|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00748 |
PRK00748 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
4-238 |
3.28e-137 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated
Pssm-ID: 179108 Cd Length: 233 Bit Score: 384.80 E-value: 3.28e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 4 FTLYPAIDMRNGKCVRLVQGDYNKETIYGDSPYDMAELFAKEGAEWIHLVDLDGAKEGKRVNDRHVIEIAQKLNLKVEIG 83
Cdd:PRK00748 1 MIIIPAIDLKDGKCVRLYQGDYDQATVYSDDPVAQAKAWEDQGAKWLHLVDLDGAKAGKPVNLELIEAIVKAVDIPVQVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 84 GGIRSEKDVYEYLSAGVDRVILGSSAVSNPPFVKKMLKQYGEKIAIGLDARNGFVSTEGWLETSTLKATELGKELANEGA 163
Cdd:PRK00748 81 GGIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFPGKIVVGLDARDGKVATDGWLETSGVTAEDLAKRFEDAGV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504293910 164 EVFIFTDIATDGMLSGPNVKSTVELAKETGKSVIASGGVSSVTDLEALARYEAdgVSGAIIGKALYTNQFTLSEA 238
Cdd:PRK00748 161 KAIIYTDISRDGTLSGPNVEATRELAAAVPIPVIASGGVSSLDDIKALKGLGA--VEGVIVGRALYEGKFDLAEA 233
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
5-243 |
4.99e-128 |
|
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: 361.66 E-value: 4.99e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 5 TLYPAIDMRNGKCVRLVQGDYNKETIYGDSPYDMAELFAKEGAEWIHLVDLDGAKEGKRVNDRHVIEIAQKLNLKVEIGG 84
Cdd:COG0106 1 IIIPAIDLKDGKCVRLVQGDYDQETVYSDDPVEVAKRWEDAGAEWLHLVDLDGAFAGKPVNLELIEEIAKATGLPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 85 GIRSEKDVYEYLSAGVDRVILGSSAVSNPPFVKKMLKQYGEKIAIGLDARNGFVSTEGWLETSTLKATELGKELANEGAE 164
Cdd:COG0106 81 GIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFPERIVVGLDARDGKVATDGWQETSGVDLEELAKRFEDAGVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504293910 165 VFIFTDIATDGMLSGPNVKSTVELAKETGKSVIASGGVSSVTDLEALARYeadGVSGAIIGKALYTNQFTLSEALERVK 243
Cdd:COG0106 161 AILYTDISRDGTLQGPNLELYRELAAATGIPVIASGGVSSLDDLRALKEL---GVEGAIVGKALYEGKIDLEEALALAR 236
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
6-240 |
1.61e-121 |
|
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: 345.23 E-value: 1.61e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 6 LYPAIDMRNGKCVRLVQGDYNKETIYGDSPYDMAELFAKEGAEWIHLVDLDGAKEGKRVNDRHVIEIAQKLNLKVEIGGG 85
Cdd:cd04732 2 IIPAIDLKDGKCVRLYQGDYDKKTVYSDDPVEVAKKWEEAGAKWLHVVDLDGAKGGEPVNLELIEEIVKAVGIPVQVGGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 86 IRSEKDVYEYLSAGVDRVILGSSAVSNPPFVKKMLKQYG-EKIAIGLDARNGFVSTEGWLETSTLKATELGKELANEGAE 164
Cdd:cd04732 82 IRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGgERIVVGLDAKDGKVATKGWLETSEVSLEELAKRFEELGVK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504293910 165 VFIFTDIATDGMLSGPNVKSTVELAKETGKSVIASGGVSSVTDLEALARYeadGVSGAIIGKALYTNQFTLSEALE 240
