|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00748 |
PRK00748 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
1-238 |
4.80e-122 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated
Pssm-ID: 179108 Cd Length: 233 Bit Score: 346.28 E-value: 4.80e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 1 MIIPALDLIDGTVVRLHQGDYAKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAQRQIPLIKTLVAGVNVPVQVGG 80
Cdd:PRK00748 2 IIIPAIDLKDGKCVRLYQGDYDQATVYSDDPVAQAKAWEDQGAKWLHLVDLDGAKAGKPVNLELIEAIVKAVDIPVQVGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 81 GVRTEADVAALLDAGVARVVVGSTAVKSPEIVKSWFARFGaDALVLALDVRidehgNKQVAVSGWQEDSGVSLEELVETY 160
Cdd:PRK00748 82 GIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFP-GKIVVGLDAR-----DGKVATDGWLETSGVTAEDLAKRF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496060659 161 LPVGLKHVLCTDISRDGTLAGSNVALYEEVCAKYPqVAFQSSGGIGGIEDVAALRGTG-VRGVIVGRALLEGKFTVEEA 238
Cdd:PRK00748 156 EDAGVKAIIYTDISRDGTLSGPNVEATRELAAAVP-IPVIASGGVSSLDDIKALKGLGaVEGVIVGRALYEGKFDLAEA 233
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
1-243 |
2.80e-110 |
|
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: 316.59 E-value: 2.80e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 1 MIIPALDLIDGTVVRLHQGDYAKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAQRQIPLIKTLVAGVNVPVQVGG 80
Cdd:COG0106 1 IIIPAIDLKDGKCVRLVQGDYDQETVYSDDPVEVAKRWEDAGAEWLHLVDLDGAFAGKPVNLELIEEIAKATGLPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 81 GVRTEADVAALLDAGVARVVVGSTAVKSPEIVKSWFARFGaDALVLALDVRidehgNKQVAVSGWQEDSGVSLEELVETY 160
Cdd:COG0106 81 GIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFP-ERIVVGLDAR-----DGKVATDGWQETSGVDLEELAKRF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 161 LPVGLKHVLCTDISRDGTLAGSNVALYEEVCAKYPqVAFQSSGGIGGIEDVAALRGTGVRGVIVGRALLEGKFTVEEAIQ 240
Cdd:COG0106 155 EDAGVAAILYTDISRDGTLQGPNLELYRELAAATG-IPVIASGGVSSLDDLRALKELGVEGAIVGKALYEGKIDLEEALA 233
|
...
gi 496060659 241 CWQ 243
Cdd:COG0106 234 LAR 236
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
1-240 |
1.31e-107 |
|
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: 309.80 E-value: 1.31e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 1 MIIPALDLIDGTVVRLHQGDYAKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAQRQIPLIKTLVAGVNVPVQVGG 80
Cdd:cd04732 1 IIIPAIDLKDGKCVRLYQGDYDKKTVYSDDPVEVAKKWEEAGAKWLHVVDLDGAKGGEPVNLELIEEIVKAVGIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 81 GVRTEADVAALLDAGVARVVVGSTAVKSPEIVKSWFARFGADALVLALDVRIDEhgnkqVAVSGWQEDSGVSLEELVETY 160
Cdd:cd04732 81 GIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGGERIVVGLDAKDGK-----VATKGWLETSEVSLEELAKRF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 161 LPVGLKHVLCTDISRDGTLAGSNVALYEEVCAKYpQVAFQSSGGIGGIEDVAALRGTGVRGVIVGRALLEGKFTVEEAIQ 240
Cdd:cd04732 156 EELGVKAIIYTDISRDGTLSGPNFELYKELAAAT-GIPVIASGGVSSLDDIKALKELGVAGVIVGKALYEGKITLEEALA 234
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
2-237 |
1.41e-98 |
|
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: 286.79 E-value: 1.41e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 2 IIPALDLIDGTVVRLHQGDYAKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAQRQIPLIKTLVAGVNVPVQVGGG 81
