|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00748 |
PRK00748 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
1-238 |
1.13e-121 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated
Pssm-ID: 179108 Cd Length: 233 Bit Score: 345.51 E-value: 1.13e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 1 MIIPALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQAYAAEGAEVLHLVDLTGAKDPAKRQIPLLKTLVAGVDVPVQVGG 80
Cdd:PRK00748 2 IIIPAIDLKDGKCVRLYQGDYDQATVYSDDPVAQAKAWEDQGAKWLHLVDLDGAKAGKPVNLELIEAIVKAVDIPVQVGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 81 GVRTEADVAALLDAGVARVVVGSTAVKDPESVKGWFRRFGaDALVLALDVRidaqgNKQVAVSGWQENSGVTLEELVGMY 160
Cdd:PRK00748 82 GIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFP-GKIVVGLDAR-----DGKVATDGWLETSGVTAEDLAKRF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505385293 161 LPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYPqVAFQSSGGIGDLADIAALRGTG-VRGVIVGRALLEGKFTVKEA 238
Cdd:PRK00748 156 EDAGVKAIIYTDISRDGTLSGPNVEATRELAAAVP-IPVIASGGVSSLDDIKALKGLGaVEGVIVGRALYEGKFDLAEA 233
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
1-243 |
2.40e-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: 316.98 E-value: 2.40e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 1 MIIPALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQAYAAEGAEVLHLVDLTGAKDPAKRQIPLLKTLVAGVDVPVQVGG 80
Cdd:COG0106 1 IIIPAIDLKDGKCVRLVQGDYDQETVYSDDPVEVAKRWEDAGAEWLHLVDLDGAFAGKPVNLELIEEIAKATGLPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 81 GVRTEADVAALLDAGVARVVVGSTAVKDPESVKGWFRRFGaDALVLALDVRidaqgNKQVAVSGWQENSGVTLEELVGMY 160
Cdd:COG0106 81 GIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFP-ERIVVGLDAR-----DGKVATDGWQETSGVDLEELAKRF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 161 LPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYPqVAFQSSGGIGDLADIAALRGTGVRGVIVGRALLEGKFTVKEAIQ 240
Cdd:COG0106 155 EDAGVAAILYTDISRDGTLQGPNLELYRELAAATG-IPVIASGGVSSLDDLRALKELGVEGAIVGKALYEGKIDLEEALA 233
|
...
gi 505385293 241 CWQ 243
Cdd:COG0106 234 LAR 236
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
1-240 |
1.90e-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: 309.41 E-value: 1.90e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 1 MIIPALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQAYAAEGAEVLHLVDLTGAKDPAKRQIPLLKTLVAGVDVPVQVGG 80
Cdd:cd04732 1 IIIPAIDLKDGKCVRLYQGDYDKKTVYSDDPVEVAKKWEEAGAKWLHVVDLDGAKGGEPVNLELIEEIVKAVGIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 81 GVRTEADVAALLDAGVARVVVGSTAVKDPESVKGWFRRFGADALVLALDVRIDaqgnkQVAVSGWQENSGVTLEELVGMY 160
Cdd:cd04732 81 GIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGGERIVVGLDAKDG-----KVATKGWLETSEVSLEELAKRF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 161 LPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYpQVAFQSSGGIGDLADIAALRGTGVRGVIVGRALLEGKFTVKEAIQ 240
Cdd:cd04732 156 EELGVKAIIYTDISRDGTLSGPNFELYKELAAAT-GIPVIASGGVSSLDDIKALKELGVAGVIVGKALYEGKITLEEALA 234
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
2-237 |
6.21e-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: 287.94 E-value: 6.21e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 2 IIPALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQAYAAEGAEVLHLVDLTGAKDPAKRQIPLLKTLVAGVDVPVQVGGG 81
