|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00748 |
PRK00748 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
1-238 |
3.24e-123 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated
Pssm-ID: 179108 Cd Length: 233 Bit Score: 349.36 E-value: 3.24e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 1 MIIPALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQSYAAQGAEVLHLVDLTGAKDPAKRQIPLLKTLVAGVNVPVQVGG 80
Cdd:PRK00748 2 IIIPAIDLKDGKCVRLYQGDYDQATVYSDDPVAQAKAWEDQGAKWLHLVDLDGAKAGKPVNLELIEAIVKAVDIPVQVGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 81 GVRTEEDVAALLDAGVARVVVGSTAVKSPEVVKGWFKRFgPQHLVLALDVRidaqgSKQVAVSGWQENSGVTLEELVESY 160
Cdd:PRK00748 82 GIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKF-PGKIVVGLDAR-----DGKVATDGWLETSGVTAEDLAKRF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515201175 161 QSVGLQHVLCTDISRDGTLAGSNVSLYEEVCARYPqVAFQSSGGIGDLHDIAALRGTG-VRGVIVGRALLEGKFNVTEA 238
Cdd:PRK00748 156 EDAGVKAIIYTDISRDGTLSGPNVEATRELAAAVP-IPVIASGGVSSLDDIKALKGLGaVEGVIVGRALYEGKFDLAEA 233
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
1-243 |
1.29e-111 |
|
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: 320.06 E-value: 1.29e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 1 MIIPALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQSYAAQGAEVLHLVDLTGAKDPAKRQIPLLKTLVAGVNVPVQVGG 80
Cdd:COG0106 1 IIIPAIDLKDGKCVRLVQGDYDQETVYSDDPVEVAKRWEDAGAEWLHLVDLDGAFAGKPVNLELIEEIAKATGLPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 81 GVRTEEDVAALLDAGVARVVVGSTAVKSPEVVKGWFKRFgPQHLVLALDVRidaqgSKQVAVSGWQENSGVTLEELVESY 160
Cdd:COG0106 81 GIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEF-PERIVVGLDAR-----DGKVATDGWQETSGVDLEELAKRF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 161 QSVGLQHVLCTDISRDGTLAGSNVSLYEEVCARYPqVAFQSSGGIGDLHDIAALRGTGVRGVIVGRALLEGKFNVTEAIQ 240
Cdd:COG0106 155 EDAGVAAILYTDISRDGTLQGPNLELYRELAAATG-IPVIASGGVSSLDDLRALKELGVEGAIVGKALYEGKIDLEEALA 233
|
...
gi 515201175 241 CWQ 243
Cdd:COG0106 234 LAR 236
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
1-240 |
1.53e-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: 1.53e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 1 MIIPALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQSYAAQGAEVLHLVDLTGAKDPAKRQIPLLKTLVAGVNVPVQVGG 80
Cdd:cd04732 1 IIIPAIDLKDGKCVRLYQGDYDKKTVYSDDPVEVAKKWEEAGAKWLHVVDLDGAKGGEPVNLELIEEIVKAVGIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 81 GVRTEEDVAALLDAGVARVVVGSTAVKSPEVVKGWFKRFGPQHLVLALDVRIDaqgskQVAVSGWQENSGVTLEELVESY 160
Cdd:cd04732 81 GIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGGERIVVGLDAKDG-----KVATKGWLETSEVSLEELAKRF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 161 QSVGLQHVLCTDISRDGTLAGSNVSLYEEVCARYpQVAFQSSGGIGDLHDIAALRGTGVRGVIVGRALLEGKFNVTEAIQ 240
Cdd:cd04732 156 EELGVKAIIYTDISRDGTLSGPNFELYKELAAAT-GIPVIASGGVSSLDDIKALKELGVAGVIVGKALYEGKITLEEALA 234
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
2-237 |
3.92e-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: 288.33 E-value: 3.92e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 2 IIPALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQSYAAQGAEVLHLVDLTGAKDPAKRQIPLLKTLVAGVNVPVQVGGG 81
