|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00748 |
PRK00748 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
1-238 |
1.53e-124 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated
Pssm-ID: 179108 Cd Length: 233 Bit Score: 352.83 E-value: 1.53e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 1 MIIPALDLIDGTVVRLHQGDYGQQRDYGSDPLPRLQSYAAQGAEVLHLVDLTGAKDPAKRQIPLLKSLVAGVDVPVQVGG 80
Cdd:PRK00748 2 IIIPAIDLKDGKCVRLYQGDYDQATVYSDDPVAQAKAWEDQGAKWLHLVDLDGAKAGKPVNLELIEAIVKAVDIPVQVGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 81 GVRTEADVAALLEAGVARVVVGSTAVKSPEEVKGWFKRFgPERLVLALDVRidadgNKQVAVSGWQENSGVTLEELVESY 160
Cdd:PRK00748 82 GIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKF-PGKIVVGLDAR-----DGKVATDGWLETSGVTAEDLAKRF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1170892739 161 LPVGLQHVLCTDISRDGTLAGSNVSLYEEVCARYPqVAFQSSGGIGDLKDIAALRGTG-VRGVIVGRALLEGKFNVTEA 238
Cdd:PRK00748 156 EDAGVKAIIYTDISRDGTLSGPNVEATRELAAAVP-IPVIASGGVSSLDDIKALKGLGaVEGVIVGRALYEGKFDLAEA 233
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
1-243 |
1.54e-112 |
|
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: 322.37 E-value: 1.54e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 1 MIIPALDLIDGTVVRLHQGDYGQQRDYGSDPLPRLQSYAAQGAEVLHLVDLTGAKDPAKRQIPLLKSLVAGVDVPVQVGG 80
Cdd:COG0106 1 IIIPAIDLKDGKCVRLVQGDYDQETVYSDDPVEVAKRWEDAGAEWLHLVDLDGAFAGKPVNLELIEEIAKATGLPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 81 GVRTEADVAALLEAGVARVVVGSTAVKSPEEVKGWFKRFgPERLVLALDVRidadgNKQVAVSGWQENSGVTLEELVESY 160
Cdd:COG0106 81 GIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEF-PERIVVGLDAR-----DGKVATDGWQETSGVDLEELAKRF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 161 LPVGLQHVLCTDISRDGTLAGSNVSLYEEVCARYPqVAFQSSGGIGDLKDIAALRGTGVRGVIVGRALLEGKFNVTEAIQ 240
Cdd:COG0106 155 EDAGVAAILYTDISRDGTLQGPNLELYRELAAATG-IPVIASGGVSSLDDLRALKELGVEGAIVGKALYEGKIDLEEALA 233
|
...
gi 1170892739 241 CWQ 243
Cdd:COG0106 234 LAR 236
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
1-240 |
1.61e-109 |
|
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: 314.80 E-value: 1.61e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 1 MIIPALDLIDGTVVRLHQGDYGQQRDYGSDPLPRLQSYAAQGAEVLHLVDLTGAKDPAKRQIPLLKSLVAGVDVPVQVGG 80
Cdd:cd04732 1 IIIPAIDLKDGKCVRLYQGDYDKKTVYSDDPVEVAKKWEEAGAKWLHVVDLDGAKGGEPVNLELIEEIVKAVGIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 81 GVRTEADVAALLEAGVARVVVGSTAVKSPEEVKGWFKRFGPERLVLALDVRIDadgnkQVAVSGWQENSGVTLEELVESY 160
Cdd:cd04732 81 GIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGGERIVVGLDAKDG-----KVATKGWLETSEVSLEELAKRF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 161 LPVGLQHVLCTDISRDGTLAGSNVSLYEEVCARYpQVAFQSSGGIGDLKDIAALRGTGVRGVIVGRALLEGKFNVTEAIQ 240
Cdd:cd04732 156 EELGVKAIIYTDISRDGTLSGPNFELYKELAAAT-GIPVIASGGVSSLDDIKALKELGVAGVIVGKALYEGKITLEEALA 234
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
2-237 |
2.76e-99 |
|
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: 288.71 E-value: 2.76e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 2 IIPALDLIDGTVVRLHQGDYGQQRDYGSDPLPRLQSYAAQGAEVLHLVDLTGAKDPAKRQIPLLKSLVAGVDVPVQVGGG 81