Cdd:TIGR00007 1 IIPAIDIKDGKCVRLYQGDYDKETVYGDDPVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQVGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 82 VRTEADVAALLDAGVARVVVGSTAVKDPESVKGWFRRFGADALVLALDVRIDAqgnkqVAVSGWQENSGVTLEELVGMYL 161
Cdd:TIGR00007 81 IRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYGPERIVVSLDARGGE-----VAVKGWLEKSEVSLEELAKRLE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505385293 162 PVGLKHVLCTDISRDGTLAGSNVSLYEEVCARyPQVAFQSSGGIGDLADIAALRGTGVRGVIVGRALLEGKFTVKE 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 |
3.31e-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: 275.90 E-value: 3.31e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 1 MIIPALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQAYAAEGAEVLHLVDLTGAKDPAKRQIPLLKTLVAGVDVPVQVGG 80
Cdd:pfam00977 1 RIIPAIDLKDGRVVRLVKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 81 GVRTEADVAALLDAGVARVVVGSTAVKDPESVKGWFRRFGADALVLALDVRidaqgNKQVAVSGWQENSGVTLEELVGMY 160
Cdd:pfam00977 81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAIDAR-----RGKVAINGWREDTGIDAVEWAKEL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505385293 161 LPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYpQVAFQSSGGIGDLADIAALRGTGVRGVIVGRALLEGKFT 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 |
1.13e-121 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated
Pssm-ID: 179108 Cd Length: 233 Bit Score: 345.51 E-value: 1.13e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 1 MIIPALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQAYAAEGAEVLHLVDLTGAKDPAKRQIPLLKTLVAGVDVPVQVGG 80
Cdd:PRK00748 2 IIIPAIDLKDGKCVRLYQGDYDQATVYSDDPVAQAKAWEDQGAKWLHLVDLDGAKAGKPVNLELIEAIVKAVDIPVQVGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 81 GVRTEADVAALLDAGVARVVVGSTAVKDPESVKGWFRRFGaDALVLALDVRidaqgNKQVAVSGWQENSGVTLEELVGMY 160
Cdd:PRK00748 82 GIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFP-GKIVVGLDAR-----DGKVATDGWLETSGVTAEDLAKRF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505385293 161 LPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYPqVAFQSSGGIGDLADIAALRGTG-VRGVIVGRALLEGKFTVKEA 238
Cdd:PRK00748 156 EDAGVKAIIYTDISRDGTLSGPNVEATRELAAAVP-IPVIASGGVSSLDDIKALKGLGaVEGVIVGRALYEGKFDLAEA 233
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
1-243 |
2.40e-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: 316.98 E-value: 2.40e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 1 MIIPALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQAYAAEGAEVLHLVDLTGAKDPAKRQIPLLKTLVAGVDVPVQVGG 80
Cdd:COG0106 1 IIIPAIDLKDGKCVRLVQGDYDQETVYSDDPVEVAKRWEDAGAEWLHLVDLDGAFAGKPVNLELIEEIAKATGLPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 81 GVRTEADVAALLDAGVARVVVGSTAVKDPESVKGWFRRFGaDALVLALDVRidaqgNKQVAVSGWQENSGVTLEELVGMY 160
Cdd:COG0106 81 GIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFP-ERIVVGLDAR-----DGKVATDGWQETSGVDLEELAKRF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 161 LPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYPqVAFQSSGGIGDLADIAALRGTGVRGVIVGRALLEGKFTVKEAIQ 240
Cdd:COG0106 155 EDAGVAAILYTDISRDGTLQGPNLELYRELAAATG-IPVIASGGVSSLDDLRALKELGVEGAIVGKALYEGKIDLEEALA 233
|
...