Cdd:TIGR00007 1 IIPAIDIKDGKCVRLYQGDYDKETVYGDDPVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQVGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 82 VRTEEDVAALLDAGVARVVVGSTAVKSPEVVKGWFKRFGPQHLVLALDVRIDAqgskqVAVSGWQENSGVTLEELVESYQ 161
Cdd:TIGR00007 81 IRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYGPERIVVSLDARGGE-----VAVKGWLEKSEVSLEELAKRLE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515201175 162 SVGLQHVLCTDISRDGTLAGSNVSLYEEVCARyPQVAFQSSGGIGDLHDIAALRGTGVRGVIVGRALLEGKFNVTE 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 |
2.28e-97 |
|
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: 283.60 E-value: 2.28e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 1 MIIPALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQSYAAQGAEVLHLVDLTGAKDPAKRQIPLLKTLVAGVNVPVQVGG 80
Cdd:pfam00977 1 RIIPAIDLKDGRVVRLVKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 81 GVRTEEDVAALLDAGVARVVVGSTAVKSPEVVKGWFKRFGPQHLVLALDVRIDaqgskQVAVSGWQENSGVTLEELVESY 160
Cdd:pfam00977 81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAIDARRG-----KVAINGWREDTGIDAVEWAKEL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515201175 161 QSVGLQHVLCTDISRDGTLAGSNVSLYEEVCARYpQVAFQSSGGIGDLHDIAALRGTGVRGVIVGRALLEGKFN 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 |
3.24e-123 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated
Pssm-ID: 179108 Cd Length: 233 Bit Score: 349.36 E-value: 3.24e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 1 MIIPALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQSYAAQGAEVLHLVDLTGAKDPAKRQIPLLKTLVAGVNVPVQVGG 80
Cdd:PRK00748 2 IIIPAIDLKDGKCVRLYQGDYDQATVYSDDPVAQAKAWEDQGAKWLHLVDLDGAKAGKPVNLELIEAIVKAVDIPVQVGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 81 GVRTEEDVAALLDAGVARVVVGSTAVKSPEVVKGWFKRFgPQHLVLALDVRidaqgSKQVAVSGWQENSGVTLEELVESY 160
Cdd:PRK00748 82 GIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKF-PGKIVVGLDAR-----DGKVATDGWLETSGVTAEDLAKRF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515201175 161 QSVGLQHVLCTDISRDGTLAGSNVSLYEEVCARYPqVAFQSSGGIGDLHDIAALRGTG-VRGVIVGRALLEGKFNVTEA 238
Cdd:PRK00748 156 EDAGVKAIIYTDISRDGTLSGPNVEATRELAAAVP-IPVIASGGVSSLDDIKALKGLGaVEGVIVGRALYEGKFDLAEA 233
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
1-243 |
1.29e-111 |
|
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: 320.06 E-value: 1.29e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 1 MIIPALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQSYAAQGAEVLHLVDLTGAKDPAKRQIPLLKTLVAGVNVPVQVGG 80
Cdd:COG0106 1 IIIPAIDLKDGKCVRLVQGDYDQETVYSDDPVEVAKRWEDAGAEWLHLVDLDGAFAGKPVNLELIEEIAKATGLPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 81 GVRTEEDVAALLDAGVARVVVGSTAVKSPEVVKGWFKRFgPQHLVLALDVRidaqgSKQVAVSGWQENSGVTLEELVESY 160
Cdd:COG0106 81 GIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEF-PERIVVGLDAR-----DGKVATDGWQETSGVDLEELAKRF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 161 QSVGLQHVLCTDISRDGTLAGSNVSLYEEVCARYPqVAFQSSGGIGDLHDIAALRGTGVRGVIVGRALLEGKFNVTEAIQ 240
Cdd:COG0106 155 EDAGVAAILYTDISRDGTLQGPNLELYRELAAATG-IPVIASGGVSSLDDLRALKELGVEGAIVGKALYEGKIDLEEALA 233
|
...
