|
Name |
Accession |
Description |
Interval |
E-value |
| HisF |
COG0107 |
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ... |
2-252 |
5.49e-142 |
|
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: 397.86 E-value: 5.49e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 2 LTKRIIPCLDVDQGRVKKGVHFIQLKDVGDPVAIAKAYEAQGADELVFLDITATTDARQTMTQTVAAVATQVFMPLTVGG 81
Cdd:COG0107 1 LAKRIIPCLDVKDGRVVKGVNFVNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRKTMLDVVRRVAEEVFIPLTVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 82 GIRSVTDMHQLLRAGADKIALNSAAVKHPDLITAGAEKFGRQAIVVAIDARWQPSrNRYQVMINGGRTPVDLGVLTWAQQ 161
Cdd:COG0107 81 GIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAIDAKRVPD-GGWEVYTHGGRKPTGLDAVEWAKE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 162 AVAAGAGELLITSMDADGTKQGFDLRLYQQLSSIVSVPVVASGGAGSANDFVTLFRDTNVSAGLAASIFHFGELTIPQVK 241
Cdd:COG0107 160 AEELGAGEILLTSMDRDGTKDGYDLELTRAVSEAVSIPVIASGGAGTLEHFVEVFTEGGADAALAASIFHFGEITIAELK 239
|
250
....*....|.
gi 491954436 242 TVLKQAKVAIR 252
Cdd:COG0107 240 AYLAEAGIPVR 250
|
|
| HisF |
cd04731 |
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ... |
4-245 |
5.00e-125 |
|
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: 354.85 E-value: 5.00e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 4 KRIIPCLDVDQGRVKKGVHFIQLKDVGDPVAIAKAYEAQGADELVFLDITATTDARQTMTQTVAAVATQVFMPLTVGGGI 83
Cdd:cd04731 1 KRIIPCLDVKDGRVVKGVNFKNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRETMLDVVERVAEEVFIPLTVGGGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 84 RSVTDMHQLLRAGADKIALNSAAVKHPDLITAGAEKFGRQAIVVAIDARWQPSrNRYQVMINGGRTPVDLGVLTWAQQAV 163
Cdd:cd04731 81 RSLEDARRLLRAGADKVSINSAAVENPELIREIAKRFGSQCVVVSIDAKRRGD-GGYEVYTHGGRKPTGLDAVEWAKEVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 164 AAGAGELLITSMDADGTKQGFDLRLYQQLSSIVSVPVVASGGAGSANDFVTLFRDTNVSAGLAASIFHFGELTIPQVKTV 243
Cdd:cd04731 160 ELGAGEILLTSMDRDGTKKGYDLELIRAVSSAVNIPVIASGGAGKPEHFVEAFEEGGADAALAASIFHFGEYTIAELKEY 239
|
..
gi 491954436 244 LK 245
Cdd:cd04731 240 LA 241
|
|
| hisF |
TIGR00735 |
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ... |
1-252 |
8.86e-112 |
|
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273241 Cd Length: 254 Bit Score: 321.62 E-value: 8.86e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 1 MLTKRIIPCLDVDQGRVKKGVHFIQLKDVGDPVAIAKAYEAQGADELVFLDITATTDARQTMTQTVAAVATQVFMPLTVG 80
Cdd:TIGR00735 1 MLAKRIIPCLDVRDGRVVKGVQFLNLRDAGDPVELAQRYDEEGADELVFLDITASSEGRTTMIDVVERTAETVFIPLTVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 81 GGIRSVTDMHQLLRAGADKIALNSAAVKHPDLITAGAEKFGRQAIVVAIDARWQP--SRNRYQVMINGGRTPVDLGVLTW 158
Cdd:TIGR00735 81 GGIKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFGSQCIVVAIDAKRVYvnSYCWYEVYIYGGRESTGLDAVEW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 159 AQQAVAAGAGELLITSMDADGTKQGFDLRLYQQLSSIVSVPVVASGGAGSANDFVTLFRDTNVSAGLAASIFHFGELTIP 238
Cdd:TIGR00735 161 AKEVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEAVKIPVIASGGAGKPEHFYEAFTKGKADAALAASVFHYREITIG 240
|
250
....*....|....