Cdd:cd04732 162 AIIYTDISRDGTLSGPNFELYKELAAATGIPVIASGGVSSLDDIKALKEL---GVAGVIVGKALYEGKITLEEALA 234
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
6-237 |
2.07e-112 |
|
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: 321.84 E-value: 2.07e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 6 LYPAIDMRNGKCVRLVQGDYNKETIYGDSPYDMAELFAKEGAEWIHLVDLDGAKEGKRVNDRHVIEIAQKLNLKVEIGGG 85
Cdd:TIGR00007 1 IIPAIDIKDGKCVRLYQGDYDKETVYGDDPVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQVGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 86 IRSEKDVYEYLSAGVDRVILGSSAVSNPPFVKKMLKQYG-EKIAIGLDARNGFVSTEGWLETSTLKATELGKELANEGAE 164
Cdd:TIGR00007 81 IRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYGpERIVVSLDARGGEVAVKGWLEKSEVSLEELAKRLEELGLE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504293910 165 VFIFTDIATDGMLSGPNVKSTVELAKETGKSVIASGGVSSVTDLEALARyeaDGVSGAIIGKALYTNQFTLSE 237
Cdd:TIGR00007 161 GIIYTDISRDGTLSGPNFELTKELVKAVNVPVIASGGVSSIDDLIALKK---LGVYGVIVGKALYEGKITLEE 230
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
6-234 |
1.07e-102 |
|
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: 297.08 E-value: 1.07e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 6 LYPAIDMRNGKCVRLVQGDYNKETIYGDSPYDMAELFAKEGAEWIHLVDLDGAKEGKRVNDRHVIEIAQKLNLKVEIGGG 85
Cdd:pfam00977 2 IIPAIDLKDGRVVRLVKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 86 IRSEKDVYEYLSAGVDRVILGSSAVSNPPFVKKMLKQYG-EKIAIGLDARNGFVSTEGWLETSTLKATELGKELANEGAE 164
Cdd:pfam00977 82 IRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGsQCIVVAIDARRGKVAINGWREDTGIDAVEWAKELEELGAG 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 165 VFIFTDIATDGMLSGPNVKSTVELAKETGKSVIASGGVSSVTDLEALARYeadGVSGAIIGKALYTNQFT 234
Cdd:pfam00977 162 EILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELFTE---GVDGVIAGSALYEGEIT 228
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00748 |
PRK00748 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
4-238 |
3.28e-137 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated
Pssm-ID: 179108 Cd Length: 233 Bit Score: 384.80 E-value: 3.28e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 4 FTLYPAIDMRNGKCVRLVQGDYNKETIYGDSPYDMAELFAKEGAEWIHLVDLDGAKEGKRVNDRHVIEIAQKLNLKVEIG 83
Cdd:PRK00748 1 MIIIPAIDLKDGKCVRLYQGDYDQATVYSDDPVAQAKAWEDQGAKWLHLVDLDGAKAGKPVNLELIEAIVKAVDIPVQVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 84 GGIRSEKDVYEYLSAGVDRVILGSSAVSNPPFVKKMLKQYGEKIAIGLDARNGFVSTEGWLETSTLKATELGKELANEGA 163
Cdd:PRK00748 81 GGIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFPGKIVVGLDARDGKVATDGWLETSGVTAEDLAKRFEDAGV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504293910 164 EVFIFTDIATDGMLSGPNVKSTVELAKETGKSVIASGGVSSVTDLEALARYEAdgVSGAIIGKALYTNQFTLSEA 238
Cdd:PRK00748 161 KAIIYTDISRDGTLSGPNVEATRELAAAVPIPVIASGGVSSLDDIKALKGLGA--VEGVIVGRALYEGKFDLAEA 233