gi 515201175 241 CWQ 243
Cdd:COG0106 234 LAR 236
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
1-240 |
1.53e-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: 1.53e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 1 MIIPALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQSYAAQGAEVLHLVDLTGAKDPAKRQIPLLKTLVAGVNVPVQVGG 80
Cdd:cd04732 1 IIIPAIDLKDGKCVRLYQGDYDKKTVYSDDPVEVAKKWEEAGAKWLHVVDLDGAKGGEPVNLELIEEIVKAVGIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 81 GVRTEEDVAALLDAGVARVVVGSTAVKSPEVVKGWFKRFGPQHLVLALDVRIDaqgskQVAVSGWQENSGVTLEELVESY 160
Cdd:cd04732 81 GIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGGERIVVGLDAKDG-----KVATKGWLETSEVSLEELAKRF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 161 QSVGLQHVLCTDISRDGTLAGSNVSLYEEVCARYpQVAFQSSGGIGDLHDIAALRGTGVRGVIVGRALLEGKFNVTEAIQ 240
Cdd:cd04732 156 EELGVKAIIYTDISRDGTLSGPNFELYKELAAAT-GIPVIASGGVSSLDDIKALKELGVAGVIVGKALYEGKITLEEALA 234
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
2-237 |
3.92e-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: 288.33 E-value: 3.92e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 2 IIPALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQSYAAQGAEVLHLVDLTGAKDPAKRQIPLLKTLVAGVNVPVQVGGG 81
Cdd:TIGR00007 1 IIPAIDIKDGKCVRLYQGDYDKETVYGDDPVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQVGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 82 VRTEEDVAALLDAGVARVVVGSTAVKSPEVVKGWFKRFGPQHLVLALDVRIDAqgskqVAVSGWQENSGVTLEELVESYQ 161
Cdd:TIGR00007 81 IRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYGPERIVVSLDARGGE-----VAVKGWLEKSEVSLEELAKRLE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515201175 162 SVGLQHVLCTDISRDGTLAGSNVSLYEEVCARyPQVAFQSSGGIGDLHDIAALRGTGVRGVIVGRALLEGKFNVTE 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 |
2.28e-97 |
|
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: 283.60 E-value: 2.28e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 1 MIIPALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQSYAAQGAEVLHLVDLTGAKDPAKRQIPLLKTLVAGVNVPVQVGG 80
Cdd:pfam00977 1 RIIPAIDLKDGRVVRLVKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 81 GVRTEEDVAALLDAGVARVVVGSTAVKSPEVVKGWFKRFGPQHLVLALDVRIDaqgskQVAVSGWQENSGVTLEELVESY 160
Cdd:pfam00977 81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAIDARRG-----KVAINGWREDTGIDAVEWAKEL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515201175 161 QSVGLQHVLCTDISRDGTLAGSNVSLYEEVCARYpQVAFQSSGGIGDLHDIAALRGTGVRGVIVGRALLEGKFN 234
Cdd:pfam00977 156 EELGAGEILLTDIDRDGTLSGPDLELTRELAEAV-NIPVIASGGVGSLEDLKELFTEGVDGVIAGSALYEGEIT 228
|
|
| PRK13585 |
PRK13585 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ... |
2-239 |
5.29e-56 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase;
Pssm-ID: 184165 Cd Length: 241 Bit Score: 178.95 E-value: 5.29e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 2 IIPALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQSYAAQGAEVLHLVDLTGAKDPAKRQIPLLKTLVAGVNVPVQVGGG 81
Cdd:PRK13585 5 VIPAVDMKGGKCVQLVQGEPGTETVSYGDPVEVAKRWVDAGAETLHLVDLDGAFEGERKNAEAIEKIIEAVGVPVQLGGG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 82 VRTEEDVAALLDAGVARVVVGSTAVKSPEVVKGWFKRFGPQHLVLALDVRidaqgSKQVAVSGWQENSGVTLEELVESYQ 161