gi 505385293 241 CWQ 243
Cdd:COG0106 234 LAR 236
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
1-240 |
1.90e-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: 309.41 E-value: 1.90e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 1 MIIPALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQAYAAEGAEVLHLVDLTGAKDPAKRQIPLLKTLVAGVDVPVQVGG 80
Cdd:cd04732 1 IIIPAIDLKDGKCVRLYQGDYDKKTVYSDDPVEVAKKWEEAGAKWLHVVDLDGAKGGEPVNLELIEEIVKAVGIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 81 GVRTEADVAALLDAGVARVVVGSTAVKDPESVKGWFRRFGADALVLALDVRIDaqgnkQVAVSGWQENSGVTLEELVGMY 160
Cdd:cd04732 81 GIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGGERIVVGLDAKDG-----KVATKGWLETSEVSLEELAKRF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 161 LPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYpQVAFQSSGGIGDLADIAALRGTGVRGVIVGRALLEGKFTVKEAIQ 240
Cdd:cd04732 156 EELGVKAIIYTDISRDGTLSGPNFELYKELAAAT-GIPVIASGGVSSLDDIKALKELGVAGVIVGKALYEGKITLEEALA 234
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
2-237 |
6.21e-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: 287.94 E-value: 6.21e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 2 IIPALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQAYAAEGAEVLHLVDLTGAKDPAKRQIPLLKTLVAGVDVPVQVGGG 81
Cdd:TIGR00007 1 IIPAIDIKDGKCVRLYQGDYDKETVYGDDPVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQVGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 82 VRTEADVAALLDAGVARVVVGSTAVKDPESVKGWFRRFGADALVLALDVRIDAqgnkqVAVSGWQENSGVTLEELVGMYL 161
Cdd:TIGR00007 81 IRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYGPERIVVSLDARGGE-----VAVKGWLEKSEVSLEELAKRLE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505385293 162 PVGLKHVLCTDISRDGTLAGSNVSLYEEVCARyPQVAFQSSGGIGDLADIAALRGTGVRGVIVGRALLEGKFTVKE 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 |
3.31e-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: 275.90 E-value: 3.31e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 1 MIIPALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQAYAAEGAEVLHLVDLTGAKDPAKRQIPLLKTLVAGVDVPVQVGG 80
Cdd:pfam00977 1 RIIPAIDLKDGRVVRLVKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 81 GVRTEADVAALLDAGVARVVVGSTAVKDPESVKGWFRRFGADALVLALDVRidaqgNKQVAVSGWQENSGVTLEELVGMY 160
Cdd:pfam00977 81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAIDAR-----RGKVAINGWREDTGIDAVEWAKEL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505385293 161 LPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYpQVAFQSSGGIGDLADIAALRGTGVRGVIVGRALLEGKFT 234
Cdd:pfam00977 156 EELGAGEILLTDIDRDGTLSGPDLELTRELAEAV-NIPVIASGGVGSLEDLKELFTEGVDGVIAGSALYEGEIT 228
|
|
| PRK13585 |
PRK13585 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ... |
2-239 |
5.00e-54 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase;
Pssm-ID: 184165 Cd Length: 241 Bit Score: 173.94 E-value: 5.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 2 IIPALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQAYAAEGAEVLHLVDLTGAKDPAKRQIPLLKTLVAGVDVPVQVGGG 81
Cdd:PRK13585 5 VIPAVDMKGGKCVQLVQGEPGTETVSYGDPVEVAKRWVDAGAETLHLVDLDGAFEGERKNAEAIEKIIEAVGVPVQLGGG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 82 VRTEADVAALLDAGVARVVVGSTAVKDPESVKGWFRRFGADALVLALDVRidaqgNKQVAVSGWQENSGVTLEELVGMYL 161
Cdd:PRK13585 85 IRSAEDAASLLDLGVDRVILGTAAVENPEIVRELSEEFGSERVMVSLDAK-----DGEVVIKGWTEKTGYTPVEAAKRFE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 162 PVGLKHVLCTDISRDGTLAGSNVSLYEEVCARY--PQVAfqsSGGIGDLADIAALRGTGVRGVIVGRALLEGKFTVKEAI 239
Cdd:PRK13585 160 ELGAGSILFTNVDVEGLLEGVNTEPVKELVDSVdiPVIA---SGGVTTLDDLRALKEAGAAGVVVGSALYKGKFTLEEAI 236
|
|
| PRK14024 |
PRK14024 |
phosphoribosyl isomerase A; Provisional |
2-239 |
6.00e-42 |
|
phosphoribosyl isomerase A; Provisional
Pssm-ID: 237589 Cd Length: 241 Bit Score: 142.79 E-value: 6.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 2 IIPALDLIDGTVVRLHQGDYGQQRDYGnDPLPRLQAYAAEGAEVLHLVDLTGAKDPAKRQiPLLKTLVAGVDVPVQVGGG 81
Cdd:PRK14024 6 LLPAVDVVDGQAVRLVQGEAGSETSYG-SPLDAALAWQRDGAEWIHLVDLDAAFGRGSNR-ELLAEVVGKLDVKVELSGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 82 VRTEADVAALLDAGVARVVVGSTAVKDPESVKGWFRRFGaDALVLALDVRidaqgNKQVAVSGWQENSG---VTLEELVG 158
Cdd:PRK14024 84 IRDDESLEAALATGCARVNIGTAALENPEWCARVIAEHG-DRVAVGLDVR-----GHTLAARGWTRDGGdlwEVLERLDS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 159 mylpVGLKHVLCTDISRDGTLAGSNVSLYEEVCARY--PQVAfqsSGGIGDLADIAALRG---TGVRGVIVGRALLEGKF 233
Cdd:PRK14024 158 ----AGCSRYVVTDVTKDGTLTGPNLELLREVCARTdaPVVA---SGGVSSLDDLRALAElvpLGVEGAIVGKALYAGAF 230
|
....*.