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
5-243 |
4.99e-128 |
|
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: 361.66 E-value: 4.99e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 5 TLYPAIDMRNGKCVRLVQGDYNKETIYGDSPYDMAELFAKEGAEWIHLVDLDGAKEGKRVNDRHVIEIAQKLNLKVEIGG 84
Cdd:COG0106 1 IIIPAIDLKDGKCVRLVQGDYDQETVYSDDPVEVAKRWEDAGAEWLHLVDLDGAFAGKPVNLELIEEIAKATGLPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 85 GIRSEKDVYEYLSAGVDRVILGSSAVSNPPFVKKMLKQYGEKIAIGLDARNGFVSTEGWLETSTLKATELGKELANEGAE 164
Cdd:COG0106 81 GIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFPERIVVGLDARDGKVATDGWQETSGVDLEELAKRFEDAGVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504293910 165 VFIFTDIATDGMLSGPNVKSTVELAKETGKSVIASGGVSSVTDLEALARYeadGVSGAIIGKALYTNQFTLSEALERVK 243
Cdd:COG0106 161 AILYTDISRDGTLQGPNLELYRELAAATGIPVIASGGVSSLDDLRALKEL---GVEGAIVGKALYEGKIDLEEALALAR 236
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
6-240 |
1.61e-121 |
|
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: 345.23 E-value: 1.61e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 6 LYPAIDMRNGKCVRLVQGDYNKETIYGDSPYDMAELFAKEGAEWIHLVDLDGAKEGKRVNDRHVIEIAQKLNLKVEIGGG 85
Cdd:cd04732 2 IIPAIDLKDGKCVRLYQGDYDKKTVYSDDPVEVAKKWEEAGAKWLHVVDLDGAKGGEPVNLELIEEIVKAVGIPVQVGGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 86 IRSEKDVYEYLSAGVDRVILGSSAVSNPPFVKKMLKQYG-EKIAIGLDARNGFVSTEGWLETSTLKATELGKELANEGAE 164
Cdd:cd04732 82 IRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGgERIVVGLDAKDGKVATKGWLETSEVSLEELAKRFEELGVK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504293910 165 VFIFTDIATDGMLSGPNVKSTVELAKETGKSVIASGGVSSVTDLEALARYeadGVSGAIIGKALYTNQFTLSEALE 240
Cdd:cd04732 162 AIIYTDISRDGTLSGPNFELYKELAAATGIPVIASGGVSSLDDIKALKEL---GVAGVIVGKALYEGKITLEEALA 234
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
6-237 |
2.07e-112 |
|
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: 321.84 E-value: 2.07e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 6 LYPAIDMRNGKCVRLVQGDYNKETIYGDSPYDMAELFAKEGAEWIHLVDLDGAKEGKRVNDRHVIEIAQKLNLKVEIGGG 85
Cdd:TIGR00007 1 IIPAIDIKDGKCVRLYQGDYDKETVYGDDPVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQVGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 86 IRSEKDVYEYLSAGVDRVILGSSAVSNPPFVKKMLKQYG-EKIAIGLDARNGFVSTEGWLETSTLKATELGKELANEGAE 164
Cdd:TIGR00007 81 IRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYGpERIVVSLDARGGEVAVKGWLEKSEVSLEELAKRLEELGLE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504293910 165 VFIFTDIATDGMLSGPNVKSTVELAKETGKSVIASGGVSSVTDLEALARyeaDGVSGAIIGKALYTNQFTLSE 237
Cdd:TIGR00007 161 GIIYTDISRDGTLSGPNFELTKELVKAVNVPVIASGGVSSIDDLIALKK---LGVYGVIVGKALYEGKITLEE 230