Cdd:PRK13585 85 IRSAEDAASLLDLGVDRVILGTAAVENPEIVRELSEEFGSERVMVSLDAK-----DGEVVIKGWTEKTGYTPVEAAKRFE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 162 SVGLQHVLCTDISRDGTLAGSNVSLYEEVCARY--PQVAfqsSGGIGDLHDIAALRGTGVRGVIVGRALLEGKFNVTEAI 239
Cdd:PRK13585 160 ELGAGSILFTNVDVEGLLEGVNTEPVKELVDSVdiPVIA---SGGVTTLDDLRALKEAGAAGVVVGSALYKGKFTLEEAI 236
|
|
| PRK14024 |
PRK14024 |
phosphoribosyl isomerase A; Provisional |
2-239 |
5.05e-42 |
|
phosphoribosyl isomerase A; Provisional
Pssm-ID: 237589 Cd Length: 241 Bit Score: 143.18 E-value: 5.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 2 IIPALDLIDGTVVRLHQGDYGQQRDYGnDPLPRLQSYAAQGAEVLHLVDLTGAKDPAKRQiPLLKTLVAGVNVPVQVGGG 81
Cdd:PRK14024 6 LLPAVDVVDGQAVRLVQGEAGSETSYG-SPLDAALAWQRDGAEWIHLVDLDAAFGRGSNR-ELLAEVVGKLDVKVELSGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 82 VRTEEDVAALLDAGVARVVVGSTAVKSPEVVKGWFKRFGPQHLVlALDVRidaqgSKQVAVSGWQENSGvTLEELVESYQ 161
Cdd:PRK14024 84 IRDDESLEAALATGCARVNIGTAALENPEWCARVIAEHGDRVAV-GLDVR-----GHTLAARGWTRDGG-DLWEVLERLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 162 SVGLQHVLCTDISRDGTLAGSNVSLYEEVCARY--PQVAfqsSGGIGDLHDIAALRG---TGVRGVIVGRALLEGKFNVT 236
Cdd:PRK14024 157 SAGCSRYVVTDVTKDGTLTGPNLELLREVCARTdaPVVA---SGGVSSLDDLRALAElvpLGVEGAIVGKALYAGAFTLP 233
|
...
gi 515201175 237 EAI 239
Cdd:PRK14024 234 EAL 236
|
|
| PRK13587 |
PRK13587 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
4-227 |
2.47e-33 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Provisional
Pssm-ID: 172156 Cd Length: 234 Bit Score: 120.32 E-value: 2.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 4 PALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQSYAA-QGAEVLHLVDLTGAKDPAKRQIPLLKTLVAGVNVPVQVGGGV 82
Cdd:PRK13587 6 PAIDLIGSTSVRLTEGKYDSEEKMSRSAEESIAYYSQfECVNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIEVGGGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 83 RTEEDVAALLDAGVARVVVGSTAVKSPEVVKGWFKRFgPQHLVLALDVRIDaqgskQVAVSGWQENSGVTLEELVESYQS 162
Cdd:PRK13587 86 RTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTF-PGRIYLSVDAYGE-----DIKVNGWEEDTELNLFSFVRQLSD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515201175 163 VGLQHVLCTDISRDGTLAGSNVSLYEEVcARYPQVAFQSSGGIGDLHDIAALRGTGVRGVIVGRA 227
Cdd:PRK13587 160 IPLGGIIYTDIAKDGKMSGPNFELTGQL-VKATTIPVIASGGIRHQQDIQRLASLNVHAAIIGKA 223
|
|
| HisA_HisF |
cd04723 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ... |
1-240 |
1.17e-32 |
|
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: 118.53 E-value: 1.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 1 MIIPALDLIDGTVVRLHQGDYGQQRD------YGNDPLPRLQSYAAQGAEVLHLVDLTGAKDPAkRQIPLLKTLVAGVNV 74
Cdd:cd04723 1 RIIPVIDLKDGVVVHGVGGDRDNYRPitsnlcSTSDPLDVARAYKELGFRGLYIADLDAIMGRG-DNDEAIRELAAAWPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 75 PVQVGGGVRTEEDVAALLDAGVARVVVGSTAVKSpEVVKGWFKRFGPQHLVLALDVRiDAQGSKQVAVSGWQEnsgvtLE 154
Cdd:cd04723 80 GLWVDGGIRSLENAQEWLKRGASRVIVGTETLPS-DDDEDRLAALGEQRLVLSLDFR-GGQLLKPTDFIGPEE-----LL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 155 ELVESYqsvgLQHVLCTDISRDGTLAGSNVSLYEEVCARYPqVAFQSSGGIGDLHDIAALRGTGVRGVIVGRALLEGKFN 234
Cdd:cd04723 153 RRLAKW----PEELIVLDIDRVGSGQGPDLELLERLAARAD-IPVIAAGGVRSVEDLELLKKLGASGALVASALHDGGLT 227
|
....*.