gi 505385293 234 TVKEAI 239
Cdd:PRK14024 231 TLPEAL 236
|
|
| HisA_HisF |
cd04723 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ... |
1-240 |
2.78e-33 |
|
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: 120.45 E-value: 2.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 1 MIIPALDLIDGTVVRLHQGDYGQQRD------YGNDPLPRLQAYAAEGAEVLHLVDLTGAKDPAkRQIPLLKTLVAGVDV 74
Cdd:cd04723 1 RIIPVIDLKDGVVVHGVGGDRDNYRPitsnlcSTSDPLDVARAYKELGFRGLYIADLDAIMGRG-DNDEAIRELAAAWPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 75 PVQVGGGVRTEADVAALLDAGVARVVVGSTAVKDpESVKGWFRRFGADALVLALDVRiDAQGNKQVAVSGWQEnsgvTLE 154
Cdd:cd04723 80 GLWVDGGIRSLENAQEWLKRGASRVIVGTETLPS-DDDEDRLAALGEQRLVLSLDFR-GGQLLKPTDFIGPEE----LLR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 155 ELVGMylpvgLKHVLCTDISRDGTLAGSNVSLYEEVCARYPqVAFQSSGGIGDLADIAALRGTGVRGVIVGRALLEGKFT 234
Cdd:cd04723 154 RLAKW-----PEELIVLDIDRVGSGQGPDLELLERLAARAD-IPVIAAGGVRSVEDLELLKKLGASGALVASALHDGGLT 227
|
....*.
gi 505385293 235 VKEAIQ 240
Cdd:cd04723 228 LEDVVR 233
|
|
| PRK13587 |
PRK13587 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
4-227 |
6.29e-31 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Provisional
Pssm-ID: 172156 Cd Length: 234 Bit Score: 114.16 E-value: 6.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 4 PALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQAYAA-EGAEVLHLVDLTGAKDPAKRQIPLLKTLVAGVDVPVQVGGGV 82
Cdd:PRK13587 6 PAIDLIGSTSVRLTEGKYDSEEKMSRSAEESIAYYSQfECVNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIEVGGGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 83 RTEADVAALLDAGVARVVVGSTAVKDPESVKGWFRRFgADALVLALDVRIDaqgnkQVAVSGWQENSGVTLEELVGMYLP 162
Cdd:PRK13587 86 RTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTF-PGRIYLSVDAYGE-----DIKVNGWEEDTELNLFSFVRQLSD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505385293 163 VGLKHVLCTDISRDGTLAGSNVSLYEEVcARYPQVAFQSSGGIGDLADIAALRGTGVRGVIVGRA 227
Cdd:PRK13587 160 IPLGGIIYTDIAKDGKMSGPNFELTGQL-VKATTIPVIASGGIRHQQDIQRLASLNVHAAIIGKA 223
|
|
| PRK04128 |
PRK04128 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
2-238 |
8.04e-31 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 167709 Cd Length: 228 Bit Score: 113.71 E-value: 8.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 2 IIPALDLIDGTVVRLHQGDYGQQRDYGnDPLPRLQAYAaEGAEVLHLVDLTGAKDPAKRQIPLLKTLVAGVDVPVQVGGG 81