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
6-234 |
1.07e-102 |
|
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: 297.08 E-value: 1.07e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 6 LYPAIDMRNGKCVRLVQGDYNKETIYGDSPYDMAELFAKEGAEWIHLVDLDGAKEGKRVNDRHVIEIAQKLNLKVEIGGG 85
Cdd:pfam00977 2 IIPAIDLKDGRVVRLVKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 86 IRSEKDVYEYLSAGVDRVILGSSAVSNPPFVKKMLKQYG-EKIAIGLDARNGFVSTEGWLETSTLKATELGKELANEGAE 164
Cdd:pfam00977 82 IRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGsQCIVVAIDARRGKVAINGWREDTGIDAVEWAKELEELGAG 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 165 VFIFTDIATDGMLSGPNVKSTVELAKETGKSVIASGGVSSVTDLEALARYeadGVSGAIIGKALYTNQFT 234
Cdd:pfam00977 162 EILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELFTE---GVDGVIAGSALYEGEIT 228
|
|
| PRK13585 |
PRK13585 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ... |
4-244 |
1.84e-77 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase;
Pssm-ID: 184165 Cd Length: 241 Bit Score: 233.65 E-value: 1.84e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 4 FTLYPAIDMRNGKCVRLVQGDYNKETIYGDSPYDMAELFAKEGAEWIHLVDLDGAKEGKRVNDRHVIEIAQKLNLKVEIG 83
Cdd:PRK13585 3 FEVIPAVDMKGGKCVQLVQGEPGTETVSYGDPVEVAKRWVDAGAETLHLVDLDGAFEGERKNAEAIEKIIEAVGVPVQLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 84 GGIRSEKDVYEYLSAGVDRVILGSSAVSNPPFVKKMLKQYG-EKIAIGLDARNGFVSTEGWLETSTLKATELGKELANEG 162
Cdd:PRK13585 83 GGIRSAEDAASLLDLGVDRVILGTAAVENPEIVRELSEEFGsERVMVSLDAKDGEVVIKGWTEKTGYTPVEAAKRFEELG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 163 AEVFIFTDIATDGMLSGPNVKSTVELAKETGKSVIASGGVSSVTDLEALaryEADGVSGAIIGKALYTNQFTLSEALERV 242
Cdd:PRK13585 163 AGSILFTNVDVEGLLEGVNTEPVKELVDSVDIPVIASGGVTTLDDLRAL---KEAGAAGVVVGSALYKGKFTLEEAIEAV 239
|
..
gi 504293910 243 KR 244
Cdd:PRK13585 240 KG 241
|
|
| PRK14024 |
PRK14024 |
phosphoribosyl isomerase A; Provisional |
1-244 |
4.98e-72 |
|
phosphoribosyl isomerase A; Provisional
Pssm-ID: 237589 Cd Length: 241 Bit Score: 219.83 E-value: 4.98e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 1 MSAFTLYPAIDMRNGKCVRLVQGDYNKETIYGDsPYDMAELFAKEGAEWIHLVDLDGAKeGKRVNDRHVIEIAQKLNLKV 80
Cdd:PRK14024 1 TMSLTLLPAVDVVDGQAVRLVQGEAGSETSYGS-PLDAALAWQRDGAEWIHLVDLDAAF-GRGSNRELLAEVVGKLDVKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 81 EIGGGIRSEKDVYEYLSAGVDRVILGSSAVSNPPFVKKMLKQYGEKIAIGLDARNGFVSTEGWletsTLKATELGKELAN 160
Cdd:PRK14024 79 ELSGGIRDDESLEAALATGCARVNIGTAALENPEWCARVIAEHGDRVAVGLDVRGHTLAARGW----TRDGGDLWEVLER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 161 ---EGAEVFIFTDIATDGMLSGPNVKSTVELAKETGKSVIASGGVSSVTDLEALARYEADGVSGAIIGKALYTNQFTLSE 237
Cdd:PRK14024 155 ldsAGCSRYVVTDVTKDGTLTGPNLELLREVCARTDAPVVASGGVSSLDDLRALAELVPLGVEGAIVGKALYAGAFTLPE 234
|
....*..