Cdd:TIGR00007 1 IIPAIDIKDGKCVRLYQGDYDKETVYGDDPVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQVGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 82 VRTEADVAALLEAGVARVVVGSTAVKSPEEVKGWFKRFGPERLVLALDVRIDAdgnkqVAVSGWQENSGVTLEELVESYL 161
Cdd:TIGR00007 81 IRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYGPERIVVSLDARGGE-----VAVKGWLEKSEVSLEELAKRLE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1170892739 162 PVGLQHVLCTDISRDGTLAGSNVSLYEEVCARyPQVAFQSSGGIGDLKDIAALRGTGVRGVIVGRALLEGKFNVTE 237
Cdd:TIGR00007 156 ELGLEGIIYTDISRDGTLSGPNFELTKELVKA-VNVPVIASGGVSSIDDLIALKKLGVYGVIVGKALYEGKITLEE 230
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
1-234 |
5.93e-96 |
|
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: 280.13 E-value: 5.93e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 1 MIIPALDLIDGTVVRLHQGDYGQQRDYGSDPLPRLQSYAAQGAEVLHLVDLTGAKDPAKRQIPLLKSLVAGVDVPVQVGG 80
Cdd:pfam00977 1 RIIPAIDLKDGRVVRLVKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 81 GVRTEADVAALLEAGVARVVVGSTAVKSPEEVKGWFKRFGPERLVLALDVRidadgNKQVAVSGWQENSGVTLEELVESY 160
Cdd:pfam00977 81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAIDAR-----RGKVAINGWREDTGIDAVEWAKEL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1170892739 161 LPVGLQHVLCTDISRDGTLAGSNVSLYEEVCARYpQVAFQSSGGIGDLKDIAALRGTGVRGVIVGRALLEGKFN 234
Cdd:pfam00977 156 EELGAGEILLTDIDRDGTLSGPDLELTRELAEAV-NIPVIASGGVGSLEDLKELFTEGVDGVIAGSALYEGEIT 228
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00748 |
PRK00748 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
1-238 |
1.53e-124 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated
Pssm-ID: 179108 Cd Length: 233 Bit Score: 352.83 E-value: 1.53e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 1 MIIPALDLIDGTVVRLHQGDYGQQRDYGSDPLPRLQSYAAQGAEVLHLVDLTGAKDPAKRQIPLLKSLVAGVDVPVQVGG 80
Cdd:PRK00748 2 IIIPAIDLKDGKCVRLYQGDYDQATVYSDDPVAQAKAWEDQGAKWLHLVDLDGAKAGKPVNLELIEAIVKAVDIPVQVGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 81 GVRTEADVAALLEAGVARVVVGSTAVKSPEEVKGWFKRFgPERLVLALDVRidadgNKQVAVSGWQENSGVTLEELVESY 160
Cdd:PRK00748 82 GIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKF-PGKIVVGLDAR-----DGKVATDGWLETSGVTAEDLAKRF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1170892739 161 LPVGLQHVLCTDISRDGTLAGSNVSLYEEVCARYPqVAFQSSGGIGDLKDIAALRGTG-VRGVIVGRALLEGKFNVTEA 238
Cdd:PRK00748 156 EDAGVKAIIYTDISRDGTLSGPNVEATRELAAAVP-IPVIASGGVSSLDDIKALKGLGaVEGVIVGRALYEGKFDLAEA 233
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
1-243 |
1.54e-112 |
|
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: 322.37 E-value: 1.54e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 1 MIIPALDLIDGTVVRLHQGDYGQQRDYGSDPLPRLQSYAAQGAEVLHLVDLTGAKDPAKRQIPLLKSLVAGVDVPVQVGG 80
Cdd:COG0106 1 IIIPAIDLKDGKCVRLVQGDYDQETVYSDDPVEVAKRWEDAGAEWLHLVDLDGAFAGKPVNLELIEEIAKATGLPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 81 GVRTEADVAALLEAGVARVVVGSTAVKSPEEVKGWFKRFgPERLVLALDVRidadgNKQVAVSGWQENSGVTLEELVESY 160
Cdd:COG0106 81 GIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEF-PERIVVGLDAR-----DGKVATDGWQETSGVDLEELAKRF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 161 LPVGLQHVLCTDISRDGTLAGSNVSLYEEVCARYPqVAFQSSGGIGDLKDIAALRGTGVRGVIVGRALLEGKFNVTEAIQ 240
Cdd:COG0106 155 EDAGVAAILYTDISRDGTLQGPNLELYRELAAATG-IPVIASGGVSSLDDLRALKELGVEGAIVGKALYEGKIDLEEALA 233
|
...
