|
Name |
Accession |
Description |
Interval |
E-value |
| AglZ_HisF2_fam |
NF038364 |
AglZ/HisF2 family acetamidino modification protein; |
2-233 |
3.11e-153 |
|
AglZ/HisF2 family acetamidino modification protein;
Pssm-ID: 439657 Cd Length: 248 Bit Score: 425.73 E-value: 3.11e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 2 KTVKFKDPKYVGDPINAVKIFNEKEADELIVIDIDATANGVEPNYIQIAKLAAECRMPLCYGGGIRTAEQAKKIIQLGVE 81
Cdd:NF038364 18 KTVKFKDPKYVGDPINAVRIFNEKEVDELIVLDIDATKEGREPDYELIEDLASECFMPLCYGGGIKTLEQARRIFSLGVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 82 KVAISSAALENPQLVTQIAEEIGSQSVVVVLDHKSRLLSKHqEVWTHNGTRNTKRNVVEVAQELEKLGAGEIVLNSIEND 161
Cdd:NF038364 98 KVALNSAALENPELITEAAEEFGSQSVVVSIDVKKNLFGGY-EVYTHNGTKKTKLDPVEFAKELEALGAGEIVLNSIDRD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 430792111 162 GKMKGYDLDLASKLRAAVHIPITILGGGGSLEDMASVVKTCGVVGVAAGSFFVFKGAYRAVLISYPSAQQKD 233
Cdd:NF038364 177 GTMKGYDLELIKKVSSAVSIPVIALGGAGSLEDLKEAIKQAGASAVAAGSLFVFKGKHRAVLINYPTPEELE 248
|
|
| HisF |
cd04731 |
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ... |
2-230 |
4.58e-107 |
|
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: 308.63 E-value: 4.58e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 2 KTVKFKDPKYVGDPINAVKIFNEKEADELIVIDIDATANGVEPNYIQIAKLAAECRMPLCYGGGIRTAEQAKKIIQLGVE 81
Cdd:cd04731 16 KGVNFKNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRETMLDVVERVAEEVFIPLTVGGGIRSLEDARRLLRAGAD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 82 KVAISSAALENPQLVTQIAEEIGSQSVVVVLDHKsRLLSKHQEVWTHNGTRNTKRNVVEVAQELEKLGAGEIVLNSIEND 161
Cdd:cd04731 96 KVSINSAAVENPELIREIAKRFGSQCVVVSIDAK-RRGDGGYEVYTHGGRKPTGLDAVEWAKEVEELGAGEILLTSMDRD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 430792111 162 GKMKGYDLDLASKLRAAVHIPITILGGGGSLEDMASVVKTCGVVGVAAGSFFVFKGAYRAVLISYPSAQ 230
Cdd:cd04731 175 GTKKGYDLELIRAVSSAVNIPVIASGGAGKPEHFVEAFEEGGADAALAASIFHFGEYTIAELKEYLAER 243
|
|
| WbuZ |
TIGR03572 |
glycosyl amidation-associated protein WbuZ; This clade of sequences is highly similar to the ... |
2-215 |
4.43e-106 |
|
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: 306.12 E-value: 4.43e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 2 KTVKFKDPKYVGDPINAVKIFNEKEADELIVIDIDATANGVEPNYIQIAKLAAECRMPLCYGGGIRTAEQAKKIIQLGVE 81
Cdd:TIGR03572 19 KTVQFKDPRYIGDPVNAARIYNAKGADELIVLDIDASKRGREPLFELISNLAEECFMPLTVGGGIRSLEDAKKLLSLGAD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 82 KVAISSAALENPQLVTQIAEEIGSQSVVVVLDHKSRLLSKHQEVWTHNGTRNTKRNVVEVAQELEKLGAGEIVLNSIEND 161
Cdd:TIGR03572 99 KVSINTAALENPDLIEEAARRFGSQCVVVSIDVKKELDGSDYKVYSDNGRRATGRDPVEWAREAEQLGAGEILLNSIDRD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 430792111 162 GKMKGYDLDLASKLRAAVHIPITILGGGGSLEDMASVVKTCGVVGVAAGSFFVF 215