Cdd:PRK04128 4 IYPAIDLMNGKAVRLYKGRKEEVKVYG-DPVEIALRFS-EYVDKIHVVDLDGAFEGKPKNLDVVKNIIRETGLKVQVGGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 82 VRTEADVAALLDAGVARVVVGSTAVkDPESVKGWFRRFgaDALVLALDVRidaqgNKQVAVSGWQENSGVTLEELVGMyL 161
Cdd:PRK04128 82 LRTYESIKDAYEIGVENVIIGTKAF-DLEFLEKVTSEF--EGITVSLDVK-----GGRIAVKGWLEESSIKVEDAYEM-L 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505385293 162 PVGLKHVLCTDISRDGTLAGsnvslYEEVCARYPQVAFQSSGGIGDLADIAALRGTGVRGVIVGRALLEGKFTVKEA 238
Cdd:PRK04128 153 KNYVNRFIYTSIERDGTLTG-----IEEIERFWGDEEFIYAGGVSSAEDVKKLAEIGFSGVIIGKALYEGRISLEEL 224
|
|
| HisF |
cd04731 |
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ... |
2-240 |
2.80e-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: 112.56 E-value: 2.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 2 IIPALDLIDGTVVRLHQgdYGQQRDYGnDPLPRLQAYAAEGAEVLHLVDLTGAKDPAKRQIPLLKTLVAGVDVPVQVGGG 81
Cdd:cd04731 3 IIPCLDVKDGRVVKGVN--FKNLRDAG-DPVELAKRYNEQGADELVFLDITASSEGRETMLDVVERVAEEVFIPLTVGGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 82 VRTEADVAALLDAGVARVVVGSTAVKDPESVKGWFRRFGADALVLALDVRIDAQGNKQVAVSGWQENSGVTLEELVGMYL 161
Cdd:cd04731 80 IRSLEDARRLLRAGADKVSINSAAVENPELIREIAKRFGSQCVVVSIDAKRRGDGGYEVYTHGGRKPTGLDAVEWAKEVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 162 PVGLKHVLCTDISRDGTLAGSNVSLYEEVCAR--YPQVAfqsSGGIGDLADI-AALRGTGVRGVIVGRALLEGKFTVKEA 238
Cdd:cd04731 160 ELGAGEILLTSMDRDGTKKGYDLELIRAVSSAvnIPVIA---SGGAGKPEHFvEAFEEGGADAALAASIFHFGEYTIAEL 236
|
..
gi 505385293 239 IQ 240
Cdd:cd04731 237 KE 238
|
|
| PRK14114 |
PRK14114 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
1-236 |
3.39e-29 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 172604 Cd Length: 241 Bit Score: 110.10 E-value: 3.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 1 MIIPALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQAYAAEGAEVLHLVDLTGAKDPAKRQIPLLKTLVAGVDvPVQVGG 80
Cdd:PRK14114 2 LVVPAIDLFRGKVARMVKGKKENTIFYEKDPAELVEKLIEEGFTLIHVVDLSKAIENSVENLPVLEKLSEFAE-HIQIGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 81 GVRTEADVAALLDAGVARVVVGSTAVKDPESVKgWFRRFGADAlVLALDVRidaqgNKQVAVSGWQENSGVTLEELVGMY 160
Cdd:PRK14114 81 GIRSLDYAEKLRKLGYRRQIVSSKVLEDPSFLK-FLKEIDVEP-VFSLDTR-----GGKVAFKGWLAEEEIDPVSLLKRL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 161 LPVGLKHVLCTDISRDGTLAGSNVSLYEEVcARYPQVAFQSSGGIG-----DLADIAALRGTG-VRGVIVGRALLEGKFT 234
Cdd:PRK14114 154 KEYGLEEIVHTEIEKDGTLQEHDFSLTRKI-AIEAEVKVFAAGGISsenslKTAQRVHRETNGlLKGVIVGRAFLEGILT 232
|
..
