRIFNEKEVDELIVLDIDATKEGREPDYELIEDLASECFMPLCYGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 82 GFRDLAGMRTMVAAGADKVSLNSAAVRDPSLISQAAAAFGSQAVVVAIDAKRvGLPGqpdadKWEVFTAGGRNATGIDAV 161
Cdd:NF038364 81 GIKTLEQARRIFSLGVEKVALNSAALENPELITEAAEEFGSQSVVVSIDVKK-NLFG-----GYEVYTHNGTKKTKLDPV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1221321412 162 AWAEEAARRGAGEILLTSMDRDGTKAGFDLALTRAVARAVPIPVIASGGVGTLEHFAEGVIEGEADAVLAASVFHF 237
Cdd:NF038364 155 EFAKELEALGAGEIVLNSIDRDGTMKGYDLELIKKVSSAVSIPVIALGGAGSLEDLKEAIKQAGASAVAAGSLFVF 230
|
|
| PLN02617 |
PLN02617 |
imidazole glycerol phosphate synthase hisHF |
2-258 |
2.59e-58 |
|
imidazole glycerol phosphate synthase hisHF
Pssm-ID: 178226 [Multi-domain] Cd Length: 538 Bit Score: 193.77 E-value: 2.59e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 2 LAKRVIPCLDVK-----DGRVVKGVNF--------VSLRDAGDPVELARAYDREGADEVVFLDITATSD---NRATTIEM 65
Cdd:PLN02617 226 LAKRVIACLDVRsndkgDLVVTKGDQYdvrehsegREVRNLGKPVELAGQYYKDGADEVAFLNITGFRDfplGDLPMLEV 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 66 AAHAAEELVIPYTVGGGFRDL--AGMRTMVA---------AGADKVSLNSAAVR------------DPSLISQAAAAFGS 122
Cdd:PLN02617 306 LRRASENVFVPLTVGGGIRDFtdANGRYYSSlevaseyfrSGADKISIGSDAVYaaeeyiasgvktGKTSIEQISRVYGN 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 123 QAVVVAIDAKRVGLPGQPDADKWEVFTA-----------------GGRNATGIDAVAWAEEAARRGAGEILLTSMDRDGT 185
Cdd:PLN02617 386 QAVVVSIDPRRVYVKDPSDVPFKTVKVTnpgpngeeyawyqctvkGGREGRPIGAYELAKAVEELGAGEILLNCIDCDGQ 465
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1221321412 186 KAGFDLALTRAVARAVPIPVIASGGVGTLEHFAEGVIEGEADAVLAASVFHFGTFSIRQVKEYMASQGIPVRL 258
Cdd:PLN02617 466 GKGFDIELVKLVSDAVTIPVIASSGAGTPEHFSDVFSKTNASAALAAGIFHRKEVPISSVKEHLLEEGIETRI 538
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
5-226 |
2.82e-42 |
|
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino acid transport and metabolism]; Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase is part of the Pathway/BioSystem: Histidine biosynthesis
Pssm-ID: 439876 Cd Length: 236 Bit Score: 144.03 E-value: 2.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 5 RVIPCLDVKDGRVV---KGV---NFVSlrdAGDPVELARAYDREGADE--VVFLDitATSDNRATTIEMAAHAAEELVIP 76
Cdd:COG0106 1 IIIPAIDLKDGKCVrlvQGDydqETVY---SDDPVEVAKRWEDAGAEWlhLVDLD--GAFAGKPVNLELIEEIAKATGLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 77 YTVGGGFRDLAGMRTMVAAGADKVSLNSAAVRDPSLISQAAAAFGSQaVVVAIDAKrvglpgqpdadKWEVFTAGGRNAT 156
Cdd:COG0106 76 VQVGGGIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFPER-IVVGLDAR-----------DGKVATDGWQETS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1221321412 157 GIDAVAWAEEAARRGAGEILLTSMDRDGTKAGFDLALTRAVARAVPIPVIASGGVGTLEHF-------AEGVIEGEA 226
Cdd:COG0106 144 GVDLEELAKRFEDAGVAAILYTDISRDGTLQGPNLELYRELAAATGIPVIASGGVSSLDDLralkelgVEGAIVGKA 220
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
5-226 |
5.67e-42 |
|
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene.