Cdd:TIGR03572 179 GTMKGYDLELIKTVSDAVSIPVIALGGAGSLDDLVEVALEAGASAVAAASLFHF 232
|
|
| HisF |
COG0107 |
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ... |
2-231 |
6.79e-99 |
|
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: 288.46 E-value: 6.79e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 2 KTVKFKDPKYVGDPINAVKIFNEKEADELIVIDIDATANGVEPNYIQIAKLAAECRMPLCYGGGIRTAEQAKKIIQLGVE 81
Cdd:COG0107 18 KGVNFVNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRKTMLDVVRRVAEEVFIPLTVGGGIRSVEDARRLLRAGAD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 82 KVAISSAALENPQLVTQIAEEIGSQSVVVVLDHKSRLLSKHqEVWTHNGTRNTKRNVVEVAQELEKLGAGEIVLNSIEND 161
Cdd:COG0107 98 KVSINSAAVKNPELITEAAERFGSQCIVVAIDAKRVPDGGW-EVYTHGGRKPTGLDAVEWAKEAEELGAGEILLTSMDRD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 162 GKMKGYDLDLASKLRAAVHIPITILGGGGSLEDMASVVKTCGVVGVAAGSFFVFKGAYRAVLISYPSAQQ 231
Cdd:COG0107 177 GTKDGYDLELTRAVSEAVSIPVIASGGAGTLEHFVEVFTEGGADAALAASIFHFGEITIAELKAYLAEAG 246
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
2-213 |
3.15e-65 |
|
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: 201.94 E-value: 3.15e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 2 KTVKFKDPKYVGDPINAVKIFNEKEADELIVIDIDATANGVEPNYIQIAKLAAECRMPLCYGGGIRTAEQAKKIIQLGVE 81
Cdd:pfam00977 18 KGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGGGIRSLEDVERLLSAGAD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 82 KVAISSAALENPQLVTQIAEEIGSQSVVVVLDhksrllSKHQEVWTHNGTRNTKRNVVEVAQELEKLGAGEIVLNSIEND 161
Cdd:pfam00977 98 RVIIGTAAVKNPELIKEAAEKFGSQCIVVAID------ARRGKVAINGWREDTGIDAVEWAKELEELGAGEILLTDIDRD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 430792111 162 GKMKGYDLDLASKLRAAVHIPITILGGGGSLEDMASVVKTcGVVGVAAGSFF 213
Cdd:pfam00977 172 GTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELFTE-GVDGVIAGSAL 222
|
|
| PRK13585 |
PRK13585 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ... |
13-211 |
4.56e-36 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase;
Pssm-ID: 184165 Cd Length: 241 Bit Score: 127.72 E-value: 4.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 13 GDPINAVKIFNEKEADELIVIDIDATANGVEPNYIQIAKLAAECRMPLCYGGGIRTAEQAKKIIQLGVEKVAISSAALEN 92
Cdd:PRK13585 32 GDPVEVAKRWVDAGAETLHLVDLDGAFEGERKNAEAIEKIIEAVGVPVQLGGGIRSAEDAASLLDLGVDRVILGTAAVEN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 93 PQLVTQIAEEIGSQSVVVVLDhksrllSKHQEVWTHNGTRNTKRNVVEVAQELEKLGAGEIVLNSIENDGKMKGYDLDLA 172
Cdd:PRK13585 112 PEIVRELSEEFGSERVMVSLD------AKDGEVVIKGWTEKTGYTPVEAAKRFEELGAGSILFTNVDVEGLLEGVNTEPV 185
|
170 180 190
....*....|....*....|....*....|....*....