gi 1170892739 241 CWQ 243
Cdd:COG0106 234 LAR 236
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
1-240 |
1.61e-109 |
|
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: 314.80 E-value: 1.61e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 1 MIIPALDLIDGTVVRLHQGDYGQQRDYGSDPLPRLQSYAAQGAEVLHLVDLTGAKDPAKRQIPLLKSLVAGVDVPVQVGG 80
Cdd:cd04732 1 IIIPAIDLKDGKCVRLYQGDYDKKTVYSDDPVEVAKKWEEAGAKWLHVVDLDGAKGGEPVNLELIEEIVKAVGIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 81 GVRTEADVAALLEAGVARVVVGSTAVKSPEEVKGWFKRFGPERLVLALDVRIDadgnkQVAVSGWQENSGVTLEELVESY 160
Cdd:cd04732 81 GIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGGERIVVGLDAKDG-----KVATKGWLETSEVSLEELAKRF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 161 LPVGLQHVLCTDISRDGTLAGSNVSLYEEVCARYpQVAFQSSGGIGDLKDIAALRGTGVRGVIVGRALLEGKFNVTEAIQ 240
Cdd:cd04732 156 EELGVKAIIYTDISRDGTLSGPNFELYKELAAAT-GIPVIASGGVSSLDDIKALKELGVAGVIVGKALYEGKITLEEALA 234
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
2-237 |
2.76e-99 |
|
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: 288.71 E-value: 2.76e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 2 IIPALDLIDGTVVRLHQGDYGQQRDYGSDPLPRLQSYAAQGAEVLHLVDLTGAKDPAKRQIPLLKSLVAGVDVPVQVGGG 81
Cdd:TIGR00007 1 IIPAIDIKDGKCVRLYQGDYDKETVYGDDPVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQVGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 82 VRTEADVAALLEAGVARVVVGSTAVKSPEEVKGWFKRFGPERLVLALDVRIDAdgnkqVAVSGWQENSGVTLEELVESYL 161
Cdd:TIGR00007 81 IRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYGPERIVVSLDARGGE-----VAVKGWLEKSEVSLEELAKRLE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1170892739 162 PVGLQHVLCTDISRDGTLAGSNVSLYEEVCARyPQVAFQSSGGIGDLKDIAALRGTGVRGVIVGRALLEGKFNVTE 237
Cdd:TIGR00007 156 ELGLEGIIYTDISRDGTLSGPNFELTKELVKA-VNVPVIASGGVSSIDDLIALKKLGVYGVIVGKALYEGKITLEE 230
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
1-234 |
5.93e-96 |
|
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: 280.13 E-value: 5.93e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 1 MIIPALDLIDGTVVRLHQGDYGQQRDYGSDPLPRLQSYAAQGAEVLHLVDLTGAKDPAKRQIPLLKSLVAGVDVPVQVGG 80
Cdd:pfam00977 1 RIIPAIDLKDGRVVRLVKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 81 GVRTEADVAALLEAGVARVVVGSTAVKSPEEVKGWFKRFGPERLVLALDVRidadgNKQVAVSGWQENSGVTLEELVESY 160
Cdd:pfam00977 81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAIDAR-----RGKVAINGWREDTGIDAVEWAKEL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1170892739 161 LPVGLQHVLCTDISRDGTLAGSNVSLYEEVCARYpQVAFQSSGGIGDLKDIAALRGTGVRGVIVGRALLEGKFN 234