Cdd:TIGR00007 1 IIPAIDIKDGKCVRLYQGDYDKETVYGDDPVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQVGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 82 VRTEADVAALLDAGVARVVVGSTAVKSPEIVKSWFARFGADALVLALDVRIDEhgnkqVAVSGWQEDSGVSLEELVETYL 161
Cdd:TIGR00007 81 IRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYGPERIVVSLDARGGE-----VAVKGWLEKSEVSLEELAKRLE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496060659 162 PVGLKHVLCTDISRDGTLAGSNVALYEEVCAKyPQVAFQSSGGIGGIEDVAALRGTGVRGVIVGRALLEGKFTVEE 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 |
3.50e-94 |
|
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: 275.51 E-value: 3.50e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 1 MIIPALDLIDGTVVRLHQGDYAKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAQRQIPLIKTLVAGVNVPVQVGG 80
Cdd:pfam00977 1 RIIPAIDLKDGRVVRLVKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 81 GVRTEADVAALLDAGVARVVVGSTAVKSPEIVKSWFARFGADALVLALDVRidehgNKQVAVSGWQEDSGVSLEELVETY 160
Cdd:pfam00977 81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAIDAR-----RGKVAINGWREDTGIDAVEWAKEL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496060659 161 LPVGLKHVLCTDISRDGTLAGSNVALYEEVCAKYpQVAFQSSGGIGGIEDVAALRGTGVRGVIVGRALLEGKFT 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 |
4.80e-122 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated
Pssm-ID: 179108 Cd Length: 233 Bit Score: 346.28 E-value: 4.80e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 1 MIIPALDLIDGTVVRLHQGDYAKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAQRQIPLIKTLVAGVNVPVQVGG 80
Cdd:PRK00748 2 IIIPAIDLKDGKCVRLYQGDYDQATVYSDDPVAQAKAWEDQGAKWLHLVDLDGAKAGKPVNLELIEAIVKAVDIPVQVGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 81 GVRTEADVAALLDAGVARVVVGSTAVKSPEIVKSWFARFGaDALVLALDVRidehgNKQVAVSGWQEDSGVSLEELVETY 160
Cdd:PRK00748 82 GIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFP-GKIVVGLDAR-----DGKVATDGWLETSGVTAEDLAKRF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496060659 161 LPVGLKHVLCTDISRDGTLAGSNVALYEEVCAKYPqVAFQSSGGIGGIEDVAALRGTG-VRGVIVGRALLEGKFTVEEA 238
Cdd:PRK00748 156 EDAGVKAIIYTDISRDGTLSGPNVEATRELAAAVP-IPVIASGGVSSLDDIKALKGLGaVEGVIVGRALYEGKFDLAEA 233
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
1-243 |
2.80e-110 |
|
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: 316.59 E-value: 2.80e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 1 MIIPALDLIDGTVVRLHQGDYAKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAQRQIPLIKTLVAGVNVPVQVGG 80
Cdd:COG0106 1 IIIPAIDLKDGKCVRLVQGDYDQETVYSDDPVEVAKRWEDAGAEWLHLVDLDGAFAGKPVNLELIEEIAKATGLPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 81 GVRTEADVAALLDAGVARVVVGSTAVKSPEIVKSWFARFGaDALVLALDVRidehgNKQVAVSGWQEDSGVSLEELVETY 160
Cdd:COG0106 81 GIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFP-ERIVVGLDAR-----DGKVATDGWQETSGVDLEELAKRF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 161 LPVGLKHVLCTDISRDGTLAGSNVALYEEVCAKYPqVAFQSSGGIGGIEDVAALRGTGVRGVIVGRALLEGKFTVEEAIQ 240
Cdd:COG0106 155 EDAGVAAILYTDISRDGTLQGPNLELYRELAAATG-IPVIASGGVSSLDDLRALKELGVEGAIVGKALYEGKIDLEEALA 233
|
...