gi 430792111 173 SKLRAAVHIPITILGGGGSLEDMAsVVKTCGVVGVAAGS 211
Cdd:PRK13585 186 KELVDSVDIPVIASGGVTTLDDLR-ALKEAGAAGVVVGS 223
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AglZ_HisF2_fam |
NF038364 |
AglZ/HisF2 family acetamidino modification protein; |
2-233 |
3.11e-153 |
|
AglZ/HisF2 family acetamidino modification protein;
Pssm-ID: 439657 Cd Length: 248 Bit Score: 425.73 E-value: 3.11e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 2 KTVKFKDPKYVGDPINAVKIFNEKEADELIVIDIDATANGVEPNYIQIAKLAAECRMPLCYGGGIRTAEQAKKIIQLGVE 81
Cdd:NF038364 18 KTVKFKDPKYVGDPINAVRIFNEKEVDELIVLDIDATKEGREPDYELIEDLASECFMPLCYGGGIKTLEQARRIFSLGVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 82 KVAISSAALENPQLVTQIAEEIGSQSVVVVLDHKSRLLSKHqEVWTHNGTRNTKRNVVEVAQELEKLGAGEIVLNSIEND 161
Cdd:NF038364 98 KVALNSAALENPELITEAAEEFGSQSVVVSIDVKKNLFGGY-EVYTHNGTKKTKLDPVEFAKELEALGAGEIVLNSIDRD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 430792111 162 GKMKGYDLDLASKLRAAVHIPITILGGGGSLEDMASVVKTCGVVGVAAGSFFVFKGAYRAVLISYPSAQQKD 233
Cdd:NF038364 177 GTMKGYDLELIKKVSSAVSIPVIALGGAGSLEDLKEAIKQAGASAVAAGSLFVFKGKHRAVLINYPTPEELE 248
|
|
| HisF |
cd04731 |
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ... |
2-230 |
4.58e-107 |
|
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: 308.63 E-value: 4.58e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 2 KTVKFKDPKYVGDPINAVKIFNEKEADELIVIDIDATANGVEPNYIQIAKLAAECRMPLCYGGGIRTAEQAKKIIQLGVE 81
Cdd:cd04731 16 KGVNFKNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRETMLDVVERVAEEVFIPLTVGGGIRSLEDARRLLRAGAD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 82 KVAISSAALENPQLVTQIAEEIGSQSVVVVLDHKsRLLSKHQEVWTHNGTRNTKRNVVEVAQELEKLGAGEIVLNSIEND 161
Cdd:cd04731 96 KVSINSAAVENPELIREIAKRFGSQCVVVSIDAK-RRGDGGYEVYTHGGRKPTGLDAVEWAKEVEELGAGEILLTSMDRD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 430792111 162 GKMKGYDLDLASKLRAAVHIPITILGGGGSLEDMASVVKTCGVVGVAAGSFFVFKGAYRAVLISYPSAQ 230
Cdd:cd04731 175 GTKKGYDLELIRAVSSAVNIPVIASGGAGKPEHFVEAFEEGGADAALAASIFHFGEYTIAELKEYLAER 243
|
|
| WbuZ |
TIGR03572 |
glycosyl amidation-associated protein WbuZ; This clade of sequences is highly similar to the ... |
2-215 |
4.43e-106 |
|
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: 306.12 E-value: 4.43e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 2 KTVKFKDPKYVGDPINAVKIFNEKEADELIVIDIDATANGVEPNYIQIAKLAAECRMPLCYGGGIRTAEQAKKIIQLGVE 81
Cdd:TIGR03572 19 KTVQFKDPRYIGDPVNAARIYNAKGADELIVLDIDASKRGREPLFELISNLAEECFMPLTVGGGIRSLEDAKKLLSLGAD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 82 KVAISSAALENPQLVTQIAEEIGSQSVVVVLDHKSRLLSKHQEVWTHNGTRNTKRNVVEVAQELEKLGAGEIVLNSIEND 161
Cdd:TIGR03572 99 KVSINTAALENPDLIEEAARRFGSQCVVVSIDVKKELDGSDYKVYSDNGRRATGRDPVEWAREAEQLGAGEILLNSIDRD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 430792111 162 GKMKGYDLDLASKLRAAVHIPITILGGGGSLEDMASVVKTCGVVGVAAGSFFVF 215
Cdd:TIGR03572 179 GTMKGYDLELIKTVSDAVSIPVIALGGAGSLDDLVEVALEAGASAVAAASLFHF 232
|
|
| HisF |
COG0107 |
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ... |
2-231 |
6.79e-99 |
|
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: 288.46 E-value: 6.79e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 2 KTVKFKDPKYVGDPINAVKIFNEKEADELIVIDIDATANGVEPNYIQIAKLAAECRMPLCYGGGIRTAEQAKKIIQLGVE 81
Cdd:COG0107 18 KGVNFVNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRKTMLDVVRRVAEEVFIPLTVGGGIRSVEDARRLLRAGAD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 82 KVAISSAALENPQLVTQIAEEIGSQSVVVVLDHKSRLLSKHqEVWTHNGTRNTKRNVVEVAQELEKLGAGEIVLNSIEND 161