gi 515201175 235 VTEAIQ 240
Cdd:cd04723 228 LEDVVR 233
|
|
| HisF |
cd04731 |
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ... |
2-240 |
1.29e-32 |
|
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: 118.72 E-value: 1.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 2 IIPALDLIDGTVVRLHQgdYGQQRDYGnDPLPRLQSYAAQGAEVLHLVDLTGAKDPAKRQIPLLKTLVAGVNVPVQVGGG 81
Cdd:cd04731 3 IIPCLDVKDGRVVKGVN--FKNLRDAG-DPVELAKRYNEQGADELVFLDITASSEGRETMLDVVERVAEEVFIPLTVGGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 82 VRTEEDVAALLDAGVARVVVGSTAVKSPEVVKGWFKRFGPQHLVLALDVRIDAQGSKQVAVSGWQENSGVTLEELVESYQ 161
Cdd:cd04731 80 IRSLEDARRLLRAGADKVSINSAAVENPELIREIAKRFGSQCVVVSIDAKRRGDGGYEVYTHGGRKPTGLDAVEWAKEVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 162 SVGLQHVLCTDISRDGTLAGSNVSLYEEVCAR--YPQVAfqsSGGIGDLHDI-AALRGTGVRGVIVGRALLEGKFNVTEA 238
Cdd:cd04731 160 ELGAGEILLTSMDRDGTKKGYDLELIRAVSSAvnIPVIA---SGGAGKPEHFvEAFEEGGADAALAASIFHFGEYTIAEL 236
|
..
gi 515201175 239 IQ 240
Cdd:cd04731 237 KE 238
|
|
| PRK04128 |
PRK04128 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
2-238 |
8.01e-32 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 167709 Cd Length: 228 Bit Score: 116.41 E-value: 8.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 2 IIPALDLIDGTVVRLHQGDYGQQRDYGnDPLprlqSYAAQGAEV---LHLVDLTGAKDPAKRQIPLLKTLVAGVNVPVQV 78
Cdd:PRK04128 4 IYPAIDLMNGKAVRLYKGRKEEVKVYG-DPV----EIALRFSEYvdkIHVVDLDGAFEGKPKNLDVVKNIIRETGLKVQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 79 GGGVRTEEDVAALLDAGVARVVVGSTAVKSpEVVKGWFKRFGpqhlvlALDVRIDAQGSKqVAVSGWQENSGVTLEELVE 158
Cdd:PRK04128 79 GGGLRTYESIKDAYEIGVENVIIGTKAFDL-EFLEKVTSEFE------GITVSLDVKGGR-IAVKGWLEESSIKVEDAYE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 159 SYQSVgLQHVLCTDISRDGTLAGsnvslYEEVCARYPQVAFQSSGGIGDLHDIAALRGTGVRGVIVGRALLEGKFNVTEA 238
Cdd:PRK04128 151 MLKNY-VNRFIYTSIERDGTLTG-----IEEIERFWGDEEFIYAGGVSSAEDVKKLAEIGFSGVIIGKALYEGRISLEEL 224