Pssm-ID: 240083 Cd Length: 234 Bit Score: 143.39 E-value: 5.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 5 RVIPCLDVKDGRVV---KG----VNFVSlrdaGDPVELARAYDREGAD--EVVFLD--ITATSDNRATTIEMAahaaEEL 73
Cdd:cd04732 1 IIIPAIDLKDGKCVrlyQGdydkKTVYS----DDPVEVAKKWEEAGAKwlHVVDLDgaKGGEPVNLELIEEIV----KAV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 74 VIPYTVGGGFRDLAGMRTMVAAGADKVSLNSAAVRDPSLISQAAAAFGSQAVVVAIDAkRVGlpgqpdadkwEVFTAGGR 153
Cdd:cd04732 73 GIPVQVGGGIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGGERIVVGLDA-KDG----------KVATKGWL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 154 NATGIDAVAWAEEAARRGAGEILLTSMDRDGTKAGFDLALTRAVARAVPIPVIASGGVGTLEHF-------AEGVIEGEA 226
Cdd:cd04732 142 ETSEVSLEELAKRFEELGVKAIIYTDISRDGTLSGPNFELYKELAAATGIPVIASGGVSSLDDIkalkelgVAGVIVGKA 221
|
|
| PRK00748 |
PRK00748 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
6-226 |
6.22e-37 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated
Pssm-ID: 179108 Cd Length: 233 Bit Score: 130.19 E-value: 6.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 6 VIPCLDVKDGRVV---KGvNFVSLRD-AGDPVELARAYDREGADEVVFLDITATSDNRATTIEMAAHAAEELVIPYTVGG 81
Cdd:PRK00748 3 IIPAIDLKDGKCVrlyQG-DYDQATVySDDPVAQAKAWEDQGAKWLHLVDLDGAKAGKPVNLELIEAIVKAVDIPVQVGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 82 GFRDLAGMRTMVAAGADKVSLNSAAVRDPSLISQAAAAFGSQaVVVAIDAKrvglpgqpdadKWEVFTAGGRNATGIDAV 161
Cdd:PRK00748 82 GIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFPGK-IVVGLDAR-----------DGKVATDGWLETSGVTAE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1221321412 162 AWAEEAARRGAGEILLTSMDRDGTKAGFDLALTRAVARAVPIPVIASGGVGTLEHFA--------EGVIEGEA 226
Cdd:PRK00748 150 DLAKRFEDAGVKAIIYTDISRDGTLSGPNVEATRELAAAVPIPVIASGGVSSLDDIKalkglgavEGVIVGRA 222
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
6-226 |
2.34e-34 |
|
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family consists of HisA, phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, the enzyme catalyzing the fourth step in histidine biosynthesis. It is closely related to the enzyme HisF for the sixth step. Examples of this enzyme in Actinobacteria have been found to be bifunctional, also possessing phosphoribosylanthranilate isomerase activity; the trusted cutoff here has now been raised to 275.0 to exclude the bifunctional group, now represented by model TIGR01919. HisA from Lactococcus lactis was reported to be inactive (MEDLINE:93322317). [Amino acid biosynthesis, Histidine family]
Pssm-ID: 272850 [Multi-domain] Cd Length: 230 Bit Score: 123.46 E-value: 2.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 6 VIPCLDVKDGRVV---KGVNFVSLRDAGDPVELARAYDREGADEVVFLDITATSDNRATTIEMAAHAAEELVIPYTVGGG 82
Cdd:TIGR00007 1 IIPAIDIKDGKCVrlyQGDYDKETVYGDDPVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQVGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 83 FRDLAGMRTMVAAGADKVSLNSAAVRDPSLISQAAAAFGSQAVVVAIDAKrvglpgqpdadKWEVFTAGGRNATGIDAVA 162
Cdd:TIGR00007 81 IRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYGPERIVVSLDAR-----------GGEVAVKGWLEKSEVSLEE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1221321412 163 WAEEAARRGAGEILLTSMDRDGTKAGFDLALTRAVARAVPIPVIASGGVGTLE--HFA-----EGVIEGEA 226
Cdd:TIGR00007 150 LAKRLEELGLEGIIYTDISRDGTLSGPNFELTKELVKAVNVPVIASGGVSSIDdlIALkklgvYGVIVGKA 220
|
|
| HisA_HisF |
cd04723 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ... |
5-247 |
4.46e-34 |
|
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) and the cyclase subunit of imidazoleglycerol phosphate synthase (HisF). The ProFAR isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene. The Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria.