Cdd:COG0107 98 KVSINSAAVKNPELITEAAERFGSQCIVVAIDAKRVPDGGW-EVYTHGGRKPTGLDAVEWAKEAEELGAGEILLTSMDRD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 162 GKMKGYDLDLASKLRAAVHIPITILGGGGSLEDMASVVKTCGVVGVAAGSFFVFKGAYRAVLISYPSAQQ 231
Cdd:COG0107 177 GTKDGYDLELTRAVSEAVSIPVIASGGAGTLEHFVEVFTEGGADAALAASIFHFGEITIAELKAYLAEAG 246
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
2-213 |
3.15e-65 |
|
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: 201.94 E-value: 3.15e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 2 KTVKFKDPKYVGDPINAVKIFNEKEADELIVIDIDATANGVEPNYIQIAKLAAECRMPLCYGGGIRTAEQAKKIIQLGVE 81
Cdd:pfam00977 18 KGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGGGIRSLEDVERLLSAGAD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 82 KVAISSAALENPQLVTQIAEEIGSQSVVVVLDhksrllSKHQEVWTHNGTRNTKRNVVEVAQELEKLGAGEIVLNSIEND 161
Cdd:pfam00977 98 RVIIGTAAVKNPELIKEAAEKFGSQCIVVAID------ARRGKVAINGWREDTGIDAVEWAKELEELGAGEILLTDIDRD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 430792111 162 GKMKGYDLDLASKLRAAVHIPITILGGGGSLEDMASVVKTcGVVGVAAGSFF 213
Cdd:pfam00977 172 GTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELFTE-GVDGVIAGSAL 222
|
|
| hisF |
TIGR00735 |
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ... |
2-216 |
3.43e-50 |
|
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273241 Cd Length: 254 Bit Score: 164.46 E-value: 3.43e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 2 KTVKFKDPKYVGDPINAVKIFNEKEADELIVIDIDATANGVEPNYIQIAKLAAECRMPLCYGGGIRTAEQAKKIIQLGVE 81
Cdd:TIGR00735 19 KGVQFLNLRDAGDPVELAQRYDEEGADELVFLDITASSEGRTTMIDVVERTAETVFIPLTVGGGIKSIEDVDKLLRAGAD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 82 KVAISSAALENPQLVTQIAEEIGSQSVVVVLDHKSRLLSKHQ--EVWTHNGTRNTKRNVVEVAQELEKLGAGEIVLNSIE 159
Cdd:TIGR00735 99 KVSINTAAVKNPELIYELADRFGSQCIVVAIDAKRVYVNSYCwyEVYIYGGRESTGLDAVEWAKEVEKLGAGEILLTSMD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 430792111 160 NDGKMKGYDLDLASKLRAAVHIPITILGGGGSLEDMASVVKTCGVVGVAAGSFFVFK 216
Cdd:TIGR00735 179 KDGTKSGYDLELTKAVSEAVKIPVIASGGAGKPEHFYEAFTKGKADAALAASVFHYR 235
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
11-207 |
7.02e-38 |
|
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: 132.22 E-value: 7.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 11 YVGDPINAVKIFNEKEADELIVIDIDATANGVEPNYIQIAKLAAECRMPLCYGGGIRTAEQAKKIIQLGVEKVAISSAAL 90
Cdd:cd04732 27 YSDDPVEVAKKWEEAGAKWLHVVDLDGAKGGEPVNLELIEEIVKAVGIPVQVGGGIRSLEDIERLLDLGVSRVIIGTAAV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 91 ENPQLVTQIAEEIGSQSVVVVLDHKSRllskhqEVWTHNGTRNTKRNVVEVAQELEKLGAGEIVLNSIENDGKMKGYDLD 170
Cdd:cd04732 107 KNPELVKELLKEYGGERIVVGLDAKDG------KVATKGWLETSEVSLEELAKRFEELGVKAIIYTDISRDGTLSGPNFE 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 430792111 171 LASKLRAAVHIPITILGGGGSLEDMASVVKTcGVVGV 207
Cdd:cd04732 181 LYKELAAATGIPVIASGGVSSLDDIKALKEL-GVAGV 216
|
|
| PRK13585 |
PRK13585 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ... |
13-211 |
4.56e-36 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase;
Pssm-ID: 184165 Cd Length: 241 Bit Score: 127.72 E-value: 4.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 13 GDPINAVKIFNEKEADELIVIDIDATANGVEPNYIQIAKLAAECRMPLCYGGGIRTAEQAKKIIQLGVEKVAISSAALEN 92
Cdd:PRK13585 32 GDPVEVAKRWVDAGAETLHLVDLDGAFEGERKNAEAIEKIIEAVGVPVQLGGGIRSAEDAASLLDLGVDRVILGTAAVEN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 93 PQLVTQIAEEIGSQSVVVVLDhksrllSKHQEVWTHNGTRNTKRNVVEVAQELEKLGAGEIVLNSIENDGKMKGYDLDLA 172
Cdd:PRK13585 112 PEIVRELSEEFGSERVMVSLD------AKDGEVVIKGWTEKTGYTPVEAAKRFEELGAGSILFTNVDVEGLLEGVNTEPV 185
|
170 180 190
....*....|....*....|....*....|....*....