gi 504293910 238 ALERVKR 244
Cdd:PRK14024 235 ALAVVRR 241
|
|
| PRK04128 |
PRK04128 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
4-240 |
3.80e-45 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 167709 Cd Length: 228 Bit Score: 150.69 E-value: 3.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 4 FTLYPAIDMRNGKCVRLVQGDYNKETIYGDsPYDMAELFAkEGAEWIHLVDLDGAKEGKRVNDRHVIEIAQKLNLKVEIG 83
Cdd:PRK04128 2 MRIYPAIDLMNGKAVRLYKGRKEEVKVYGD-PVEIALRFS-EYVDKIHVVDLDGAFEGKPKNLDVVKNIIRETGLKVQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 84 GGIRSEKDVYEYLSAGVDRVILGSSAVsNPPFVKKMLKQYgEKIAIGLDARNGFVSTEGWLETSTLKATELGKELANEgA 163
Cdd:PRK04128 80 GGLRTYESIKDAYEIGVENVIIGTKAF-DLEFLEKVTSEF-EGITVSLDVKGGRIAVKGWLEESSIKVEDAYEMLKNY-V 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504293910 164 EVFIFTDIATDGMLSG-PNVKSTVElaketGKSVIASGGVSSVTDLEALARyeaDGVSGAIIGKALYTNQFTLSEALE 240
Cdd:PRK04128 157 NRFIYTSIERDGTLTGiEEIERFWG-----DEEFIYAGGVSSAEDVKKLAE---IGFSGVIIGKALYEGRISLEELLE 226
|
|
| HisA_HisF |
cd04723 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ... |
6-240 |
8.24e-42 |
|
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: 142.41 E-value: 8.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 6 LYPAIDMRNGKCVRLVQGD---YNKET---IYGDSPYDMAELFAKEGAEWIHLVDLDgAKEGKRVNDRHVIEIAQKLNLK 79
Cdd:cd04723 2 IIPVIDLKDGVVVHGVGGDrdnYRPITsnlCSTSDPLDVARAYKELGFRGLYIADLD-AIMGRGDNDEAIRELAAAWPLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 80 VEIGGGIRSEKDVYEYLSAGVDRVILGSSAVSNPpFVKKMLKQYGE-KIAIGLDARNGFVSTEGWLETstlkATELGKEL 158
Cdd:cd04723 81 LWVDGGIRSLENAQEWLKRGASRVIVGTETLPSD-DDEDRLAALGEqRLVLSLDFRGGQLLKPTDFIG----PEELLRRL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 159 ANEGAEvFIFTDIATDGMLSGPNVKSTVELAKETGKSVIASGGVSSVTDLEALARYeadGVSGAIIGKALYTNQFTLSEA 238
Cdd:cd04723 156 AKWPEE-LIVLDIDRVGSGQGPDLELLERLAARADIPVIAAGGVRSVEDLELLKKL---GASGALVASALHDGGLTLEDV 231
|
..
gi 504293910 239 LE 240
Cdd:cd04723 232 VR 233
|
|
| PRK13587 |
PRK13587 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
6-233 |
1.48e-39 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Provisional
Pssm-ID: 172156 Cd Length: 234 Bit Score: 136.50 E-value: 1.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 6 LYPAIDMRNGKCVRLVQGDYNKETIYGDSPYDMAELFAK-EGAEWIHLVDLDGAKEgKRVNDRHVIEIAQKLNLK-VEIG 83
Cdd:PRK13587 4 LWPAIDLIGSTSVRLTEGKYDSEEKMSRSAEESIAYYSQfECVNRIHIVDLIGAKA-QHAREFDYIKSLRRLTTKdIEVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 84 GGIRSEKDVYEYLSAGVDRVILGSSAVSNPPFVKKMLKQYGEKIAIGLDARNGFVSTEGWLETSTLKATELGKELANEGA 163
Cdd:PRK13587 83 GGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGRIYLSVDAYGEDIKVNGWEEDTELNLFSFVRQLSDIPL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 164 EVFIFTDIATDGMLSGPNVKSTVELAKETGKSVIASGGVSSVTDLEalaRYEADGVSGAIIGKALYTNQF 233
Cdd:PRK13587 163 GGIIYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGGIRHQQDIQ---RLASLNVHAAIIGKAAHQASF 229