gi 491954436 239 QVKTVLKQAKVAIR 252
Cdd:TIGR00735 241 EVKEYLAERGIPVR 254
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
5-236 |
3.28e-90 |
|
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: 265.88 E-value: 3.28e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 5 RIIPCLDVDQGRV---KKGVHFIQLKDVGDPVAIAKAYEAQGADELVFLDITATTDARQTMTQTVAAVATQVFMPLTVGG 81
Cdd:pfam00977 1 RIIPAIDLKDGRVvrlVKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 82 GIRSVTDMHQLLRAGADKIALNSAAVKHPDLITAGAEKFGRQAIVVAIDARWQpsrnryQVMINGGRTPVDLGVLTWAQQ 161
Cdd:pfam00977 81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAIDARRG------KVAINGWREDTGIDAVEWAKE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491954436 162 AVAAGAGELLITSMDADGTKQGFDLRLYQQLSSIVSVPVVASGGAGSANDFVTLFRdTNVSAGLAASIFHFGELT 236
Cdd:pfam00977 155 LEELGAGEILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELFT-EGVDGVIAGSALYEGEIT 228
|
|
| AglZ_HisF2_fam |
NF038364 |
AglZ/HisF2 family acetamidino modification protein; |
2-232 |
3.78e-72 |
|
AglZ/HisF2 family acetamidino modification protein;
Pssm-ID: 439657 Cd Length: 248 Bit Score: 220.81 E-value: 3.78e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 2 LTKRIIPCLDVDQGRVKKGVHFIQLKDVGDPVAIAKAYEAQGADELVFLDITATTDARQTMTQTVAAVATQVFMPLTVGG 81
Cdd:NF038364 1 LRPRIIPCLLLHNGGLVKTVKFKDPKYVGDPINAVRIFNEKEVDELIVLDIDATKEGREPDYELIEDLASECFMPLCYGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 82 GIRSVTDMHQLLRAGADKIALNSAAVKHPDLITAGAEKFGRQAIVVAIDARWQPSRnRYQVMINGGRTPVDLGVLTWAQQ 161
Cdd:NF038364 81 GIKTLEQARRIFSLGVEKVALNSAALENPELITEAAEEFGSQSVVVSIDVKKNLFG-GYEVYTHNGTKKTKLDPVEFAKE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491954436 162 AVAAGAGELLITSMDADGTKQGFDLRLYQQLSSIVSVPVVASGGAGSANDFVTLFRDTNVSAGLAASIFHF 232
Cdd:NF038364 160 LEALGAGEIVLNSIDRDGTMKGYDLELIKKVSSAVSIPVIALGGAGSLEDLKEAIKQAGASAVAAGSLFVF 230
|
|
| PLN02617 |
PLN02617 |
imidazole glycerol phosphate synthase hisHF |
2-252 |
2.33e-50 |
|
imidazole glycerol phosphate synthase hisHF
Pssm-ID: 178226 [Multi-domain] Cd Length: 538 Bit Score: 172.59 E-value: 2.33e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 2 LTKRIIPCLDV---DQGR--VKKGVHF--------IQLKDVGDPVAIAKAYEAQGADELVFLDITATTDARQT---MTQT 65
Cdd:PLN02617 226 LAKRVIACLDVrsnDKGDlvVTKGDQYdvrehsegREVRNLGKPVELAGQYYKDGADEVAFLNITGFRDFPLGdlpMLEV 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 66 VAAVATQVFMPLTVGGGIRSVTD-----------MHQLLRAGADKIALNSAAV-KHPDLITAG-----------AEKFGR 122
Cdd:PLN02617 306 LRRASENVFVPLTVGGGIRDFTDangryysslevASEYFRSGADKISIGSDAVyAAEEYIASGvktgktsieqiSRVYGN 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 123 QAIVVAIDAR-----------------WQPSRNR-----YQVMINGGRTPVDLGVLTWAQQAVAAGAGELLITSMDADGT 180
Cdd:PLN02617 386 QAVVVSIDPRrvyvkdpsdvpfktvkvTNPGPNGeeyawYQCTVKGGREGRPIGAYELAKAVEELGAGEILLNCIDCDGQ 465
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491954436 181 KQGFDLRLYQQLSSIVSVPVVASGGAGSANDFVTLFRDTNVSAGLAASIFHFGELTIPQVKTVLKQAKVAIR 252
Cdd:PLN02617 466 GKGFDIELVKLVSDAVTIPVIASSGAGTPEHFSDVFSKTNASAALAAGIFHRKEVPISSVKEHLLEEGIETR 537