gi 430792111 173 SKLRAAVHIPITILGGGGSLEDMAsVVKTCGVVGVAAGS 211
Cdd:PRK13585 186 KELVDSVDIPVIASGGVTTLDDLR-ALKEAGAAGVVVGS 223
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
11-211 |
1.89e-34 |
|
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: 123.22 E-value: 1.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 11 YVGDPINAVKIFNEKEADELIVIDIDATANGVEPNYIQIAKLAAECRMPLCYGGGIRTAEQAKKIIQLGVEKVAISSAAL 90
Cdd:COG0106 27 YSDDPVEVAKRWEDAGAEWLHLVDLDGAFAGKPVNLELIEEIAKATGLPVQVGGGIRSLEDIERLLDAGASRVILGTAAV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 91 ENPQLVTQIAEEIGSQsVVVVLDHKSRllskhqEVWTHNGTRNTKRNVVEVAQELEKLGAGEIVLNSIENDGKMKGYDLD 170
Cdd:COG0106 107 KDPELVKEALEEFPER-IVVGLDARDG------KVATDGWQETSGVDLEELAKRFEDAGVAAILYTDISRDGTLQGPNLE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 430792111 171 LASKLRAAVHIPITILGGGGSLEDMASvVKTCGVVGVAAGS 211
Cdd:COG0106 180 LYRELAAATGIPVIASGGVSSLDDLRA-LKELGVEGAIVGK 219
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
11-211 |
2.15e-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: 123.08 E-value: 2.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 11 YVGDPINAVKIFNEKEADELIVIDIDATANGVEPNYIQIAKLAAECRMPLCYGGGIRTAEQAKKIIQLGVEKVAISSAAL 90
Cdd:TIGR00007 26 YGDDPVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQVGGGIRSLEDVEKLLDLGVDRVIIGTAAV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 91 ENPQLVTQIAEEIGSQSVVVVLDhksrllSKHQEVWTHNGTRNTKRNVVEVAQELEKLGAGEIVLNSIENDGKMKGYDLD 170
Cdd:TIGR00007 106 ENPDLVKELLKEYGPERIVVSLD------ARGGEVAVKGWLEKSEVSLEELAKRLEELGLEGIIYTDISRDGTLSGPNFE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 430792111 171 LASKLRAAVHIPITILGGGGSLEDMASVVKTcGVVGVAAGS 211
Cdd:TIGR00007 180 LTKELVKAVNVPVIASGGVSSIDDLIALKKL-GVYGVIVGK 219
|
|
| PRK00748 |
PRK00748 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
11-210 |
1.72e-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: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 11 YVGDPINAVKIFNEKEADELIVIDIDATANGVEPNYIQIAKLAAECRMPLCYGGGIRTAEQAKKIIQLGVEKVAISSAAL 90
Cdd:PRK00748 28 YSDDPVAQAKAWEDQGAKWLHLVDLDGAKAGKPVNLELIEAIVKAVDIPVQVGGGIRSLETVEALLDAGVSRVIIGTAAV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 91 ENPQLVTQIAEEIGSQsVVVVLDhksrllSKHQEVWTHNGTRNTKRNVVEVAQELEKLGAGEIVLNSIENDGKMKGYDLD 170
Cdd:PRK00748 108 KNPELVKEACKKFPGK-IVVGLD------ARDGKVATDGWLETSGVTAEDLAKRFEDAGVKAIIYTDISRDGTLSGPNVE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 430792111 171 LASKLRAAVHIPITILGGGGSLEDMASVVKTCGVVGVAAG 210