Pssm-ID: 240074 [Multi-domain] Cd Length: 233 Bit Score: 122.76 E-value: 4.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 5 RVIPCLDVKDGRVVKGV------------NFVSLrdaGDPVELARAYDREGADEVVFLDITA---TSDNRattiEMAAHA 69
Cdd:cd04723 1 RIIPVIDLKDGVVVHGVggdrdnyrpitsNLCST---SDPLDVARAYKELGFRGLYIADLDAimgRGDND----EAIREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 70 AEELVIPYTVGGGFRDLAGMRTMVAAGADKVSLNSAAVRDpSLISQAAAAFGSQAVVVAIDAKRvglpGQPDADKWevft 149
Cdd:cd04723 74 AAAWPLGLWVDGGIRSLENAQEWLKRGASRVIVGTETLPS-DDDEDRLAALGEQRLVLSLDFRG----GQLLKPTD---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 150 aggrnatGIDAVAWAEEAARRgAGEILLTSMDRDGTKAGFDLALTRAVARAVPIPVIASGGVGTLEHFAEGVIEGeADAV 229
Cdd:cd04723 145 -------FIGPEELLRRLAKW-PEELIVLDIDRVGSGQGPDLELLERLAARADIPVIAAGGVRSVEDLELLKKLG-ASGA 215
|
250
....*....|....*...
gi 1221321412 230 LAASVFHFGTFSIRQVKE 247
Cdd:cd04723 216 LVASALHDGGLTLEDVVR 233
|
|
| PRK13585 |
PRK13585 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ... |
6-215 |
9.63e-32 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase;
Pssm-ID: 184165 Cd Length: 241 Bit Score: 116.93 E-value: 9.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 6 VIPCLDVKDGRVVK---GVNFVSLRDAGDPVELARAYDREGADEVVFLDITATSDNRATTIEMAAHAAEELVIPYTVGGG 82
Cdd:PRK13585 5 VIPAVDMKGGKCVQlvqGEPGTETVSYGDPVEVAKRWVDAGAETLHLVDLDGAFEGERKNAEAIEKIIEAVGVPVQLGGG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 83 FRDLAGMRTMVAAGADKVSLNSAAVRDPSLISQAAAAFGSQAVVVAIDAKrvglpgqpdadKWEVFTAGGRNATGIDAVA 162
Cdd:PRK13585 85 IRSAEDAASLLDLGVDRVILGTAAVENPEIVRELSEEFGSERVMVSLDAK-----------DGEVVIKGWTEKTGYTPVE 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1221321412 163 WAEEAARRGAGEILLTSMDRDGTKAGFDLALTRAVARAVPIPVIASGGVGTLE 215
Cdd:PRK13585 154 AAKRFEELGAGSILFTNVDVEGLLEGVNTEPVKELVDSVDIPVIASGGVTTLD 206
|
|
| PRK14024 |
PRK14024 |
phosphoribosyl isomerase A; Provisional |
7-226 |
1.16e-16 |
|
phosphoribosyl isomerase A; Provisional
Pssm-ID: 237589 Cd Length: 241 Bit Score: 76.92 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 7 IPCLDVKDGRVVKGVNFV--SLRDAGDPVELARAYDREGADEVVFLDITAtSDNRATTIEMAAHAAEELVIPYTVGGGFR 84
Cdd:PRK14024 7 LPAVDVVDGQAVRLVQGEagSETSYGSPLDAALAWQRDGAEWIHLVDLDA-AFGRGSNRELLAEVVGKLDVKVELSGGIR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 85 DLAGMRTMVAAGADKVSLNSAAVRDPSLISQAAAAFGSQaVVVAIDAKRVGLPG----QPDADKWEVFtaggrnatgida 160
Cdd:PRK14024 86 DDESLEAALATGCARVNIGTAALENPEWCARVIAEHGDR-VAVGLDVRGHTLAArgwtRDGGDLWEVL------------ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1221321412 161 vawaEEAARRGAGEILLTSMDRDGTKAGFDLALTRAVARAVPIPVIASGGVGTLEHFA----------EGVIEGEA 226
Cdd:PRK14024 153 ----ERLDSAGCSRYVVTDVTKDGTLTGPNLELLREVCARTDAPVVASGGVSSLDDLRalaelvplgvEGAIVGKA 224
|
|
| PRK14114 |
PRK14114 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
6-248 |
7.20e-12 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 172604 Cd Length: 241 Bit Score: 63.49 E-value: 7.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 6 VIPCLDV---KDGRVVKGVNFVSLRDAGDPVELARAYDREGADEVVFLDIT---ATSDNRATTIEMAAHAAEELVIpytv 79