Cdd:pfam00977 156 EELGAGEILLTDIDRDGTLSGPDLELTRELAEAV-NIPVIASGGVGSLEDLKELFTEGVDGVIAGSALYEGEIT 228
|
|
| PRK13585 |
PRK13585 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ... |
2-239 |
9.03e-55 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase;
Pssm-ID: 184165 Cd Length: 241 Bit Score: 175.87 E-value: 9.03e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 2 IIPALDLIDGTVVRLHQGDYGQQRDYGSDPLPRLQSYAAQGAEVLHLVDLTGAKDPAKRQIPLLKSLVAGVDVPVQVGGG 81
Cdd:PRK13585 5 VIPAVDMKGGKCVQLVQGEPGTETVSYGDPVEVAKRWVDAGAETLHLVDLDGAFEGERKNAEAIEKIIEAVGVPVQLGGG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 82 VRTEADVAALLEAGVARVVVGSTAVKSPEEVKGWFKRFGPERLVLALDVRidaDGnkQVAVSGWQENSGVTLEELVESYL 161
Cdd:PRK13585 85 IRSAEDAASLLDLGVDRVILGTAAVENPEIVRELSEEFGSERVMVSLDAK---DG--EVVIKGWTEKTGYTPVEAAKRFE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 162 PVGLQHVLCTDISRDGTLAGSNVSLYEEVCARY--PQVAfqsSGGIGDLKDIAALRGTGVRGVIVGRALLEGKFNVTEAI 239
Cdd:PRK13585 160 ELGAGSILFTNVDVEGLLEGVNTEPVKELVDSVdiPVIA---SGGVTTLDDLRALKEAGAAGVVVGSALYKGKFTLEEAI 236
|
|
| PRK14024 |
PRK14024 |
phosphoribosyl isomerase A; Provisional |
2-239 |
1.18e-42 |
|
phosphoribosyl isomerase A; Provisional
Pssm-ID: 237589 Cd Length: 241 Bit Score: 144.72 E-value: 1.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 2 IIPALDLIDGTVVRLHQGDYGQQRDYGsDPLPRLQSYAAQGAEVLHLVDLTGAKDPAKRQiPLLKSLVAGVDVPVQVGGG 81
Cdd:PRK14024 6 LLPAVDVVDGQAVRLVQGEAGSETSYG-SPLDAALAWQRDGAEWIHLVDLDAAFGRGSNR-ELLAEVVGKLDVKVELSGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 82 VRTEADVAALLEAGVARVVVGSTAVKSPEEVKGWFKRFGpERLVLALDVRidadgNKQVAVSGWQENSGvTLEELVESYL 161
Cdd:PRK14024 84 IRDDESLEAALATGCARVNIGTAALENPEWCARVIAEHG-DRVAVGLDVR-----GHTLAARGWTRDGG-DLWEVLERLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 162 PVGLQHVLCTDISRDGTLAGSNVSLYEEVCARY--PQVAfqsSGGIG---DLKDIAALRGTGVRGVIVGRALLEGKFNVT 236
Cdd:PRK14024 157 SAGCSRYVVTDVTKDGTLTGPNLELLREVCARTdaPVVA---SGGVSsldDLRALAELVPLGVEGAIVGKALYAGAFTLP 233
|
...
gi 1170892739 237 EAI 239
Cdd:PRK14024 234 EAL 236
|
|
| HisA_HisF |
cd04723 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ... |
1-240 |
9.78e-34 |
|
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) and the cyclase subunit of imidazoleglycerol phosphate synthase (HisF). The ProFAR isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene. The Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria.