gi 496060659 241 CWQ 243
Cdd:COG0106 234 LAR 236
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
1-240 |
1.31e-107 |
|
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: 309.80 E-value: 1.31e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 1 MIIPALDLIDGTVVRLHQGDYAKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAQRQIPLIKTLVAGVNVPVQVGG 80
Cdd:cd04732 1 IIIPAIDLKDGKCVRLYQGDYDKKTVYSDDPVEVAKKWEEAGAKWLHVVDLDGAKGGEPVNLELIEEIVKAVGIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 81 GVRTEADVAALLDAGVARVVVGSTAVKSPEIVKSWFARFGADALVLALDVRIDEhgnkqVAVSGWQEDSGVSLEELVETY 160
Cdd:cd04732 81 GIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGGERIVVGLDAKDGK-----VATKGWLETSEVSLEELAKRF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 161 LPVGLKHVLCTDISRDGTLAGSNVALYEEVCAKYpQVAFQSSGGIGGIEDVAALRGTGVRGVIVGRALLEGKFTVEEAIQ 240
Cdd:cd04732 156 EELGVKAIIYTDISRDGTLSGPNFELYKELAAAT-GIPVIASGGVSSLDDIKALKELGVAGVIVGKALYEGKITLEEALA 234
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
2-237 |
1.41e-98 |
|
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: 286.79 E-value: 1.41e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 2 IIPALDLIDGTVVRLHQGDYAKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAQRQIPLIKTLVAGVNVPVQVGGG 81
Cdd:TIGR00007 1 IIPAIDIKDGKCVRLYQGDYDKETVYGDDPVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQVGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 82 VRTEADVAALLDAGVARVVVGSTAVKSPEIVKSWFARFGADALVLALDVRIDEhgnkqVAVSGWQEDSGVSLEELVETYL 161
Cdd:TIGR00007 81 IRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYGPERIVVSLDARGGE-----VAVKGWLEKSEVSLEELAKRLE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496060659 162 PVGLKHVLCTDISRDGTLAGSNVALYEEVCAKyPQVAFQSSGGIGGIEDVAALRGTGVRGVIVGRALLEGKFTVEE 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 |
3.50e-94 |
|
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: 275.51 E-value: 3.50e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 1 MIIPALDLIDGTVVRLHQGDYAKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAQRQIPLIKTLVAGVNVPVQVGG 80
Cdd:pfam00977 1 RIIPAIDLKDGRVVRLVKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 81 GVRTEADVAALLDAGVARVVVGSTAVKSPEIVKSWFARFGADALVLALDVRidehgNKQVAVSGWQEDSGVSLEELVETY 160
Cdd:pfam00977 81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAIDAR-----RGKVAINGWREDTGIDAVEWAKEL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496060659 161 LPVGLKHVLCTDISRDGTLAGSNVALYEEVCAKYpQVAFQSSGGIGGIEDVAALRGTGVRGVIVGRALLEGKFT 234
Cdd:pfam00977 156 EELGAGEILLTDIDRDGTLSGPDLELTRELAEAV-NIPVIASGGVGSLEDLKELFTEGVDGVIAGSALYEGEIT 228
|
|
| PRK13585 |
PRK13585 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ... |
2-239 |
1.10e-54 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase;