Cdd:PRK14114 3 VVPAIDLfrgKVARMVKGKKENTIFYEKDPAELVEKLIEEGFTLIHVVDLSkaiENSVENLPVLEKLSEFAEHIQI---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 80 GGGFRDLAGMRTMVAAGADKVSLNSAAVRDPSLIsQAAAAFGSQAVVvAIDAK--RVGLPGQPDADKwevftaggrnatg 157
Cdd:PRK14114 79 GGGIRSLDYAEKLRKLGYRRQIVSSKVLEDPSFL-KFLKEIDVEPVF-SLDTRggKVAFKGWLAEEE------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 158 IDAVAWAEEAARRGAGEILLTSMDRDGTKAGFDLALTRAVARAVPIPVIASGGVGTLEHFAEGV-----IEGEADAVLAA 232
Cdd:PRK14114 144 IDPVSLLKRLKEYGLEEIVHTEIEKDGTLQEHDFSLTRKIAIEAEVKVFAAGGISSENSLKTAQrvhreTNGLLKGVIVG 223
|
250
....*....|....*.
gi 1221321412 233 SVFHFGTFSIRQVKEY 248
Cdd:PRK14114 224 RAFLEGILTVEVMKRY 239
|
|
| PRK13587 |
PRK13587 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
76-211 |
2.80e-08 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Provisional
Pssm-ID: 172156 Cd Length: 234 Bit Score: 52.91 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 76 PYTVGGGFRDLAGMRTMVAAGADKVSLNSAAVRDPSLISQAAAAFGSQaVVVAIDAKRVglpgqpdadkwEVFTAGGRNA 155
Cdd:PRK13587 78 DIEVGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGR-IYLSVDAYGE-----------DIKVNGWEED 145
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1221321412 156 TGIDAVAWAEEAARRGAGEILLTSMDRDGTKAGFDLALTRAVARAVPIPVIASGGV 211
Cdd:PRK13587 146 TELNLFSFVRQLSDIPLGGIIYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGGI 201
|
|
| PRK13586 |
PRK13586 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
5-215 |
3.21e-07 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 237439 Cd Length: 232 Bit Score: 49.74 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 5 RVIPCLDVKDGRVVKGVNFV--SLRDAGDPVELARAYDREGADEVVFLDITATS---DNRATTIEMAAHAAEELvipyTV 79
Cdd:PRK13586 3 KIIPSIDISLGKAVKRIRGVkgTGLILGNPIEIASKLYNEGYTRIHVVDLDAAEgvgNNEMYIKEISKIGFDWI----QV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 80 GGGFRDLAGMRTMVAAGADKVSLNSAAVRDPSLISQAAAAFGSQAVVVAID---AKRVGLPGqpdadkWEvftagGRNAT 156
Cdd:PRK13586 79 GGGIRDIEKAKRLLSLDVNALVFSTIVFTNFNLFHDIVREIGSNRVLVSIDydnTKRVLIRG------WK-----EKSME 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1221321412 157 GIDAVAWAEEAARRGageILLTSMDRDGTKAGFDLALTRAVARAVPIPVIAsGGVGTLE 215
Cdd:PRK13586 148 VIDGIKKVNELELLG---IIFTYISNEGTTKGIDYNVKDYARLIRGLKEYA-GGVSSDA 202
|
|
| PRK04128 |
PRK04128 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
5-190 |
3.37e-07 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 167709 Cd Length: 228 Bit Score: 49.77 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 5 RVIPCLDVKDGRVVKGVN--FVSLRDAGDPVELARAYdREGADEVVFLDITATSDNRATTIEMAAHAAEELVIPYTVGGG 82
Cdd:PRK04128 3 RIYPAIDLMNGKAVRLYKgrKEEVKVYGDPVEIALRF-SEYVDKIHVVDLDGAFEGKPKNLDVVKNIIRETGLKVQVGGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 83 FRDLAGMRTMVAAGADKVSLNSAAVrDPSLISQAAAAFGSqaVVVAIDAKrvglpgqpdadKWEVFTAGGRNATGIDAVA 162
Cdd:PRK04128 82 LRTYESIKDAYEIGVENVIIGTKAF-DLEFLEKVTSEFEG--ITVSLDVK-----------GGRIAVKGWLEESSIKVED 147
|
170 180
....*....|....*....|....*...