gi 505385293 235 VK 236
Cdd:PRK14114 233 VE 234
|
|
| hisF |
TIGR00735 |
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ... |
2-206 |
1.09e-26 |
|
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273241 Cd Length: 254 Bit Score: 103.60 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 2 IIPALDLIDGTVVRLHQgdYGQQRDYGnDPLPRLQAYAAEGAEVLHLVDLTGAKDPAKRQIPLLKTLVAGVDVPVQVGGG 81
Cdd:TIGR00735 6 IIPCLDVRDGRVVKGVQ--FLNLRDAG-DPVELAQRYDEEGADELVFLDITASSEGRTTMIDVVERTAETVFIPLTVGGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 82 VRTEADVAALLDAGVARVVVGSTAVKDPESVKGWFRRFGADALVLALDVRIDAQGNK---QVAVSGWQENSGVTLEELVG 158
Cdd:TIGR00735 83 IKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFGSQCIVVAIDAKRVYVNSYcwyEVYIYGGRESTGLDAVEWAK 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505385293 159 MYLPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYPqVAFQSSGGIG 206
Cdd:TIGR00735 163 EVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEAVK-IPVIASGGAG 209
|
|
| HisF |
COG0107 |
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ... |
2-240 |
3.28e-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: 99.33 E-value: 3.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 2 IIPALDLIDGTVVRlhqgdyGQQ----RDYGnDPLPRLQAYAAEGAEVLHLVDLTGAKDpaKRQIPL--LKTLVAGVDVP 75
Cdd:COG0107 5 IIPCLDVKDGRVVK------GVNfvnlRDAG-DPVELAKRYNEQGADELVFLDITASSE--GRKTMLdvVRRVAEEVFIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 76 VQVGGGVRTEADVAALLDAGVARVVVGSTAVKDPESVKGWFRRFGADALVLALDVRIDAQGNKQVAVSGWQENSGVTLEE 155
Cdd:COG0107 76 LTVGGGIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAIDAKRVPDGGWEVYTHGGRKPTGLDAVE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 156 LVgmylpvglKHV--------LCTDISRDGTLAGSNVSLYEEVCA--RYPQVAfqsSGGIGDLADIA-ALRGTGVRGVIV 224
Cdd:COG0107 156 WA--------KEAeelgageiLLTSMDRDGTKDGYDLELTRAVSEavSIPVIA---SGGAGTLEHFVeVFTEGGADAALA 224
|
250
....*....|....*.
gi 505385293 225 GRALLEGKFTVKEAIQ 240
Cdd:COG0107 225 ASIFHFGEITIAELKA 240
|
|
| PRK13586 |
PRK13586 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
2-232 |
1.49e-18 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 237439 Cd Length: 232 Bit Score: 81.32 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 2 IIPALDLIDGTVVRLHQGDYGQQRDYGNdPLPRLQAYAAEGAEVLHLVDLTGAKDPAKRQIPLLKTLVAGVDVpVQVGGG 81
Cdd:PRK13586 4 IIPSIDISLGKAVKRIRGVKGTGLILGN-PIEIASKLYNEGYTRIHVVDLDAAEGVGNNEMYIKEISKIGFDW-IQVGGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 82 VRTEADVAALLDAGVARVVVGSTAVKDPESVKGWFRRFGADALVLAldvrIDAQGNKQVAVSGWQENSgVTLEELVGMYL 161
Cdd:PRK13586 82 IRDIEKAKRLLSLDVNALVFSTIVFTNFNLFHDIVREIGSNRVLVS----IDYDNTKRVLIRGWKEKS-MEVIDGIKKVN 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505385293 162 PVGLKHVLCTDISRDGTLAG--SNVSLYeevcARYPQVAFQSSGGIGDLADIAALRGTGVRGVIVGRALLEGK 232
Cdd:PRK13586 157 ELELLGIIFTYISNEGTTKGidYNVKDY----ARLIRGLKEYAGGVSSDADLEYLKNVGFDYIIVGMAFYLGK 225
|
|
| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
64-116 |
9.01e-06 |
|
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: 45.26 E-value: 9.01e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 505385293 64 LLKTLVAGVDVPVQVGGGVRTEADVAALLDAGVARVVVGsTAVKDPESVKGWF 116
Cdd:cd04729 168 LLKELRKALGIPVIAEGRINSPEQAAKALELGADAVVVG-SAITRPEHITGWF 219
|
|
| PRK01130 |
PRK01130 |
putative N-acetylmannosamine-6-phosphate 2-epimerase; |
64-116 |
2.54e-05 |
|
putative N-acetylmannosamine-6-phosphate 2-epimerase;