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HisF |
COG0107 |
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ... |
2-252 |
5.49e-142 |
|
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: 397.86 E-value: 5.49e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 2 LTKRIIPCLDVDQGRVKKGVHFIQLKDVGDPVAIAKAYEAQGADELVFLDITATTDARQTMTQTVAAVATQVFMPLTVGG 81
Cdd:COG0107 1 LAKRIIPCLDVKDGRVVKGVNFVNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRKTMLDVVRRVAEEVFIPLTVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 82 GIRSVTDMHQLLRAGADKIALNSAAVKHPDLITAGAEKFGRQAIVVAIDARWQPSrNRYQVMINGGRTPVDLGVLTWAQQ 161
Cdd:COG0107 81 GIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAIDAKRVPD-GGWEVYTHGGRKPTGLDAVEWAKE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 162 AVAAGAGELLITSMDADGTKQGFDLRLYQQLSSIVSVPVVASGGAGSANDFVTLFRDTNVSAGLAASIFHFGELTIPQVK 241
Cdd:COG0107 160 AEELGAGEILLTSMDRDGTKDGYDLELTRAVSEAVSIPVIASGGAGTLEHFVEVFTEGGADAALAASIFHFGEITIAELK 239
|
250
....*....|.
gi 491954436 242 TVLKQAKVAIR 252
Cdd:COG0107 240 AYLAEAGIPVR 250
|
|
| HisF |
cd04731 |
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ... |
4-245 |
5.00e-125 |
|
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: 354.85 E-value: 5.00e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 4 KRIIPCLDVDQGRVKKGVHFIQLKDVGDPVAIAKAYEAQGADELVFLDITATTDARQTMTQTVAAVATQVFMPLTVGGGI 83
Cdd:cd04731 1 KRIIPCLDVKDGRVVKGVNFKNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRETMLDVVERVAEEVFIPLTVGGGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 84 RSVTDMHQLLRAGADKIALNSAAVKHPDLITAGAEKFGRQAIVVAIDARWQPSrNRYQVMINGGRTPVDLGVLTWAQQAV 163
Cdd:cd04731 81 RSLEDARRLLRAGADKVSINSAAVENPELIREIAKRFGSQCVVVSIDAKRRGD-GGYEVYTHGGRKPTGLDAVEWAKEVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 164 AAGAGELLITSMDADGTKQGFDLRLYQQLSSIVSVPVVASGGAGSANDFVTLFRDTNVSAGLAASIFHFGELTIPQVKTV 243
Cdd:cd04731 160 ELGAGEILLTSMDRDGTKKGYDLELIRAVSSAVNIPVIASGGAGKPEHFVEAFEEGGADAALAASIFHFGEYTIAELKEY 239
|
..
gi 491954436 244 LK 245
Cdd:cd04731 240 LA 241
|
|
| hisF |
TIGR00735 |
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ... |
1-252 |
8.86e-112 |
|
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273241 Cd Length: 254 Bit Score: 321.62 E-value: 8.86e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 1 MLTKRIIPCLDVDQGRVKKGVHFIQLKDVGDPVAIAKAYEAQGADELVFLDITATTDARQTMTQTVAAVATQVFMPLTVG 80
Cdd:TIGR00735 1 MLAKRIIPCLDVRDGRVVKGVQFLNLRDAGDPVELAQRYDEEGADELVFLDITASSEGRTTMIDVVERTAETVFIPLTVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 81 GGIRSVTDMHQLLRAGADKIALNSAAVKHPDLITAGAEKFGRQAIVVAIDARWQP--SRNRYQVMINGGRTPVDLGVLTW 158
Cdd:TIGR00735 81 GGIKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFGSQCIVVAIDAKRVYvnSYCWYEVYIYGGRESTGLDAVEW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 159 AQQAVAAGAGELLITSMDADGTKQGFDLRLYQQLSSIVSVPVVASGGAGSANDFVTLFRDTNVSAGLAASIFHFGELTIP 238
Cdd:TIGR00735 161 AKEVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEAVKIPVIASGGAGKPEHFYEAFTKGKADAALAASVFHYREITIG 240
|
250
....*....|....