Cdd:PRK00748 181 ATRELAAAVPIPVIASGGVSSLDDIKALKGLGAVEGVIVG 220
|
|
| HisA_HisF |
cd04723 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ... |
11-211 |
6.76e-24 |
|
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: 95.80 E-value: 6.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 11 YVGDPINAVKIFNEKEADELIVIDIDAtANGVEPNYIQIAKLAAECRMPLCYGGGIRTAEQAKKIIQLGVEKVAISSAAL 90
Cdd:cd04723 33 STSDPLDVARAYKELGFRGLYIADLDA-IMGRGDNDEAIRELAAAWPLGLWVDGGIRSLENAQEWLKRGASRVIVGTETL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 91 ENpQLVTQIAEEIGSQSVVVVLDHKSRLLSKHQEVWTHngtrntkrnvVEVAQELEKLgAGEIVLNSIENDGKMKGYDLD 170
Cdd:cd04723 112 PS-DDDEDRLAALGEQRLVLSLDFRGGQLLKPTDFIGP----------EELLRRLAKW-PEELIVLDIDRVGSGQGPDLE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 430792111 171 LASKLRAAVHIPITILGGGGSLEDMASVVKTcGVVGVAAGS 211
Cdd:cd04723 180 LLERLAARADIPVIAAGGVRSVEDLELLKKL-GASGALVAS 219
|
|
| PLN02617 |
PLN02617 |
imidazole glycerol phosphate synthase hisHF |
59-212 |
1.45e-16 |
|
imidazole glycerol phosphate synthase hisHF
Pssm-ID: 178226 [Multi-domain] Cd Length: 538 Bit Score: 78.21 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 59 PLCYGGGIR-----------TAEQAKKIIQLGVEKVAISSAALENPQL------------VTQIAEEIGSQSVVVVLD-- 113
Cdd:PLN02617 316 PLTVGGGIRdftdangryysSLEVASEYFRSGADKISIGSDAVYAAEEyiasgvktgktsIEQISRVYGNQAVVVSIDpr 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 114 -----HKSRLLSKH-----------QEVW---THNGTRNTkRNV--VEVAQELEKLGAGEIVLNSIENDGKMKGYDLDLA 172
Cdd:PLN02617 396 rvyvkDPSDVPFKTvkvtnpgpngeEYAWyqcTVKGGREG-RPIgaYELAKAVEELGAGEILLNCIDCDGQGKGFDIELV 474
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 430792111 173 SKLRAAVHIPITILGGGGSLEDMASVV-KTCGVVGVAAGSF 212
Cdd:PLN02617 475 KLVSDAVTIPVIASSGAGTPEHFSDVFsKTNASAALAAGIF 515
|
|
| PRK14024 |
PRK14024 |
phosphoribosyl isomerase A; Provisional |
13-195 |
9.95e-13 |
|
phosphoribosyl isomerase A; Provisional
Pssm-ID: 237589 Cd Length: 241 Bit Score: 65.36 E-value: 9.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 13 GDPINAVKIFNEKEADELIVIDIDAtANGVEPNYIQIAKLAAECRMPLCYGGGIRTAEQAKKIIQLGVEKVAISSAALEN 92
Cdd:PRK14024 32 GSPLDAALAWQRDGAEWIHLVDLDA-AFGRGSNRELLAEVVGKLDVKVELSGGIRDDESLEAALATGCARVNIGTAALEN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 93 PQLVTQIAEEIGSQsVVVVLDHKSRLLSKHQevWTHNGTrntkrNVVEVAQELEKLGAGEIVLNSIENDGKMKGYDLDLA 172
Cdd:PRK14024 111 PEWCARVIAEHGDR-VAVGLDVRGHTLAARG--WTRDGG-----DLWEVLERLDSAGCSRYVVTDVTKDGTLTGPNLELL 182
|
170 180
....*....|....*....|...