|
|
| hisF |
TIGR00735 |
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ... |
2-206 |
6.72e-29 |
|
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273241 Cd Length: 254 Bit Score: 109.38 E-value: 6.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 2 IIPALDLIDGTVVRLHQgdYGQQRDYGnDPLPRLQSYAAQGAEVLHLVDLTGAKDPAKRQIPLLKTLVAGVNVPVQVGGG 81
Cdd:TIGR00735 6 IIPCLDVRDGRVVKGVQ--FLNLRDAG-DPVELAQRYDEEGADELVFLDITASSEGRTTMIDVVERTAETVFIPLTVGGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 82 VRTEEDVAALLDAGVARVVVGSTAVKSPEVVKGWFKRFGPQHLVLALDVRIDAQGSK---QVAVSGWQENSGVTLEELVE 158
Cdd:TIGR00735 83 IKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFGSQCIVVAIDAKRVYVNSYcwyEVYIYGGRESTGLDAVEWAK 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515201175 159 SYQSVGLQHVLCTDISRDGTLAGSNVSLYEEVCARYPqVAFQSSGGIG 206
Cdd:TIGR00735 163 EVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEAVK-IPVIASGGAG 209
|
|
| PRK14114 |
PRK14114 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
1-235 |
4.80e-28 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 172604 Cd Length: 241 Bit Score: 107.02 E-value: 4.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 1 MIIPALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQSYAAQGAEVLHLVDLTGAKDPAKRQIPLLKTLVAGVNvPVQVGG 80
Cdd:PRK14114 2 LVVPAIDLFRGKVARMVKGKKENTIFYEKDPAELVEKLIEEGFTLIHVVDLSKAIENSVENLPVLEKLSEFAE-HIQIGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 81 GVRTEEDVAALLDAGVARVVVGSTAVKSPEVVKgWFKRFGPQHlVLALDVRidaqgSKQVAVSGWQENSGVTLEELVESY 160
Cdd:PRK14114 81 GIRSLDYAEKLRKLGYRRQIVSSKVLEDPSFLK-FLKEIDVEP-VFSLDTR-----GGKVAFKGWLAEEEIDPVSLLKRL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 161 QSVGLQHVLCTDISRDGTLAGSNVSLYEEVcARYPQVAFQSSGGIGDLHDIAAL-----RGTG-VRGVIVGRALLEGKFN 234
Cdd:PRK14114 154 KEYGLEEIVHTEIEKDGTLQEHDFSLTRKI-AIEAEVKVFAAGGISSENSLKTAqrvhrETNGlLKGVIVGRAFLEGILT 232
|
.