gi 491954436 239 QVKTVLKQAKVAIR 252
Cdd:TIGR00735 241 EVKEYLAERGIPVR 254
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
5-236 |
3.28e-90 |
|
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: 265.88 E-value: 3.28e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 5 RIIPCLDVDQGRV---KKGVHFIQLKDVGDPVAIAKAYEAQGADELVFLDITATTDARQTMTQTVAAVATQVFMPLTVGG 81
Cdd:pfam00977 1 RIIPAIDLKDGRVvrlVKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 82 GIRSVTDMHQLLRAGADKIALNSAAVKHPDLITAGAEKFGRQAIVVAIDARWQpsrnryQVMINGGRTPVDLGVLTWAQQ 161
Cdd:pfam00977 81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAIDARRG------KVAINGWREDTGIDAVEWAKE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491954436 162 AVAAGAGELLITSMDADGTKQGFDLRLYQQLSSIVSVPVVASGGAGSANDFVTLFRdTNVSAGLAASIFHFGELT 236
Cdd:pfam00977 155 LEELGAGEILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELFT-EGVDGVIAGSALYEGEIT 228
|
|
| WbuZ |
TIGR03572 |
glycosyl amidation-associated protein WbuZ; This clade of sequences is highly similar to the ... |
1-232 |
1.29e-88 |
|
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: 262.21 E-value: 1.29e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 1 MLTKRIIPCLDVDQGRVKKGVHFIQLKDVGDPVAIAKAYEAQGADELVFLDITATTDARQTMTQTVAAVATQVFMPLTVG 80
Cdd:TIGR03572 1 MLKKRIIPCLLLKDGRLVKTVQFKDPRYIGDPVNAARIYNAKGADELIVLDIDASKRGREPLFELISNLAEECFMPLTVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 81 GGIRSVTDMHQLLRAGADKIALNSAAVKHPDLITAGAEKFGRQAIVVAIDARWQPSRNRYQVMINGGRTPVDLGVLTWAQ 160
Cdd:TIGR03572 81 GGIRSLEDAKKLLSLGADKVSINTAALENPDLIEEAARRFGSQCVVVSIDVKKELDGSDYKVYSDNGRRATGRDPVEWAR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491954436 161 QAVAAGAGELLITSMDADGTKQGFDLRLYQQLSSIVSVPVVASGGAGSANDFVTLFRDTNVSAGLAASIFHF 232
Cdd:TIGR03572 161 EAEQLGAGEILLNSIDRDGTMKGYDLELIKTVSDAVSIPVIALGGAGSLDDLVEVALEAGASAVAAASLFHF 232
|
|
| AglZ_HisF2_fam |
NF038364 |
AglZ/HisF2 family acetamidino modification protein; |
2-232 |
3.78e-72 |
|
AglZ/HisF2 family acetamidino modification protein;
Pssm-ID: 439657 Cd Length: 248 Bit Score: 220.81 E-value: 3.78e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 2 LTKRIIPCLDVDQGRVKKGVHFIQLKDVGDPVAIAKAYEAQGADELVFLDITATTDARQTMTQTVAAVATQVFMPLTVGG 81
Cdd:NF038364 1 LRPRIIPCLLLHNGGLVKTVKFKDPKYVGDPINAVRIFNEKEVDELIVLDIDATKEGREPDYELIEDLASECFMPLCYGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 82 GIRSVTDMHQLLRAGADKIALNSAAVKHPDLITAGAEKFGRQAIVVAIDARWQPSRnRYQVMINGGRTPVDLGVLTWAQQ 161
Cdd:NF038364 81 GIKTLEQARRIFSLGVEKVALNSAALENPELITEAAEEFGSQSVVVSIDVKKNLFG-GYEVYTHNGTKKTKLDPVEFAKE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491954436 162 AVAAGAGELLITSMDADGTKQGFDLRLYQQLSSIVSVPVVASGGAGSANDFVTLFRDTNVSAGLAASIFHF 232
Cdd:NF038364 160 LEALGAGEIVLNSIDRDGTMKGYDLELIKKVSSAVSIPVIALGGAGSLEDLKEAIKQAGASAVAAGSLFVF 230
|
|
| PLN02617 |
PLN02617 |