Pssm-ID: 234907 Cd Length: 221 Bit Score: 43.98 E-value: 2.54e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 505385293 64 LLKTLVAGVDVPVQVGGGVRTEADVAALLDAGVARVVVGsTAVKDPESVKGWF 116
Cdd:PRK01130 164 LLKELLKAVGCPVIAEGRINTPEQAKKALELGAHAVVVG-GAITRPEEITKWF 215
|
|
| PEP_mutase |
pfam13714 |
Phosphoenolpyruvate phosphomutase; This domain includes the enzyme Phosphoenolpyruvate ... |
34-103 |
1.01e-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: 42.19 E-value: 1.01e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 34 RLQAYAAEGAEVLHLvdlTGAKDPakrqiPLLKTLVAGVDVPVQVGGGVRTeADVAALLDAGVARVVVGS 103
Cdd:pfam13714 163 RARAYAEAGADGIFV---PGLLDP-----ADIAALVAAVPGPVNVLAGPGT-LSVAELAALGVARISYGN 223
|
|
| PLN02446 |
PLN02446 |
(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
77-228 |
2.68e-03 |
|
(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase
Pssm-ID: 215245 Cd Length: 262 Bit Score: 38.15 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 77 QVGGGVrTEADVAALLDAGVARVVVGSTAVK----DPESVKGWFRRFGADALVLALDVRiDAQGNKQVAVSGWQENSGVT 152
Cdd:PLN02446 87 QVGGGV-NSENAMSYLDAGASHVIVTSYVFRdgqiDLERLKDLVRLVGKQRLVLDLSCR-KKDGRYYVVTDRWQKFSDLA 164
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505385293 153 LEELVGMYLPVGLKHVLCTDISRDGTLAGSNVSLYeEVCARYPQVAFQSSGGIGDLADIAALR--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 ... |
37-103 |
3.27e-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: 37.57 E-value: 3.27e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385293 37 AYAAEGAEVLHLVD---LTGAKDPAKRQIPLLKTLVAGVDVPVQVGGGVRTEADVAALLDAGVARVVVGS 103
Cdd:cd04722 131 AAEEAGVDEVGLGNgggGGGGRDAVPIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| ICL_PEPM |
cd00377 |
Members of the ICL/PEPM enzyme family catalyze either P-C or C-C bond formation/cleavage. ... |
34-105 |
7.72e-03 |
|
Members of the ICL/PEPM enzyme family catalyze either P-C or C-C bond formation/cleavage. Known members are phosphoenolpyruvate mutase (PEPM), phosphonopyruvate hydrolase (PPH), carboxyPEP mutase (CPEP mutase), oxaloacetate hydrolase (OAH), isocitrate lyase (ICL), and 2-methylisocitrate lyase (MICL). Isocitrate lyase (ICL) catalyzes the conversion of isocitrate to succinate and glyoxylate, the first committed step in the glyoxylate pathway. This carbon-conserving pathway is present in most prokaryotes, lower eukaryotes and plants, but has not been observed in vertebrates. PEP mutase (PEPM) turns phosphoenolpyruvate (PEP) into phosphonopyruvate (P-pyr), an important intermediate in the formation of organophosphonates, which function as antibiotics or play a role in pathogenesis or signaling. P-pyr can be hydrolyzed by phosphonopyruvate hydrolase (PPH) to from pyruvate and phosphate. Oxaloacetate acetylhydrolase (OAH) catalyzes the hydrolytic cleavage of oxaloacetate to form acetate and oxalate, an important pathway to produce oxalate in filamentous fungi. 2-methylisocitrate lyase (MICL) cleaves 2-methylisocitrate to pyruvate and succinate, part of the methylcitrate cycle for the alpha-oxidation of propionate.
Pssm-ID: 119340 [Multi-domain] Cd Length: 243 Bit Score: 36.70 E-value: 7.72e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505385293 34 RLQAYAAEGAEVLHLvdltgakdPAKRQIPLLKTLVAGVDVPV---QVGGGVRTeaDVAALLDAGVARVVVGSTA 105
Cdd:cd00377 165 RAKAYAEAGADGIFV--------EGLKDPEEIRAFAEAPDVPLnvnMTPGGNLL--TVAELAELGVRRVSYGLAL 229
|
|
| |