gi 430792111 173 SKLRAAVHIPITILGGGGSLEDM 195
Cdd:PRK14024 183 REVCARTDAPVVASGGVSSLDDL 205
|
|
| PRK13586 |
PRK13586 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
12-208 |
8.52e-12 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 237439 Cd Length: 232 Bit Score: 62.84 E-value: 8.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 12 VGDPIN-AVKIFNEKeADELIVIDIDAT-ANGVEPNYI-QIAKLAAECrmpLCYGGGIRTAEQAKKIIQLGVEKVAISSA 88
Cdd:PRK13586 29 LGNPIEiASKLYNEG-YTRIHVVDLDAAeGVGNNEMYIkEISKIGFDW---IQVGGGIRDIEKAKRLLSLDVNALVFSTI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 89 ALENPQLVTQIAEEIGSQSVVVVLDHKS--RLLskhqevwthngTRNTKRNVVEVAQELEK---LGAGEIVLNSIENDGK 163
Cdd:PRK13586 105 VFTNFNLFHDIVREIGSNRVLVSIDYDNtkRVL-----------IRGWKEKSMEVIDGIKKvneLELLGIIFTYISNEGT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 430792111 164 MKGYD---LDLASKLRAAVHIPitilGGGGSLEDMASvVKTCG----VVGVA 208
Cdd:PRK13586 174 TKGIDynvKDYARLIRGLKEYA----GGVSSDADLEY-LKNVGfdyiIVGMA 220
|
|
| PRK14114 |
PRK14114 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
11-214 |
1.06e-11 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 172604 Cd Length: 241 Bit Score: 62.72 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 11 YVGDPINAVKIFNEKEADELIVIDI-DATANGVEpNYIQIAKLAaECRMPLCYGGGIRTAEQAKKIIQLGVEKVAISSAA 89
Cdd:PRK14114 28 YEKDPAELVEKLIEEGFTLIHVVDLsKAIENSVE-NLPVLEKLS-EFAEHIQIGGGIRSLDYAEKLRKLGYRRQIVSSKV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 90 LENPQLVTQIaEEIGSQSVVVVLDHKSRLLSKHqevWTHngtrNTKRNVVEVAQELEKLGAGEIVLNSIENDGKMKGYDL 169
Cdd:PRK14114 106 LEDPSFLKFL-KEIDVEPVFSLDTRGGKVAFKG---WLA----EEEIDPVSLLKRLKEYGLEEIVHTEIEKDGTLQEHDF 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 430792111 170 DLASKLraAVHIPITILGGGG-----SLEDMASV-VKTCGVV-GVAAGSFFV 214
Cdd:PRK14114 178 SLTRKI--AIEAEVKVFAAGGissenSLKTAQRVhRETNGLLkGVIVGRAFL 227
|
|
| PRK13587 |
PRK13587 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
32-209 |
2.30e-09 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Provisional
Pssm-ID: 172156 Cd Length: 234 Bit Score: 55.99 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 32 VIDIDATANGV--EPNYIQiaKLAAECRMPLCYGGGIRTAEQAKKIIQLGVEKVAISSAALENPQLVTQIAEEIGSQSVV 109
Cdd:PRK13587 51 IVDLIGAKAQHarEFDYIK--SLRRLTTKDIEVGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGRIYL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 110 VVLDHKsrllskhQEVWTHNGTRNTKRNVVEVAQELEKLGAGEIVLNSIENDGKMKGYDLDLASKLRAAVHIPITILGGG 189
Cdd:PRK13587 129 SVDAYG-------EDIKVNGWEEDTELNLFSFVRQLSDIPLGGIIYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGGI 201
|
170 180
....*....|....*....|...
gi 430792111 190 GSLEDMASVVKT---CGVVGVAA 209
Cdd:PRK13587 202 RHQQDIQRLASLnvhAAIIGKAA 224
|
|
| OYE_like_4_FMN |
cd04735 |
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ... |
34-101 |
7.21e-07 |
|
Old yellow enzyme (OYE)-related FMN binding domain, group 4. 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. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.
Pssm-ID: 240086 [Multi-domain] Cd Length: 353 Bit Score: 49.13 E-value: 7.21e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 430792111 34 DIDATANGVEPNYIQIAKLAAE---CRMPLCYGGGIRTAEQAKKIIQLGVEKVAISSAALENPQLVTQIAE 101
Cdd:cd04735 258 DFDRKSRRGRDDNQTIMELVKEriaGRLPLIAVGSINTPDDALEALETGADLVAIGRGLLVDPDWVEKIKE 328
|
|
| PRK04128 |
PRK04128 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
10-168 |
1.12e-05 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 167709 Cd Length: 228 Bit Score: 45.15 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 10 KYVGDPINAVKIFNEKeADELIVIDIDATANGVEPNYIQIAKLAAECRMPLCYGGGIRTAEQAKKIIQLGVEKVAISSAA 89