gi 1221321412 163 wAEEAARRGAGEILLTSMDRDGTKAGFD 190
Cdd:PRK04128 148 -AYEMLKNYVNRFIYTSIERDGTLTGIE 174
|
|
| PLN02446 |
PLN02446 |
(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
8-215 |
1.72e-06 |
|
(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase
Pssm-ID: 215245 Cd Length: 262 Bit Score: 47.78 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 8 PCLDVKDGRVVKGV-------------------NFVSLRDAGdpvELARAYDREG--ADEVVFLditaTSDNRATTIEMA 66
Cdd:PLN02446 5 PCIDIHKGKVKQIVgstlkdskdgsedgselvtNFESDKSAA---EFAEMYKRDGltGGHVIML----GADDASLAAALE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 67 AHAAeelvIPYT--VGGGFRDLAGMRtMVAAGADKVSLNSAAVRDPSL----ISQAAAAFGSQAVVVAIDAKRVGLPGQP 140
Cdd:PLN02446 78 ALRA----YPGGlqVGGGVNSENAMS-YLDAGASHVIVTSYVFRDGQIdlerLKDLVRLVGKQRLVLDLSCRKKDGRYYV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1221321412 141 DADKWEVFTAggrnatgidaVAWAEEAARRGAG---EILLTSMDRDGTKAGFDLALTRAVARAVPIPVIASGGVGTLE 215
Cdd:PLN02446 153 VTDRWQKFSD----------LAVDEETLEFLAAycdEFLVHGVDVEGKRLGIDEELVALLGEHSPIPVTYAGGVRSLD 220
|
|
| FadH |
COG1902 |
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ... |
159-229 |
3.06e-05 |
|
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family [Energy production and conversion];
Pssm-ID: 441506 [Multi-domain] Cd Length: 365 Bit Score: 44.39 E-value: 3.06e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1221321412 159 DAVAWAEEAARRGA-------GEILLTSMDRDGTKAGFDLALTRAVARAVPIPVIASGGVGTLEHfAEGVIE-GEADAV 229
Cdd:COG1902 237 ESVELAKALEEAGVdylhvssGGYEPDAMIPTIVPEGYQLPFAARIRKAVGIPVIAVGGITTPEQ-AEAALAsGDADLV 314
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
25-233 |
1.91e-04 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 41.42 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 25 SLRDAGDPVELARAYDREGADEVVFLDITATSDNRATTI-EMAAHAAEELVIPYTVGGGFRDLAGMRTMVA-----AGAD 98
Cdd:cd04722 7 AGGPSGDPVELAKAAAEAGADAIIVGTRSSDPEEAETDDkEVLKEVAAETDLPLGVQLAINDAAAAVDIAAaaaraAGAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 99 KVSLNSAAVR----DPSLISQAAAAFGSQAVVVAIDAKRVGLPGQpdadkWEVFTAGGRNATGIDAVAWAEEAARRgage 174
Cdd:cd04722 87 GVEIHGAVGYlareDLELIRELREAVPDVKVVVKLSPTGELAAAA-----AEEAGVDEVGLGNGGGGGGGRDAVPI---- 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1221321412 175 illtsmdrdgtkagfDLALTRAVARAVPIPVIASGGVGTLEHFAEGVIEGeADAVLAAS 233
Cdd:cd04722 158 ---------------ADLLLILAKRGSKVPVIAGGGINDPEDAAEALALG-ADGVIVGS 200
|
|
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
146-229 |
2.10e-04 |
|
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.
Pssm-ID: 239201 [Multi-domain] Cd Length: 327 Bit Score: 41.79 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221321412 146 EVFTAGGRNATGIDAVAWAEEAA------RRGAGEILLTSMDRDGTKAGFDLALTRAVARAVPIPVIASGGVGTLEHFAE 219
Cdd:cd02803 219 DFVPGGLTLEEAIEIAKALEEAGvdalhvSGGSYESPPPIIPPPYVPEGYFLELAEKIKKAVKIPVIAVGGIRDPEVAEE 298
|
90
....*....|
gi 1221321412 220 GVIEGEADAV 229
Cdd:cd02803 299 ILAEGKADLV 308
|
|
| |