imidazole glycerol phosphate synthase hisHF |
2-252 |
2.33e-50 |
|
imidazole glycerol phosphate synthase hisHF
Pssm-ID: 178226 [Multi-domain] Cd Length: 538 Bit Score: 172.59 E-value: 2.33e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 2 LTKRIIPCLDV---DQGR--VKKGVHF--------IQLKDVGDPVAIAKAYEAQGADELVFLDITATTDARQT---MTQT 65
Cdd:PLN02617 226 LAKRVIACLDVrsnDKGDlvVTKGDQYdvrehsegREVRNLGKPVELAGQYYKDGADEVAFLNITGFRDFPLGdlpMLEV 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 66 VAAVATQVFMPLTVGGGIRSVTD-----------MHQLLRAGADKIALNSAAV-KHPDLITAG-----------AEKFGR 122
Cdd:PLN02617 306 LRRASENVFVPLTVGGGIRDFTDangryysslevASEYFRSGADKISIGSDAVyAAEEYIASGvktgktsieqiSRVYGN 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 123 QAIVVAIDAR-----------------WQPSRNR-----YQVMINGGRTPVDLGVLTWAQQAVAAGAGELLITSMDADGT 180
Cdd:PLN02617 386 QAVVVSIDPRrvyvkdpsdvpfktvkvTNPGPNGeeyawYQCTVKGGREGRPIGAYELAKAVEELGAGEILLNCIDCDGQ 465
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491954436 181 KQGFDLRLYQQLSSIVSVPVVASGGAGSANDFVTLFRDTNVSAGLAASIFHFGELTIPQVKTVLKQAKVAIR 252
Cdd:PLN02617 466 GKGFDIELVKLVSDAVTIPVIASSGAGTPEHFSDVFSKTNASAALAAGIFHRKEVPISSVKEHLLEEGIETR 537
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
5-222 |
7.52e-35 |
|
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: 124.51 E-value: 7.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 5 RIIPCLDVDQGRV---KKGVhFIQLKDV-GDPVAIAKAYEAQGADELVFLDITATTDARQTMTQTVAAVATQVFMPLTVG 80
Cdd:cd04732 1 IIIPAIDLKDGKCvrlYQGD-YDKKTVYsDDPVEVAKKWEEAGAKWLHVVDLDGAKGGEPVNLELIEEIVKAVGIPVQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 81 GGIRSVTDMHQLLRAGADKIALNSAAVKHPDLITAGAEKFGRQAIVVAIDArwqpsRNRYqVMINGGRTPVDLGVLTWAQ 160
Cdd:cd04732 80 GGIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGGERIVVGLDA-----KDGK-VATKGWLETSEVSLEELAK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491954436 161 QAVAAGAGELLITSMDADGTKQGFDLRLYQQLSSIVSVPVVASGGAGSANDFVTLfRDTNVS 222
Cdd:cd04732 154 RFEELGVKAIIYTDISRDGTLSGPNFELYKELAAATGIPVIASGGVSSLDDIKAL-KELGVA 214
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
5-223 |
5.13e-33 |
|
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: 119.76 E-value: 5.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 5 RIIPCLDVDQGRV---KKGVhfiqLKDV----GDPVAIAKAYEAQGADEL--VFLDitATTDARQTMTQTVAAVATQVFM 75
Cdd:COG0106 1 IIIPAIDLKDGKCvrlVQGD----YDQEtvysDDPVEVAKRWEDAGAEWLhlVDLD--GAFAGKPVNLELIEEIAKATGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 76 PLTVGGGIRSVTDMHQLLRAGADKIALNSAAVKHPDLITAGAEKFGRQaIVVAIDARwqpsrnRYQVMINGGRTPVDLGV 155
Cdd:COG0106 75 PVQVGGGIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFPER-IVVGLDAR------DGKVATDGWQETSGVDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491954436 156 LTWAQQAVAAGAGELLITSMDADGTKQGFDLRLYQQLSSIVSVPVVASGGAGSANDFVTLfRDTNVSA 223