gi 515201175 235 V 235
Cdd:PRK14114 233 V 233
|
|
| HisF |
COG0107 |
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ... |
2-222 |
1.07e-26 |
|
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: 103.56 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 2 IIPALDLIDGTVVRlhqgdyGQQ----RDYGnDPLPRLQSYAAQGAEVLHLVDLTGAKDpaKRQIPL--LKTLVAGVNVP 75
Cdd:COG0107 5 IIPCLDVKDGRVVK------GVNfvnlRDAG-DPVELAKRYNEQGADELVFLDITASSE--GRKTMLdvVRRVAEEVFIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 76 VQVGGGVRTEEDVAALLDAGVARVVVGSTAVKSPEVVKGWFKRFGPQHLVLALDVRIDAQGSKQVAVSGWQENSGVTLEE 155
Cdd:COG0107 76 LTVGGGIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAIDAKRVPDGGWEVYTHGGRKPTGLDAVE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 156 LVESYQSVGLQHVLCTDISRDGTLAGSNVSLYEEVCA--RYPQVAfqsSGGIGDLHDIA-ALRGTGVRGV 222
Cdd:COG0107 156 WAKEAEELGAGEILLTSMDRDGTKDGYDLELTRAVSEavSIPVIA---SGGAGTLEHFVeVFTEGGADAA 222
|
|
| PRK13586 |
PRK13586 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
2-232 |
1.23e-16 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 237439 Cd Length: 232 Bit Score: 76.32 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 2 IIPALDLIDGTVVRLHQGDYGQQRDYGNdPLPRLQSYAAQGAEVLHLVDLTGAKDPAKRQIPLLKTLVAGVNVpVQVGGG 81
Cdd:PRK13586 4 IIPSIDISLGKAVKRIRGVKGTGLILGN-PIEIASKLYNEGYTRIHVVDLDAAEGVGNNEMYIKEISKIGFDW-IQVGGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 82 VRTEEDVAALLDAGVARVVVGSTAVKSPEVVKGWFKRFGPQHLVLAldvrIDAQGSKQVAVSGWQENSgVTLEELVESYQ 161
Cdd:PRK13586 82 IRDIEKAKRLLSLDVNALVFSTIVFTNFNLFHDIVREIGSNRVLVS----IDYDNTKRVLIRGWKEKS-MEVIDGIKKVN 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515201175 162 SVGLQHVLCTDISRDGTLAG--SNVSLYeevcARYPQVAFQSSGGIGDLHDIAALRGTGVRGVIVGRALLEGK 232
Cdd:PRK13586 157 ELELLGIIFTYISNEGTTKGidYNVKDY----ARLIRGLKEYAGGVSSDADLEYLKNVGFDYIIVGMAFYLGK 225
|
|
| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
64-116 |
2.86e-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: 43.72 E-value: 2.86e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 515201175 64 LLKTLVAGVNVPVQVGGGVRTEEDVAALLDAGVARVVVGsTAVKSPEVVKGWF 116
Cdd:cd04729 168 LLKELRKALGIPVIAEGRINSPEQAAKALELGADAVVVG-SAITRPEHITGWF 219
|
|
| PRK01130 |
PRK01130 |
putative N-acetylmannosamine-6-phosphate 2-epimerase; |
64-116 |
3.27e-05 |
|
putative N-acetylmannosamine-6-phosphate 2-epimerase;
Pssm-ID: 234907 Cd Length: 221 Bit Score: 43.60 E-value: 3.27e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 515201175 64 LLKTLVAGVNVPVQVGGGVRTEEDVAALLDAGVARVVVGsTAVKSPEVVKGWF 116
Cdd:PRK01130 164 LLKELLKAVGCPVIAEGRINTPEQAKKALELGAHAVVVG-GAITRPEEITKWF 215
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
38-103 |
5.73e-04 |
|
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: 39.88 E-value: 5.73e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515201175 38 YAAQGAEVLHLVD---LTGAKDPAKRQIPLLKTLVAGVNVPVQVGGGVRTEEDVAALLDAGVARVVVGS 103
Cdd:cd04722 132 AEEAGVDEVGLGNgggGGGGRDAVPIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| PEP_mutase |
pfam13714 |
Phosphoenolpyruvate phosphomutase; This domain includes the enzyme Phosphoenolpyruvate ... |
34-103 |
5.83e-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: 39.88 E-value: 5.83e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 34 RLQSYAAQGAEVLHLvdlTGAKDPakrqiPLLKTLVAGVNVPVQVGGGVRTEeDVAALLDAGVARVVVGS 103
Cdd:pfam13714 163 RARAYAEAGADGIFV---PGLLDP-----ADIAALVAAVPGPVNVLAGPGTL-SVAELAALGVARISYGN 223
|
|
| KGPDC_HPS |
cd04726 |
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ... |
39-112 |
9.44e-04 |
|
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate synthase (HPS). KGPDC catalyzes the formation of L-xylulose 5-phosphate and carbon dioxide from 3-keto-L-gulonate 6-phosphate as part of the anaerobic pathway for L-ascorbate utilization in some eubacteria. HPS catalyzes the formation of D-arabino-3-hexulose-6-phosphate from D-ribulose 5-phosphate and formaldehyde in microorganisms that can use formaldehyde as a carbon source. Both catalyze reactions that involve the Mg2+-assisted formation and stabilization of 1,2-enediolate reaction intermediates.