Cdd:PRK04128 27 KVYGDPVEIALRFSEY-VDKIHVVDLDGAFEGKPKNLDVVKNIIRETGLKVQVGGGLRTYESIKDAYEIGVENVIIGTKA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 90 LeNPQLVTQIAEEIGsqSVVVVLD-HKSRLLSKhqevwthnGTRNTKRNVVEVAQELEKLGAGEIVLNSIENDGKMKGYD 168
Cdd:PRK04128 106 F-DLEFLEKVTSEFE--GITVSLDvKGGRIAVK--------GWLEESSIKVEDAYEMLKNYVNRFIYTSIERDGTLTGIE 174
|
|
| HisA_HisF |
cd04723 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ... |
24-88 |
2.36e-05 |
|
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: 44.18 E-value: 2.36e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 430792111 24 EKEADELIVIDIDATANGVEPNYIQIAKLAAECRMPLCYGGGIRTAEQAKKIIQLGVEKVAISSA 88
Cdd:cd04723 156 AKWPEELIVLDIDRVGSGQGPDLELLERLAARADIPVIAAGGVRSVEDLELLKKLGASGALVASA 220
|
|
| PLN02446 |
PLN02446 |
(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
63-223 |
4.44e-05 |
|
(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase
Pssm-ID: 215245 Cd Length: 262 Bit Score: 43.54 E-value: 4.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 63 GGGIrTAEQAKKIIQLGVEKVAISSAALENPQL----VTQIAEEIGSQSVVvvLDHKSRLLSKHQEVWTHngtRNTKRNV 138
Cdd:PLN02446 89 GGGV-NSENAMSYLDAGASHVIVTSYVFRDGQIdlerLKDLVRLVGKQRLV--LDLSCRKKDGRYYVVTD---RWQKFSD 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 139 VEVAQE-LEKLGA--GEIVLNSIENDGKMKGYDLDLASKLRAAVHIPITILGGGGSLEDMASV-VKTCGVVGVAAGSFF- 213
Cdd:PLN02446 163 LAVDEEtLEFLAAycDEFLVHGVDVEGKRLGIDEELVALLGEHSPIPVTYAGGVRSLDDLERVkVAGGGRVDVTVGSALd 242
|
170
....*....|..
gi 430792111 214 VFKG--AYRAVL 223
Cdd:PLN02446 243 IFGGnlPYDDVV 254
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
14-92 |
1.36e-04 |
|
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: 41.80 E-value: 1.36e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 430792111 14 DPINAVKIFNEKEADELIVIDIDATANGVEPNYIQIAKLAAECRMPLCYGGGIRTAEQAKKIIQLGVEKVAISSAALEN 92
Cdd:TIGR00007 146 SLEELAKRLEELGLEGIIYTDISRDGTLSGPNFELTKELVKAVNVPVIASGGVSSIDDLIALKKLGVYGVIVGKALYEG 224
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
44-103 |
1.76e-04 |
|
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. 1VHN, a putative flavin oxidoreductase, has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present.
Pssm-ID: 239200 [Multi-domain] Cd Length: 231 Bit Score: 41.33 E-value: 1.76e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 430792111 44 PNYIQIAKLAAECRMPLCYGGGIRTAEQAKKIIQL-GVEKVAISSAALENPQLVTQIAEEI 103
Cdd:cd02801 170 ADWDYIAEIKEAVSIPVIANGDIFSLEDALRCLEQtGVDGVMIGRGALGNPWLFREIKELL 230
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
14-92 |
1.12e-03 |
|
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: 39.00 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 14 DPINAVKIFNEKEADELIVIDI--DATANGvePNYIQIAKLAAECRMPLCYGGGIRTAEQAKKIIQLGVEKVAISSAALE 91
Cdd:cd04732 147 SLEELAKRFEELGVKAIIYTDIsrDGTLSG--PNFELYKELAAATGIPVIASGGVSSLDDIKALKELGVAGVIVGKALYE 224
|
.
gi 430792111 92 N 92
Cdd:cd04732 225 G 225
|
|
| PcrB |
COG1646 |
Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism]; |
42-101 |
2.16e-03 |
|
Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism];
Pssm-ID: 441252 Cd Length: 241 Bit Score: 38.22 E-value: 2.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 42 VEPNYIQIAKLAAEcRMPLCYGGGIRTAEQAKKIIQLGVEKVAISSAALENPQLVTQIAE 101
Cdd:COG1646 182 VDPEMVKAVKKALE-DTPLIYGGGIRSPEKAREMAEAGADTIVVGNAIEEDPDLALETVE 240
|
|
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
139-210 |
4.39e-03 |
|
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: 37.55 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430792111 139 VEVAQELEKLGAG--EIVLNSIENDGKM-------KGYDLDLASKLRAAVHIPITILGGGGSLEDMASVVKTCGVVGVAA 209
Cdd:cd02803 231 IEIAKALEEAGVDalHVSGGSYESPPPIipppyvpEGYFLELAEKIKKAVKIPVIAVGGIRDPEVAEEILAEGKADLVAL 310
|
.
gi 430792111 210 G 210
Cdd:cd02803 311 G 311
|
|
| |