Pssm-ID: 240074 [Multi-domain] Cd Length: 233 Bit Score: 121.61 E-value: 9.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 1 MIIPALDLIDGTVVRLHQGDYGQQRD------YGSDPLPRLQSYAAQGAEVLHLVDLTGAKDPAkRQIPLLKSLVAGVDV 74
Cdd:cd04723 1 RIIPVIDLKDGVVVHGVGGDRDNYRPitsnlcSTSDPLDVARAYKELGFRGLYIADLDAIMGRG-DNDEAIRELAAAWPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 75 PVQVGGGVRTEADVAALLEAGVARVVVGSTAVKSpEEVKGWFKRFGPERLVLALDVRiDADGNKQVAVSGWQEnsgvtLE 154
Cdd:cd04723 80 GLWVDGGIRSLENAQEWLKRGASRVIVGTETLPS-DDDEDRLAALGEQRLVLSLDFR-GGQLLKPTDFIGPEE-----LL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 155 ELVESYlpvgLQHVLCTDISRDGTLAGSNVSLYEEVCARYPqVAFQSSGGIGDLKDIAALRGTGVRGVIVGRALLEGKFN 234
Cdd:cd04723 153 RRLAKW----PEELIVLDIDRVGSGQGPDLELLERLAARAD-IPVIAAGGVRSVEDLELLKKLGASGALVASALHDGGLT 227
|
....*.
gi 1170892739 235 VTEAIQ 240
Cdd:cd04723 228 LEDVVR 233
|
|
| PRK13587 |
PRK13587 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
4-227 |
8.23e-33 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Provisional
Pssm-ID: 172156 Cd Length: 234 Bit Score: 119.16 E-value: 8.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 4 PALDLIDGTVVRLHQGDYGQQRDYGSDPLPRLQSYAA-QGAEVLHLVDLTGAKDPAKRQIPLLKSLVAGVDVPVQVGGGV 82
Cdd:PRK13587 6 PAIDLIGSTSVRLTEGKYDSEEKMSRSAEESIAYYSQfECVNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIEVGGGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 83 RTEADVAALLEAGVARVVVGSTAVKSPEEVKGWFKRFgPERLVLALDVRIDadgnkQVAVSGWQENSGVTLEELVESYLP 162
Cdd:PRK13587 86 RTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTF-PGRIYLSVDAYGE-----DIKVNGWEEDTELNLFSFVRQLSD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1170892739 163 VGLQHVLCTDISRDGTLAGSNVSLYEEVcARYPQVAFQSSGGIGDLKDIAALRGTGVRGVIVGRA 227
Cdd:PRK13587 160 IPLGGIIYTDIAKDGKMSGPNFELTGQL-VKATTIPVIASGGIRHQQDIQRLASLNVHAAIIGKA 223
|
|
| PRK04128 |
PRK04128 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
2-238 |
9.84e-30 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 167709 Cd Length: 228 Bit Score: 111.02 E-value: 9.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 2 IIPALDLIDGTVVRLHQGDYGQQRDYGsDPLprlqSYAAQGAEV---LHLVDLTGAKDPAKRQIPLLKSLVAGVDVPVQV 78
Cdd:PRK04128 4 IYPAIDLMNGKAVRLYKGRKEEVKVYG-DPV----EIALRFSEYvdkIHVVDLDGAFEGKPKNLDVVKNIIRETGLKVQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 79 GGGVRTEADVAALLEAGVARVVVGSTAVKSP--EEVKGWFkrfgpERLVLALDVRidadgNKQVAVSGWQENSGVTLEEL 156
Cdd:PRK04128 79 GGGLRTYESIKDAYEIGVENVIIGTKAFDLEflEKVTSEF-----EGITVSLDVK-----GGRIAVKGWLEESSIKVEDA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 157 VEsYLPVGLQHVLCTDISRDGTLAGsnvslYEEVCARYPQVAFQSSGGIGDLKDIAALRGTGVRGVIVGRALLEGKFNVT 236
Cdd:PRK04128 149 YE-MLKNYVNRFIYTSIERDGTLTG-----IEEIERFWGDEEFIYAGGVSSAEDVKKLAEIGFSGVIIGKALYEGRISLE 222
|
..