Cdd:COG0106 148 EELAKRFEDAGVAAILYTDISRDGTLQGPNLELYRELAAATGIPVIASGGVSSLDDLRAL-KELGVEG 214
|
|
| PRK13585 |
PRK13585 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ... |
6-223 |
7.23e-29 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase;
Pssm-ID: 184165 Cd Length: 241 Bit Score: 109.23 E-value: 7.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 6 IIPCLDVDQGRVkkgVHFIQ------LKDVGDPVAIAKAYEAQGADELVFLDITATTDARQTMTQTVAAVATQVFMPLTV 79
Cdd:PRK13585 5 VIPAVDMKGGKC---VQLVQgepgteTVSYGDPVEVAKRWVDAGAETLHLVDLDGAFEGERKNAEAIEKIIEAVGVPVQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 80 GGGIRSVTDMHQLLRAGADKIALNSAAVKHPDLITAGAEKFGRQAIVVAIDARwqpsrnRYQVMINGGRTPVDLGVLTWA 159
Cdd:PRK13585 82 GGGIRSAEDAASLLDLGVDRVILGTAAVENPEIVRELSEEFGSERVMVSLDAK------DGEVVIKGWTEKTGYTPVEAA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491954436 160 QQAVAAGAGELLITSMDADGTKQGFDLRLYQQLSSIVSVPVVASGGAGSANDFVTLfRDTNVSA 223
Cdd:PRK13585 156 KRFEELGAGSILFTNVDVEGLLEGVNTEPVKELVDSVDIPVIASGGVTTLDDLRAL-KEAGAAG 218
|
|
| PRK00748 |
PRK00748 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
6-215 |
1.86e-28 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated
Pssm-ID: 179108 Cd Length: 233 Bit Score: 107.84 E-value: 1.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 6 IIPCLDVDQGRV---KKGVhFIQLKDVG-DPVAIAKAYEAQGADELVFLDITATTDARQTMTQTVAAVATQVFMPLTVGG 81
Cdd:PRK00748 3 IIPAIDLKDGKCvrlYQGD-YDQATVYSdDPVAQAKAWEDQGAKWLHLVDLDGAKAGKPVNLELIEAIVKAVDIPVQVGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 82 GIRSVTDMHQLLRAGADKIALNSAAVKHPDLITAGAEKFGRQaIVVAIDARwqpsrnRYQVMING-----GRTPVDL--- 153
Cdd:PRK00748 82 GIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFPGK-IVVGLDAR------DGKVATDGwletsGVTAEDLakr 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491954436 154 ----GVLTwaqqavaagageLLITSMDADGTKQGFDLRLYQQLSSIVSVPVVASGGAGSANDFVTL 215
Cdd:PRK00748 155 fedaGVKA------------IIYTDISRDGTLSGPNVEATRELAAAVPIPVIASGGVSSLDDIKAL 208
|
|
| HisA_HisF |
cd04723 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ... |
5-236 |
6.16e-28 |
|
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: 106.59 E-value: 6.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 5 RIIPCLDVDQGRVKKGVH---------FIQLKDVGDPVAIAKAYEAQGADELVFLDITATTDaRQTMTQTVAAVATQVFM 75
Cdd:cd04723 1 RIIPVIDLKDGVVVHGVGgdrdnyrpiTSNLCSTSDPLDVARAYKELGFRGLYIADLDAIMG-RGDNDEAIRELAAAWPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 76 PLTVGGGIRSVTDMHQLLRAGADKIALNSAAVKHpDLITAGAEKFGRQAIVVAIDARwqpsrNRYQVMINGGRTPVDLgv 155
Cdd:cd04723 80 GLWVDGGIRSLENAQEWLKRGASRVIVGTETLPS-DDDEDRLAALGEQRLVLSLDFR-----GGQLLKPTDFIGPEEL-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 156 ltwaQQAVAAGAGELLITSMDADGTKQGFDLRLYQQLSSIVSVPVVASGGAGSANDFVTLFRdTNVSAGLAASIFHFGEL 235
Cdd:cd04723 152 ----LRRLAKWPEELIVLDIDRVGSGQGPDLELLERLAARADIPVIAAGGVRSVEDLELLKK-LGASGALVASALHDGGL 226
|
.