|
|
| PRK14114 |
PRK14114 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
8-244 |
4.05e-34 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 172604 Cd Length: 241 Bit Score: 122.81 E-value: 4.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 8 PAIDMRNGKCVRLVQGDYNKETIYGDSPYDMAELFAKEGAEWIHLVDLDGAKEgKRVNDRHVIEIAQKLNLKVEIGGGIR 87
Cdd:PRK14114 5 PAIDLFRGKVARMVKGKKENTIFYEKDPAELVEKLIEEGFTLIHVVDLSKAIE-NSVENLPVLEKLSEFAEHIQIGGGIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 88 SEKDVYEYLSAGVDRVILGSSAVSNPPFVKKmLKQYGEKIAIGLDARNGFVSTEGWLETSTLKATELGKELANEGAEVFI 167
Cdd:PRK14114 84 SLDYAEKLRKLGYRRQIVSSKVLEDPSFLKF-LKEIDVEPVFSLDTRGGKVAFKGWLAEEEIDPVSLLKRLKEYGLEEIV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 168 FTDIATDGMLSGPNVKSTVELAKETGKSVIASGGVSSVTDLEALARY--EADG-VSGAIIGKALYTNQFTLsEALERVKR 244
Cdd:PRK14114 163 HTEIEKDGTLQEHDFSLTRKIAIEAEVKVFAAGGISSENSLKTAQRVhrETNGlLKGVIVGRAFLEGILTV-EVMKRYAR 241
|
|
| HisF |
cd04731 |
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ... |
8-222 |
2.84e-28 |
|
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: 107.55 E-value: 2.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 8 PAIDMRNGkcvRLVQGDYNKETIYGDSPYDMAELFAKEGAEWIHLVDLDGAKEGKRVNDRHVIEIAQKLNLKVEIGGGIR 87
Cdd:cd04731 5 PCLDVKDG---RVVKGVNFKNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRETMLDVVERVAEEVFIPLTVGGGIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 88 SEKDVYEYLSAGVDRVILGSSAVSNPPFVKKMLKQYG-EKIAIGLDA-RNGF----VSTEGWLETSTLKATELGKELANE 161
Cdd:cd04731 82 SLEDARRLLRAGADKVSINSAAVENPELIREIAKRFGsQCVVVSIDAkRRGDggyeVYTHGGRKPTGLDAVEWAKEVEEL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504293910 162 GAEVFIFTDIATDGMLSGPNVKSTVELAKETGKSVIASGGVSSVTDL-EALARYEADGVSGA 222
Cdd:cd04731 162 GAGEILLTSMDRDGTKKGYDLELIRAVSSAVNIPVIASGGAGKPEHFvEAFEEGGADAALAA 223
|
|
| hisF |
TIGR00735 |
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ... |
1-237 |
4.53e-25 |
|
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273241 Cd Length: 254 Bit Score: 99.36 E-value: 4.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 1 MSAFTLYPAIDMRNGKCVRLVQgdYNKETIYGDsPYDMAELFAKEGAEWIHLVDLDGAKEGkRVNDRHVIE-IAQKLNLK 79
Cdd:TIGR00735 1 MLAKRIIPCLDVRDGRVVKGVQ--FLNLRDAGD-PVELAQRYDEEGADELVFLDITASSEG-RTTMIDVVErTAETVFIP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 80 VEIGGGIRSEKDVYEYLSAGVDRVILGSSAVSNPPFVKKMLKQYGEK-IAIGLDARNGFVSTEGWLETST--------LK 150
Cdd:TIGR00735 77 LTVGGGIKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFGSQcIVVAIDAKRVYVNSYCWYEVYIyggrestgLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 151 ATELGKELANEGAEVFIFTDIATDGMLSGPNVKSTVELAKETGKSVIASGGVSSVTD-LEALARYEADGVSGAIIgkaLY 229
Cdd:TIGR00735 157 AVEWAKEVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEAVKIPVIASGGAGKPEHfYEAFTKGKADAALAASV---FH 233
|
....*...