Pssm-ID: 240077 [Multi-domain] Cd Length: 202 Bit Score: 39.10 E-value: 9.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201175 39 AAQGAEVLHLVDLTGAKDPAKRQ--------------------------IPLLKTLVAGVNVPVQVGGGVrTEEDVAALL 92
Cdd:cd04726 98 AAKKYGKEVQVDLIGVEDPEKRAkllklgvdivilhrgidaqaaggwwpEDDLKKVKKLLGVKVAVAGGI-TPDTLPEFK 176
|
90 100
....*....|....*....|
gi 515201175 93 DAGVARVVVGSTAVKSPEVV 112
Cdd:cd04726 177 KAGADIVIVGRAITGAADPA 196
|
|
| PRK04302 |
PRK04302 |
triosephosphate isomerase; Provisional |
73-113 |
2.46e-03 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 235274 Cd Length: 223 Bit Score: 37.92 E-value: 2.46e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 515201175 73 NVPVQVGGGVRTEEDVAALLDAGVARVVVGSTAVKSPEVVK 113
Cdd:PRK04302 173 DVKVLCGAGISTGEDVKAALELGADGVLLASGVVKAKDPEA 213
|
|
| PcrB |
COG1646 |
Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism]; |
73-113 |
5.24e-03 |
|
Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism];
Pssm-ID: 441252 Cd Length: 241 Bit Score: 37.06 E-value: 5.24e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 515201175 73 NVPVQVGGGVRTEEDVAALLDAGVARVVVGsTAV-KSPEVVK 113
Cdd:COG1646 196 DTPLIYGGGIRSPEKAREMAEAGADTIVVG-NAIeEDPDLAL 236
|
|
| TMP-TENI |
pfam02581 |
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ... |
55-103 |
9.19e-03 |
|
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl)thiazole phosphate to yield thiamine phosphate. This Pfam family also includes the regulatory protein TENI, a protein from Bacillus subtilis that regulates the production of several extracellular enzymes by reducing alkaline protease production. While TenI shows high sequence similarity with thiamin phosphate synthase, the purified protein has no thiamin phosphate synthase activity. Instead, it is a thiazole tautomerase.
Pssm-ID: 426849 [Multi-domain] Cd Length: 180 Bit Score: 35.99 E-value: 9.19e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 515201175 55 KDPAKRQIPLLKTLVAGVNVPVQVGGGVrTEEDVAALLDAGVARVVVGS 103
Cdd:pfam02581 131 PDAPPLGLEGLKAIAEAVEIPVVAIGGI-TPENVPEVIEAGADGVAVVS 178
|
|
| Aldolase_Class_I |
cd00945 |
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ... |
69-102 |
9.23e-03 |
|
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which stabilizes a reaction intermediates via Schiff base formation, and have TIM beta/alpha barrel fold. The members of this family include 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-4-hydroxyglutarate (KHG) aldolases, transaldolase, dihydrodipicolinate synthase sub-family, Type I 3-dehydroquinate dehydratase, DeoC and DhnA proteins, and metal-independent fructose-1,6-bisphosphate aldolase. Although structurally similar, the class II aldolases use a different mechanism and are believed to have an independent evolutionary origin.
Pssm-ID: 188634 [Multi-domain] Cd Length: 201 Bit Score: 36.15 E-value: 9.23e-03
10 20 30
....*....|....*....|....*....|....
gi 515201175 69 VAGVNVPVQVGGGVRTEEDVAALLDAGVARVVVG 102
Cdd:cd00945 168 AVGGRVGVKAAGGIKTLEDALAAIEAGADGIGTS 201
|
|
| |