gi 1170892739 237 EA 238
Cdd:PRK04128 223 EL 224
|
|
| HisF |
cd04731 |
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ... |
2-240 |
1.16e-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: 108.32 E-value: 1.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 2 IIPALDLIDGTVVRLHQgdYGQQRDYGsDPLPRLQSYAAQGAEVLHLVDLTGAKDPAKRQIPLLKSLVAGVDVPVQVGGG 81
Cdd:cd04731 3 IIPCLDVKDGRVVKGVN--FKNLRDAG-DPVELAKRYNEQGADELVFLDITASSEGRETMLDVVERVAEEVFIPLTVGGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 82 VRTEADVAALLEAGVARVVVGSTAVKSPEEVKGWFKRFGPERLVLALDVRIDADGNKQVAVSGWQENSGVTLEELVESYL 161
Cdd:cd04731 80 IRSLEDARRLLRAGADKVSINSAAVENPELIREIAKRFGSQCVVVSIDAKRRGDGGYEVYTHGGRKPTGLDAVEWAKEVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 162 PVGLQHVLCTDISRDGTLAGSNVSLYEEVCAR--YPQVAfqsSGGIGDLKDI-AALRGTGVRGVIVGRALLEGKFNVTEA 238
Cdd:cd04731 160 ELGAGEILLTSMDRDGTKKGYDLELIRAVSSAvnIPVIA---SGGAGKPEHFvEAFEEGGADAALAASIFHFGEYTIAEL 236
|
..
gi 1170892739 239 IQ 240
Cdd:cd04731 237 KE 238
|
|
| PRK14114 |
PRK14114 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
1-235 |
1.81e-27 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 172604 Cd Length: 241 Bit Score: 105.48 E-value: 1.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 1 MIIPALDLIDGTVVRLHQGDYGQQRDYGSDPLPRLQSYAAQGAEVLHLVDLTGAKDPAKRQIPLLKSLVAGVDvPVQVGG 80
Cdd:PRK14114 2 LVVPAIDLFRGKVARMVKGKKENTIFYEKDPAELVEKLIEEGFTLIHVVDLSKAIENSVENLPVLEKLSEFAE-HIQIGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 81 GVRTEADVAALLEAGVARVVVGSTAVKSPEEVKgWFKRFGPERlVLALDVRidadgNKQVAVSGWQENSGVTLEELVESY 160
Cdd:PRK14114 81 GIRSLDYAEKLRKLGYRRQIVSSKVLEDPSFLK-FLKEIDVEP-VFSLDTR-----GGKVAFKGWLAEEEIDPVSLLKRL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 161 LPVGLQHVLCTDISRDGTLAGSNVSLYEEVcARYPQVAFQSSGGIGDLKDIAAL-----RGTG-VRGVIVGRALLEGKFN 234
Cdd:PRK14114 154 KEYGLEEIVHTEIEKDGTLQEHDFSLTRKI-AIEAEVKVFAAGGISSENSLKTAqrvhrETNGlLKGVIVGRAFLEGILT 232
|
.