gi 504293910 230 TNQFTLSE 237
Cdd:TIGR00735 234 YREITIGE 241
|
|
| HisF |
COG0107 |
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ... |
8-222 |
1.64e-23 |
|
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: 95.09 E-value: 1.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 8 PAIDMRNGkcvRLVQGDYNKETIY-GDsPYDMAELFAKEGAEWIHLVDLDGAKEGkRVNDRHVIE-IAQKLNLKVEIGGG 85
Cdd:COG0107 7 PCLDVKDG---RVVKGVNFVNLRDaGD-PVELAKRYNEQGADELVFLDITASSEG-RKTMLDVVRrVAEEVFIPLTVGGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 86 IRSEKDVYEYLSAGVDRVILGSSAVSNPPFVKKMLKQYG-EKIAIGLDARngFVSTEGWL-------ETSTLKATELGKE 157
Cdd:COG0107 82 IRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGsQCIVVAIDAK--RVPDGGWEvythggrKPTGLDAVEWAKE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504293910 158 LANEGAEVFIFTDIATDGMLSGPNVKSTVELAKETGKSVIASGGVSSVTDL-EALARYEADGVSGA 222
Cdd:COG0107 160 AEELGAGEILLTSMDRDGTKDGYDLELTRAVSEAVSIPVIASGGAGTLEHFvEVFTEGGADAALAA 225
|
|
| PRK13586 |
PRK13586 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
8-231 |
2.40e-22 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 237439 Cd Length: 232 Bit Score: 91.73 E-value: 2.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 8 PAIDMRNGKCVRLVQGDYNKETIYGDsPYDMAELFAKEGAEWIHLVDLDGAkEGKRVNDRHVIEIAqKLNLK-VEIGGGI 86
Cdd:PRK13586 6 PSIDISLGKAVKRIRGVKGTGLILGN-PIEIASKLYNEGYTRIHVVDLDAA-EGVGNNEMYIKEIS-KIGFDwIQVGGGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 87 RSEKDVYEYLSAGVDRVILGSSAVSNPPFVKKMLKQYG-EKIAIGLD-ARNGFVSTEGWLETSTlKATELGKELANEGAE 164
Cdd:PRK13586 83 RDIEKAKRLLSLDVNALVFSTIVFTNFNLFHDIVREIGsNRVLVSIDyDNTKRVLIRGWKEKSM-EVIDGIKKVNELELL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504293910 165 VFIFTDIATDGMLSG--PNVKSTVELAKETGKSviaSGGVSSVTDLEALARYeadGVSGAIIGKALYTN 231
Cdd:PRK13586 162 GIIFTYISNEGTTKGidYNVKDYARLIRGLKEY---AGGVSSDADLEYLKNV---GFDYIIVGMAFYLG 224
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
32-219 |
1.80e-03 |
|
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: 38.34 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 32 GDSPYDMAELFAKEGAEWIHLVDLDGAKEGKRVNDRHVI-EIAQKLNLKVEIGGGIRSEKDVYEYL-----SAGVDRVIL 105
Cdd:cd04722 11 SGDPVELAKAAAEAGADAIIVGTRSSDPEEAETDDKEVLkEVAAETDLPLGVQLAINDAAAAVDIAaaaarAAGADGVEI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504293910 106 GSSAVSNPPFVKKMLKQygekiaigldARNGFVSTEGWLETSTLkaTELGKELANEGAEVFIFTDIATDGMLSGPNVKST 185
Cdd:cd04722 91 HGAVGYLAREDLELIRE----------LREAVPDVKVVVKLSPT--GELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPIA 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 504293910 186 VELAK----ETGKSVIASGGVSSVTDLEALARYEADGV 219
Cdd:cd04722 159 DLLLIlakrGSKVPVIAGGGINDPEDAAEALALGADGV 196
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
182-234 |
7.49e-03 |
|
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) [Signal transduction mechanisms];
Pssm-ID: 441802 [Multi-domain] Cd Length: 576 Bit Score: 37.46 E-value: 7.49e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 504293910 182 VKSTVELAKETGKSVIAsGGVSSVTDLEALARYEADGVSGAIIGKALYTNQFT 234
Cdd:COG2200 521 VRAIVALAHRLGLKVVA-EGVETEEQLEALRELGCDYAQGYLFGRPLPLEELE 572
|
|
| |