Pssm-ID: 184165 Cd Length: 241 Bit Score: 175.48 E-value: 1.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 2 IIPALDLIDGTVVRLHQGDYAKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAQRQIPLIKTLVAGVNVPVQVGGG 81
Cdd:PRK13585 5 VIPAVDMKGGKCVQLVQGEPGTETVSYGDPVEVAKRWVDAGAETLHLVDLDGAFEGERKNAEAIEKIIEAVGVPVQLGGG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 82 VRTEADVAALLDAGVARVVVGSTAVKSPEIVKSWFARFGADALVLALDVRidehgNKQVAVSGWQEDSGVSLEELVETYL 161
Cdd:PRK13585 85 IRSAEDAASLLDLGVDRVILGTAAVENPEIVRELSEEFGSERVMVSLDAK-----DGEVVIKGWTEKTGYTPVEAAKRFE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 162 PVGLKHVLCTDISRDGTLAGSNVALYEEVCA--KYPQVAfqsSGGIGGIEDVAALRGTGVRGVIVGRALLEGKFTVEEAI 239
Cdd:PRK13585 160 ELGAGSILFTNVDVEGLLEGVNTEPVKELVDsvDIPVIA---SGGVTTLDDLRALKEAGAAGVVVGSALYKGKFTLEEAI 236
|
|
| PRK14024 |
PRK14024 |
phosphoribosyl isomerase A; Provisional |
2-239 |
1.74e-42 |
|
phosphoribosyl isomerase A; Provisional
Pssm-ID: 237589 Cd Length: 241 Bit Score: 144.33 E-value: 1.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 2 IIPALDLIDGTVVRLHQGDYAKQRDYGnDPLPRLQDYAAQGAEVLHLVDLTGAKDPAQRQiPLIKTLVAGVNVPVQVGGG 81
Cdd:PRK14024 6 LLPAVDVVDGQAVRLVQGEAGSETSYG-SPLDAALAWQRDGAEWIHLVDLDAAFGRGSNR-ELLAEVVGKLDVKVELSGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 82 VRTEADVAALLDAGVARVVVGSTAVKSPEIVKSWFARFGaDALVLALDVRidehgNKQVAVSGWQEDSGvSLEELVETYL 161
Cdd:PRK14024 84 IRDDESLEAALATGCARVNIGTAALENPEWCARVIAEHG-DRVAVGLDVR-----GHTLAARGWTRDGG-DLWEVLERLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 162 PVGLKHVLCTDISRDGTLAGSNVALYEEVCAKY--PQVAfqsSGGIGGIEDVAALRG---TGVRGVIVGRALLEGKFTVE 236
Cdd:PRK14024 157 SAGCSRYVVTDVTKDGTLTGPNLELLREVCARTdaPVVA---SGGVSSLDDLRALAElvpLGVEGAIVGKALYAGAFTLP 233
|
...
gi 496060659 237 EAI 239
Cdd:PRK14024 234 EAL 236
|
|
| HisA_HisF |
cd04723 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ... |
1-240 |
2.96e-34 |
|
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) and the cyclase subunit of imidazoleglycerol phosphate synthase (HisF). The ProFAR isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene. The Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria.
Pssm-ID: 240074 [Multi-domain] Cd Length: 233 Bit Score: 122.76 E-value: 2.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 1 MIIPALDLIDGTVVRLHQGDYAKQRD------YGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAqRQIPLIKTLVAGVNV 74
Cdd:cd04723 1 RIIPVIDLKDGVVVHGVGGDRDNYRPitsnlcSTSDPLDVARAYKELGFRGLYIADLDAIMGRG-DNDEAIRELAAAWPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 75 PVQVGGGVRTEADVAALLDAGVARVVVGSTAVKSpEIVKSWFARFGADALVLALDVRidehgNKQVAVSGWQEDSgVSLE 154
Cdd:cd04723 80 GLWVDGGIRSLENAQEWLKRGASRVIVGTETLPS-DDDEDRLAALGEQRLVLSLDFR-----GGQLLKPTDFIGP-EELL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 155 ELVETYLpvglKHVLCTDISRDGTLAGSNVALYEEVCAKYPqVAFQSSGGIGGIEDVAALRGTGVRGVIVGRALLEGKFT 234
Cdd:cd04723 153 RRLAKWP----EELIVLDIDRVGSGQGPDLELLERLAARAD-IPVIAAGGVRSVEDLELLKKLGASGALVASALHDGGLT 227
|
....*.