gi 1170892739 235 V 235
Cdd:PRK14114 233 V 233
|
|
| hisF |
TIGR00735 |
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ... |
2-206 |
2.27e-26 |
|
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273241 Cd Length: 254 Bit Score: 102.83 E-value: 2.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 2 IIPALDLIDGTVVRLHQgdYGQQRDYGsDPLPRLQSYAAQGAEVLHLVDLTGAKDPAKRQIPLLKSLVAGVDVPVQVGGG 81
Cdd:TIGR00735 6 IIPCLDVRDGRVVKGVQ--FLNLRDAG-DPVELAQRYDEEGADELVFLDITASSEGRTTMIDVVERTAETVFIPLTVGGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 82 VRTEADVAALLEAGVARVVVGSTAVKSPEEVKGWFKRFGPERLVLALDVRIDADGNK---QVAVSGWQENSGVTLEELVE 158
Cdd:TIGR00735 83 IKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFGSQCIVVAIDAKRVYVNSYcwyEVYIYGGRESTGLDAVEWAK 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1170892739 159 SYLPVGLQHVLCTDISRDGTLAGSNVSLYEEVCARYPqVAFQSSGGIG 206
Cdd:TIGR00735 163 EVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEAVK-IPVIASGGAG 209
|
|
| HisF |
COG0107 |
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ... |
2-222 |
8.97e-24 |
|
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: 95.86 E-value: 8.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 2 IIPALDLIDGTVVRlhqgdyGQQ----RDYGsDPLPRLQSYAAQGAEVLHLVDLTGAKDpaKRQIPL--LKSLVAGVDVP 75
Cdd:COG0107 5 IIPCLDVKDGRVVK------GVNfvnlRDAG-DPVELAKRYNEQGADELVFLDITASSE--GRKTMLdvVRRVAEEVFIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 76 VQVGGGVRTEADVAALLEAGVARVVVGSTAVKSPEEVKGWFKRFGPERLVLALDVRIDADGNKQVAVSGWQENSGVTLEE 155
Cdd:COG0107 76 LTVGGGIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAIDAKRVPDGGWEVYTHGGRKPTGLDAVE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1170892739 156 L---VESYlpvGLQHVLCTDISRDGTLAGSNVSLYEEVCA--RYPQVAfqsSGGIGDLKDIA-ALRGTGVRGV 222
Cdd:COG0107 156 WakeAEEL---GAGEILLTSMDRDGTKDGYDLELTRAVSEavSIPVIA---SGGAGTLEHFVeVFTEGGADAA 222
|
|
| PRK13586 |
PRK13586 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
2-232 |
1.47e-17 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 237439 Cd Length: 232 Bit Score: 78.63 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 2 IIPALDLIDGTVVRLHQGDYGQQRDYGsDPLPRLQSYAAQGAEVLHLVDLTGAKDPAKRQIPLLKSLVAGVDVpVQVGGG 81
Cdd:PRK13586 4 IIPSIDISLGKAVKRIRGVKGTGLILG-NPIEIASKLYNEGYTRIHVVDLDAAEGVGNNEMYIKEISKIGFDW-IQVGGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 82 VRTEADVAALLEAGVARVVVGSTAVKSPEEVKGWFKRFGPERLVLAldvrIDADGNKQVAVSGWQENSgVTLEELVESYL 161
Cdd:PRK13586 82 IRDIEKAKRLLSLDVNALVFSTIVFTNFNLFHDIVREIGSNRVLVS----IDYDNTKRVLIRGWKEKS-MEVIDGIKKVN 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1170892739 162 PVGLQHVLCTDISRDGTLAG--SNVSLYeevcARYPQVAFQSSGGIGDLKDIAALRGTGVRGVIVGRALLEGK 232
Cdd:PRK13586 157 ELELLGIIFTYISNEGTTKGidYNVKDY----ARLIRGLKEYAGGVSSDADLEYLKNVGFDYIIVGMAFYLGK 225
|
|
| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
64-116 |
1.54e-05 |
|
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to N-acetylglucosamine-6-phosphate. This reaction is part of the pathway that allows the usage of sialic acid as a carbohydrate source. Sialic acids are a family of related sugars that are found as a component of glycoproteins, gangliosides, and other sialoglycoconjugates.