gi 491954436 236 T 236
Cdd:cd04723 227 T 227
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
6-215 |
3.09e-25 |
|
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: 99.20 E-value: 3.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 6 IIPCLDVDQGRVkkgVHFIQ-----LKDVGD-PVAIAKAYEAQGADELVFLDITATTDARQTMTQTVAAVATQVFMPLTV 79
Cdd:TIGR00007 1 IIPAIDIKDGKC---VRLYQgdydkETVYGDdPVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 80 GGGIRSVTDMHQLLRAGADKIALNSAAVKHPDLITAGAEKFGRQAIVVAIDArwqpsRNRYqVMING-----GRTPVDLG 154
Cdd:TIGR00007 78 GGGIRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYGPERIVVSLDA-----RGGE-VAVKGwleksEVSLEELA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491954436 155 vltwaQQAVAAGAGELLITSMDADGTKQGFDLRLYQQLSSIVSVPVVASGGAGSANDFVTL 215
Cdd:TIGR00007 152 -----KRLEELGLEGIIYTDISRDGTLSGPNFELTKELVKAVNVPVIASGGVSSIDDLIAL 207
|
|
| PRK13587 |
PRK13587 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
76-229 |
3.24e-08 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Provisional
Pssm-ID: 172156 Cd Length: 234 Bit Score: 52.53 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 76 PLTVGGGIRSVTDMHQLLRAGADKIALNSAAVKHPDLITAGAEKF-GRqaIVVAIDARwqpsrnRYQVMINGGRTPVDLG 154
Cdd:PRK13587 78 DIEVGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFpGR--IYLSVDAY------GEDIKVNGWEEDTELN 149
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491954436 155 VLTWAQQAVAAGAGELLITSMDADGTKQGFDLRLYQQLSSIVSVPVVASGGAGSANDFVTLfrdtnVSAGLAASI 229
Cdd:PRK13587 150 LFSFVRQLSDIPLGGIIYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGGIRHQQDIQRL-----ASLNVHAAI 219
|
|
| PRK13586 |
PRK13586 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
5-215 |
2.14e-07 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 237439 Cd Length: 232 Bit Score: 50.12 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 5 RIIPCLDVDQG------RVKKGVHFIqlkdVGDPVAIAKAYEAQGADELVFLDITATtDARQTMTQTVAAVATQVFMPLT 78
Cdd:PRK13586 3 KIIPSIDISLGkavkriRGVKGTGLI----LGNPIEIASKLYNEGYTRIHVVDLDAA-EGVGNNEMYIKEISKIGFDWIQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 79 VGGGIRSVTDMHQLLRAGADKIALNSAAVKHPDLITAGAEKFGRQAIVVAIDArwqpSRNRYqVMINGGRTPVdLGVLTW 158
Cdd:PRK13586 78 VGGGIRDIEKAKRLLSLDVNALVFSTIVFTNFNLFHDIVREIGSNRVLVSIDY----DNTKR-VLIRGWKEKS-MEVIDG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491954436 159 AQQAVAAGAGELLITSMDADGTKQGFDLRLYQQLSSIVSVPVVAsGGAGSANDFVTL 215
Cdd:PRK13586 152 IKKVNELELLGIIFTYISNEGTTKGIDYNVKDYARLIRGLKEYA-GGVSSDADLEYL 207
|
|
| PRK14024 |
PRK14024 |
phosphoribosyl isomerase A; Provisional |
6-215 |
7.15e-07 |
|
phosphoribosyl isomerase A; Provisional
Pssm-ID: 237589 Cd Length: 241 Bit Score: 48.80 E-value: 7.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 6 IIPCLDVDQGRvkkGVHFIQLK-----DVGDPVAIAKAYEAQGADELVFLDITA---TTDARQTMTQTVAAVATQVFMpl 77
Cdd:PRK14024 6 LLPAVDVVDGQ---AVRLVQGEagsetSYGSPLDAALAWQRDGAEWIHLVDLDAafgRGSNRELLAEVVGKLDVKVEL-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 78 tvGGGIRSVTDMHQLLRAGADKIALNSAAVKHPDLITAGAEKFGRQaIVVAIDARWQPSRNRYQVmINGGrtpvDLgvlt 157
Cdd:PRK14024 81 --SGGIRDDESLEAALATGCARVNIGTAALENPEWCARVIAEHGDR-VAVGLDVRGHTLAARGWT-RDGG----DL---- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 158 WAQQAVAAGA--GELLITSMDADGTKQGFDLRLYQQLSSIVSVPVVASGGAGSANDFVTL 215
Cdd:PRK14024 149 WEVLERLDSAgcSRYVVTDVTKDGTLTGPNLELLREVCARTDAPVVASGGVSSLDDLRAL 208
|
|
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
28-113 |
1.14e-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: 42.56 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 28 DVGDPVAIAKAYEAQGADelvFLDITATTDARQTMTQT------------VAAVATQVFMPLTVGGGIRSVTDMHQLLRA 95
Cdd:cd02803 226 TLEEAIEIAKALEEAGVD---ALHVSGGSYESPPPIIPppyvpegyflelAEKIKKAVKIPVIAVGGIRDPEVAEEILAE 302
|
90
....*....|....*....