gi 496060659 235 VEEAIQ 240
Cdd:cd04723 228 LEDVVR 233
|
|
| PRK04128 |
PRK04128 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
2-238 |
3.65e-32 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 167709 Cd Length: 228 Bit Score: 117.18 E-value: 3.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 2 IIPALDLIDGTVVRLHQGDYAKQRDYGnDPLP---RLQDYAaqgaEVLHLVDLTGAKDPAQRQIPLIKTLVAGVNVPVQV 78
Cdd:PRK04128 4 IYPAIDLMNGKAVRLYKGRKEEVKVYG-DPVEialRFSEYV----DKIHVVDLDGAFEGKPKNLDVVKNIIRETGLKVQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 79 GGGVRTEADVAALLDAGVARVVVGSTAVKSpEIVKSWFARFgaDALVLALDVRidehgNKQVAVSGWQEDSGVSLEELVE 158
Cdd:PRK04128 79 GGGLRTYESIKDAYEIGVENVIIGTKAFDL-EFLEKVTSEF--EGITVSLDVK-----GGRIAVKGWLEESSIKVEDAYE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 159 TyLPVGLKHVLCTDISRDGTLAGsnvalYEEVCAKYPQVAFQSSGGIGGIEDVAALRGTGVRGVIVGRALLEGKFTVEEA 238
Cdd:PRK04128 151 M-LKNYVNRFIYTSIERDGTLTG-----IEEIERFWGDEEFIYAGGVSSAEDVKKLAEIGFSGVIIGKALYEGRISLEEL 224
|
|
| PRK13587 |
PRK13587 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
4-227 |
9.70e-32 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Provisional
Pssm-ID: 172156 Cd Length: 234 Bit Score: 116.47 E-value: 9.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 4 PALDLIDGTVVRLHQGDYAKQRDYGNDPLPRLQDYAA-QGAEVLHLVDLTGAKDPAQRQIPLIKTLVAGVNVPVQVGGGV 82
Cdd:PRK13587 6 PAIDLIGSTSVRLTEGKYDSEEKMSRSAEESIAYYSQfECVNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIEVGGGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 83 RTEADVAALLDAGVARVVVGSTAVKSPEIVKSWFARFgADALVLALDVRIDehgnkQVAVSGWQEDSGVSLEELVETYLP 162
Cdd:PRK13587 86 RTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTF-PGRIYLSVDAYGE-----DIKVNGWEEDTELNLFSFVRQLSD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496060659 163 VGLKHVLCTDISRDGTLAGSNVALYEEVcAKYPQVAFQSSGGIGGIEDVAALRGTGVRGVIVGRA 227
Cdd:PRK13587 160 IPLGGIIYTDIAKDGKMSGPNFELTGQL-VKATTIPVIASGGIRHQQDIQRLASLNVHAAIIGKA 223
|
|
| HisF |
cd04731 |
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ... |
2-240 |
6.61e-30 |
|
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: 111.79 E-value: 6.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 2 IIPALDLIDGTVVRLHQgdYAKQRDYGnDPLPRLQDYAAQGAEVLHLVDLTGAKDPAQRQIPLIKTLVAGVNVPVQVGGG 81
Cdd:cd04731 3 IIPCLDVKDGRVVKGVN--FKNLRDAG-DPVELAKRYNEQGADELVFLDITASSEGRETMLDVVERVAEEVFIPLTVGGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 82 VRTEADVAALLDAGVARVVVGSTAVKSPEIVKSWFARFGADALVLALDVRIDEHGNKQVAVSGWQEDSGVSLEELVETYL 161
Cdd:cd04731 80 IRSLEDARRLLRAGADKVSINSAAVENPELIREIAKRFGSQCVVVSIDAKRRGDGGYEVYTHGGRKPTGLDAVEWAKEVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 162 PVGLKHVLCTDISRDGTLAGSNVALYEEVCA--KYPQVAfqsSGGIGGIED-VAALRGTGVRGVIVGRALLEGKFTVEEA 238
Cdd:cd04731 160 ELGAGEILLTSMDRDGTKKGYDLELIRAVSSavNIPVIA---SGGAGKPEHfVEAFEEGGADAALAASIFHFGEYTIAEL 236
|
..