Pssm-ID: 240080 [Multi-domain] Cd Length: 219 Bit Score: 44.49 E-value: 1.54e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1170892739 64 LLKSLVAGVDVPVQVGGGVRTEADVAALLEAGVARVVVGsTAVKSPEEVKGWF 116
Cdd:cd04729 168 LLKELRKALGIPVIAEGRINSPEQAAKALELGADAVVVG-SAITRPEHITGWF 219
|
|
| PRK01130 |
PRK01130 |
putative N-acetylmannosamine-6-phosphate 2-epimerase; |
64-116 |
1.76e-05 |
|
putative N-acetylmannosamine-6-phosphate 2-epimerase;
Pssm-ID: 234907 Cd Length: 221 Bit Score: 44.37 E-value: 1.76e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1170892739 64 LLKSLVAGVDVPVQVGGGVRTEADVAALLEAGVARVVVGsTAVKSPEEVKGWF 116
Cdd:PRK01130 164 LLKELLKAVGCPVIAEGRINTPEQAKKALELGAHAVVVG-GAITRPEEITKWF 215
|
|
| PEP_mutase |
pfam13714 |
Phosphoenolpyruvate phosphomutase; This domain includes the enzyme Phosphoenolpyruvate ... |
34-103 |
1.47e-04 |
|
Phosphoenolpyruvate phosphomutase; This domain includes the enzyme Phosphoenolpyruvate phosphomutase (EC:5.4.2.9). This protein Swiss:O86937 has been characterized as catalysing the formation of a carbon-phosphorus bond by converting phosphoenolpyruvate (PEP) to phosphonopyruvate (P-Pyr). This enzyme has a TIM barrel fold.
Pssm-ID: 433424 Cd Length: 241 Bit Score: 41.80 E-value: 1.47e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 34 RLQSYAAQGAEVLHLvdlTGAKDPakrqiPLLKSLVAGVDVPVQVGGGVRTeADVAALLEAGVARVVVGS 103
Cdd:pfam13714 163 RARAYAEAGADGIFV---PGLLDP-----ADIAALVAAVPGPVNVLAGPGT-LSVAELAALGVARISYGN 223
|
|
| PLN02446 |
PLN02446 |
(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
77-228 |
9.99e-04 |
|
(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase
Pssm-ID: 215245 Cd Length: 262 Bit Score: 39.30 E-value: 9.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 77 QVGGGVrTEADVAALLEAGVARVVVGSTAVKS----PEEVKGWFKRFGPERLVLALDVRiDADGNKQVAVSGWQENSGVT 152
Cdd:PLN02446 87 QVGGGV-NSENAMSYLDAGASHVIVTSYVFRDgqidLERLKDLVRLVGKQRLVLDLSCR-KKDGRYYVVTDRWQKFSDLA 164
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1170892739 153 LEELVESYLPVGLQHVLCTDISRDGTLAGSNVSLYeEVCARYPQVAFQSSGGIGDLKDIAALR--GTGVRGVIVGRAL 228
Cdd:PLN02446 165 VDEETLEFLAAYCDEFLVHGVDVEGKRLGIDEELV-ALLGEHSPIPVTYAGGVRSLDDLERVKvaGGGRVDVTVGSAL 241
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
38-103 |
6.03e-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: 36.80 E-value: 6.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1170892739 38 YAAQGAEVLHLVD---LTGAKDPAKRQIPLLKSLVAGVDVPVQVGGGVRTEADVAALLEAGVARVVVGS 103
Cdd:cd04722 132 AEEAGVDEVGLGNgggGGGGRDAVPIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| PLN02591 |
PLN02591 |
tryptophan synthase |
31-111 |
6.61e-03 |
|
tryptophan synthase
Pssm-ID: 178201 Cd Length: 250 Bit Score: 36.95 E-value: 6.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892739 31 PLPRLQSYAAQGAEVLHLVDL---TGAKDPAKRQIP-LLKSLVAGVDVPVQVGGGVRTEADVAALLEAGVARVVVGSTAV 106
Cdd:PLN02591 143 PTERMKAIAEASEGFVYLVSStgvTGARASVSGRVEsLLQELKEVTDKPVAVGFGISKPEHAKQIAGWGADGVIVGSAMV 222
|
90
....*....|.
gi 1170892739 107 K------SPEE 111
Cdd:PLN02591 223 KalgeakSPEE 233
|
|
| |