gi 491954436 96 G-ADKIALNSAAVKHPDLI 113
Cdd:cd02803 303 GkADLVALGRALLADPDLP 321
|
|
| PRK14114 |
PRK14114 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
6-241 |
2.55e-04 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 172604 Cd Length: 241 Bit Score: 41.15 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 6 IIPCLDVDQGRVKKGVHFIQLKDV---GDPVAIAKAYEAQGADELVFLDIT---ATTDARQTMTQTVAAVATQVfmplTV 79
Cdd:PRK14114 3 VVPAIDLFRGKVARMVKGKKENTIfyeKDPAELVEKLIEEGFTLIHVVDLSkaiENSVENLPVLEKLSEFAEHI----QI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 80 GGGIRSVTDMHQLLRAGADKIALNSAAVKHPDLItagaeKFGRQ---AIVVAIDARwqpsrnRYQVMINGGRTPVDLGVL 156
Cdd:PRK14114 79 GGGIRSLDYAEKLRKLGYRRQIVSSKVLEDPSFL-----KFLKEidvEPVFSLDTR------GGKVAFKGWLAEEEIDPV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954436 157 TWAQQAVAAGAGELLITSMDADGTKQGFDLRLYQQLSSIVSVPVVASGGAGSANDFVT---LFRDTN--VSAGLAASIFH 231
Cdd:PRK14114 148 SLLKRLKEYGLEEIVHTEIEKDGTLQEHDFSLTRKIAIEAEVKVFAAGGISSENSLKTaqrVHRETNglLKGVIVGRAFL 227
|
250
....*....|
gi 491954436 232 FGELTIPQVK 241
Cdd:PRK14114 228 EGILTVEVMK 237
|
|
| GGGP-family |
TIGR01768 |
geranylgeranylglyceryl phosphate synthase family protein; This model represents a family of ... |
53-100 |
3.47e-03 |
|
geranylgeranylglyceryl phosphate synthase family protein; This model represents a family of sequences including geranylgeranylglyceryl phosphate synthase which catalyzes the first committed step in the synthesis of ether-linked membrane lipids in archaea. The clade of bacterial sequences may have the same function or a closely related function. This model supercedes TIGR00265, which has been retired.
Pssm-ID: 273794 Cd Length: 223 Bit Score: 37.85 E-value: 3.47e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 491954436 53 TATTDARQTMTQTVAAVATQVfmPLTVGGGIRSVTDMHQLLRAGADKI 100
Cdd:TIGR01768 160 GAPEPVPPELVAEVKKVLDKA--RLFVGGGIRSVEKAREMAEAGADTV 205
|
|
| PcrB |
COG1646 |
Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism]; |
63-115 |
4.15e-03 |
|
Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism];
Pssm-ID: 441252 Cd Length: 241 Bit Score: 37.45 E-value: 4.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 491954436 63 TQTVAAVATQVF-MPLTVGGGIRSVTDMHQLLRAGADKIALNSAAVKHPDLITA 115
Cdd:COG1646 184 PEMVKAVKKALEdTPLIYGGGIRSPEKAREMAEAGADTIVVGNAIEEDPDLALE 237
|
|
| |