gi 496060659 239 IQ 240
Cdd:cd04731 237 KE 238
|
|
| PRK14114 |
PRK14114 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
1-236 |
1.73e-27 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 172604 Cd Length: 241 Bit Score: 105.48 E-value: 1.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 1 MIIPALDLIDGTVVRLHQGDYAKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAQRQIPLIKTLVAGVNvPVQVGG 80
Cdd:PRK14114 2 LVVPAIDLFRGKVARMVKGKKENTIFYEKDPAELVEKLIEEGFTLIHVVDLSKAIENSVENLPVLEKLSEFAE-HIQIGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 81 GVRTEADVAALLDAGVARVVVGSTAVKSPEIVKSwFARFGADAlVLALDVRidehgNKQVAVSGWQEDSGVSLEELVETY 160
Cdd:PRK14114 81 GIRSLDYAEKLRKLGYRRQIVSSKVLEDPSFLKF-LKEIDVEP-VFSLDTR-----GGKVAFKGWLAEEEIDPVSLLKRL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 161 LPVGLKHVLCTDISRDGTLAGSNVALYEEVcAKYPQVAFQSSGGIGGIEDVAAL-----RGTG-VRGVIVGRALLEGKFT 234
Cdd:PRK14114 154 KEYGLEEIVHTEIEKDGTLQEHDFSLTRKI-AIEAEVKVFAAGGISSENSLKTAqrvhrETNGlLKGVIVGRAFLEGILT 232
|
..
gi 496060659 235 VE 236
Cdd:PRK14114 233 VE 234
|
|
| hisF |
TIGR00735 |
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ... |
2-237 |
1.15e-25 |
|
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273241 Cd Length: 254 Bit Score: 100.90 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 2 IIPALDLIDGTVVRlhqGDYAKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAQRQIPLIKTLVAGVNVPVQVGGG 81
Cdd:TIGR00735 6 IIPCLDVRDGRVVK---GVQFLNLRDAGDPVELAQRYDEEGADELVFLDITASSEGRTTMIDVVERTAETVFIPLTVGGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 82 VRTEADVAALLDAGVARVVVGSTAVKSPEIVKSWFARFGADALVLALDVR---IDEHGNKQVAVSGWQEDSGVSLEELVE 158
Cdd:TIGR00735 83 IKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFGSQCIVVAIDAKrvyVNSYCWYEVYIYGGRESTGLDAVEWAK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 159 TYLPVGLKHVLCTDISRDGTLAGSNVALYEEVCA--KYPQVAfqsSGGIGGIEDVA-ALRGTGVRGVIVGRALLEGKFTV 235
Cdd:TIGR00735 163 EVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEavKIPVIA---SGGAGKPEHFYeAFTKGKADAALAASVFHYREITI 239
|
..
gi 496060659 236 EE 237
Cdd:TIGR00735 240 GE 241
|
|
| HisF |
COG0107 |
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ... |
2-222 |
6.27e-25 |
|
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: 98.94 E-value: 6.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 2 IIPALDLIDGTVVRLHQgdYAKQRDYGnDPLPRLQDYAAQGAEVLHLVDLTGAKDpaQRQIPL--IKTLVAGVNVPVQVG 79
Cdd:COG0107 5 IIPCLDVKDGRVVKGVN--FVNLRDAG-DPVELAKRYNEQGADELVFLDITASSE--GRKTMLdvVRRVAEEVFIPLTVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 80 GGVRTEADVAALLDAGVARVVVGSTAVKSPEIVKSWFARFGADALVLALDVRIDEHGNKQVAVSGWQEDSGVSLEELVet 159
Cdd:COG0107 80 GGIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAIDAKRVPDGGWEVYTHGGRKPTGLDAVEWA-- 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496060659 160 ylpvglKHV--------LCTDISRDGTLAGSNVALYEEVCA--KYPQVAfqsSGGIGGIED-VAALRGTGVRGV 222
Cdd:COG0107 158 ------KEAeelgageiLLTSMDRDGTKDGYDLELTRAVSEavSIPVIA---SGGAGTLEHfVEVFTEGGADAA 222
|
|
| PRK13586 |
PRK13586 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
2-232 |
4.17e-16 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 237439 Cd Length: 232 Bit Score: 74.78 E-value: 4.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 2 IIPALDLIDGTVVRLHQGDYAKQRDYGNdPLPRLQDYAAQGAEVLHLVDLTGAKDPAQRQIpLIKTLVAGVNVPVQVGGG 81
Cdd:PRK13586 4 IIPSIDISLGKAVKRIRGVKGTGLILGN-PIEIASKLYNEGYTRIHVVDLDAAEGVGNNEM-YIKEISKIGFDWIQVGGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 82 VRTEADVAALLDAGVARVVVGSTAVKSPEIVKSWFARFGADALVLAldvrIDEHGNKQVAVSGWQEDSgVSLEELVETYL 161
Cdd:PRK13586 82 IRDIEKAKRLLSLDVNALVFSTIVFTNFNLFHDIVREIGSNRVLVS----IDYDNTKRVLIRGWKEKS-MEVIDGIKKVN 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496060659 162 PVGLKHVLCTDISRDGTLAG--SNVALYeevcAKYPQVAFQSSGGIGGIEDVAALRGTGVRGVIVGRALLEGK 232
Cdd:PRK13586 157 ELELLGIIFTYISNEGTTKGidYNVKDY----ARLIRGLKEYAGGVSSDADLEYLKNVGFDYIIVGMAFYLGK 225
|
|
| PRK01130 |
PRK01130 |
putative N-acetylmannosamine-6-phosphate 2-epimerase; |
64-118 |
1.92e-04 |
|
putative N-acetylmannosamine-6-phosphate 2-epimerase;
Pssm-ID: 234907 Cd Length: 221 Bit Score: 41.29 E-value: 1.92e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 496060659 64 LIKTLVAGVNVPVQVGGGVRTEADVAALLDAGVARVVVGsTAVKSPEIVKSWFAR 118
Cdd:PRK01130 164 LLKELLKAVGCPVIAEGRINTPEQAKKALELGAHAVVVG-GAITRPEEITKWFVD 217
|
|
| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
64-116 |
4.43e-04 |
|
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: 40.25 E-value: 4.43e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 496060659 64 LIKTLVAGVNVPVQVGGGVRTEADVAALLDAGVARVVVGsTAVKSPEIVKSWF 116
Cdd:cd04729 168 LLKELRKALGIPVIAEGRINSPEQAAKALELGADAVVVG-SAITRPEHITGWF 219
|
|
| PEP_mutase |
pfam13714 |
Phosphoenolpyruvate phosphomutase; This domain includes the enzyme Phosphoenolpyruvate ... |
34-103 |
7.76e-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: 39.49 E-value: 7.76e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 34 RLQDYAAQGAEVLHLvdlTGAKDPAQrqiplIKTLVAGVNVPVQVGGGVRTeADVAALLDAGVARVVVGS 103
Cdd:pfam13714 163 RARAYAEAGADGIFV---PGLLDPAD-----IAALVAAVPGPVNVLAGPGT-LSVAELAALGVARISYGN 223
|
|
| PLN02446 |
PLN02446 |
(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
77-228 |
5.41e-03 |
|
(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase
Pssm-ID: 215245 Cd Length: 262 Bit Score: 37.38 E-value: 5.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496060659 77 QVGGGVrTEADVAALLDAGVARVVVGSTAVKSPEI----VKSWFARFGADALVLALDVRiDEHGNKQVAVSGWQEDSGVS 152
Cdd:PLN02446 87 QVGGGV-NSENAMSYLDAGASHVIVTSYVFRDGQIdlerLKDLVRLVGKQRLVLDLSCR-KKDGRYYVVTDRWQKFSDLA 164
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496060659 153 LEELVETYLPVGLKHVLCTDISRDGTLAGSNVALYeEVCAKYPQVAFQSSGGIGGIEDVAALR--GTGVRGVIVGRAL 228
Cdd:PLN02446 165 VDEETLEFLAAYCDEFLVHGVDVEGKRLGIDEELV-ALLGEHSPIPVTYAGGVRSLDDLERVKvaGGGRVDVTVGSAL 241
|
|
| |
