|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00748 |
PRK00748 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
1-238 |
3.76e-121 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated
Pssm-ID: 179108 Cd Length: 233 Bit Score: 343.97 E-value: 3.76e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 1 MIIPALDLIDGTVVRLHQGDYARQRDYGNDPLPRLQDYAAQGAGVLHLVDLTGAKDPAKRQIPLIKTLVAGVNVPVQVGG 80
Cdd:PRK00748 2 IIIPAIDLKDGKCVRLYQGDYDQATVYSDDPVAQAKAWEDQGAKWLHLVDLDGAKAGKPVNLELIEAIVKAVDIPVQVGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 81 GVRTEEDVAALLKAGVARVVIGSTAVKSPDVVKGWFERFGAQaLVLALDVRidehgTKQVAVSGWQENSGVSLEQLVETY 160
Cdd:PRK00748 82 GIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFPGK-IVVGLDAR-----DGKVATDGWLETSGVTAEDLAKRF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446508881 161 LPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYPqIAFQSSGGIGDIDDIAALRGTG-VRGVIVGRALLEGKFTVKEA 238
Cdd:PRK00748 156 EDAGVKAIIYTDISRDGTLSGPNVEATRELAAAVP-IPVIASGGVSSLDDIKALKGLGaVEGVIVGRALYEGKFDLAEA 233
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
1-240 |
1.39e-108 |
|
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: 312.49 E-value: 1.39e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 1 MIIPALDLIDGTVVRLHQGDYARQRDYGNDPLPRLQDYAAQGAGVLHLVDLTGAKDPAKRQIPLIKTLVAGVNVPVQVGG 80
Cdd:cd04732 1 IIIPAIDLKDGKCVRLYQGDYDKKTVYSDDPVEVAKKWEEAGAKWLHVVDLDGAKGGEPVNLELIEEIVKAVGIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 81 GVRTEEDVAALLKAGVARVVIGSTAVKSPDVVKGWFERFGAQALVLALDVRIDEhgtkqVAVSGWQENSGVSLEQLVETY 160
Cdd:cd04732 81 GIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGGERIVVGLDAKDGK-----VATKGWLETSEVSLEELAKRF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 161 LPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYpQIAFQSSGGIGDIDDIAALRGTGVRGVIVGRALLEGKFTVKEAIQ 240
Cdd:cd04732 156 EELGVKAIIYTDISRDGTLSGPNFELYKELAAAT-GIPVIASGGVSSLDDIKALKELGVAGVIVGKALYEGKITLEEALA 234
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
1-243 |
2.28e-108 |
|
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: 311.97 E-value: 2.28e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 1 MIIPALDLIDGTVVRLHQGDYARQRDYGNDPLPRLQDYAAQGAGVLHLVDLTGAKDPAKRQIPLIKTLVAGVNVPVQVGG 80
Cdd:COG0106 1 IIIPAIDLKDGKCVRLVQGDYDQETVYSDDPVEVAKRWEDAGAEWLHLVDLDGAFAGKPVNLELIEEIAKATGLPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 81 GVRTEEDVAALLKAGVARVVIGSTAVKSPDVVKGWFERFGAQaLVLALDVRidehgTKQVAVSGWQENSGVSLEQLVETY 160
Cdd:COG0106 81 GIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFPER-IVVGLDAR-----DGKVATDGWQETSGVDLEELAKRF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 161 LPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYPqIAFQSSGGIGDIDDIAALRGTGVRGVIVGRALLEGKFTVKEAIQ 240
Cdd:COG0106 155 EDAGVAAILYTDISRDGTLQGPNLELYRELAAATG-IPVIASGGVSSLDDLRALKELGVEGAIVGKALYEGKIDLEEALA 233
|
...
gi 446508881 241 CWQ 243
Cdd:COG0106 234 LAR 236
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
2-237 |
1.23e-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: 289.48 E-value: 1.23e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 2 IIPALDLIDGTVVRLHQGDYARQRDYGNDPLPRLQDYAAQGAGVLHLVDLTGAKDPAKRQIPLIKTLVAGVNVPVQVGGG 81
Cdd:TIGR00007 1 IIPAIDIKDGKCVRLYQGDYDKETVYGDDPVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQVGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 82 VRTEEDVAALLKAGVARVVIGSTAVKSPDVVKGWFERFGAQALVLALDVRIDEhgtkqVAVSGWQENSGVSLEQLVETYL 161
Cdd:TIGR00007 81 IRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYGPERIVVSLDARGGE-----VAVKGWLEKSEVSLEELAKRLE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446508881 162 PVGLKHVLCTDISRDGTLAGSNVSLYEEVCARyPQIAFQSSGGIGDIDDIAALRGTGVRGVIVGRALLEGKFTVKE 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 |
1.64e-95 |
|
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: 278.98 E-value: 1.64e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 1 MIIPALDLIDGTVVRLHQGDYARQRDYGNDPLPRLQDYAAQGAGVLHLVDLTGAKDPAKRQIPLIKTLVAGVNVPVQVGG 80
Cdd:pfam00977 1 RIIPAIDLKDGRVVRLVKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 81 GVRTEEDVAALLKAGVARVVIGSTAVKSPDVVKGWFERFGAQALVLALDVRIDEhgtkqVAVSGWQENSGVSLEQLVETY 160
Cdd:pfam00977 81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAIDARRGK-----VAINGWREDTGIDAVEWAKEL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446508881 161 LPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYpQIAFQSSGGIGDIDDIAALRGTGVRGVIVGRALLEGKFT 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 |
3.76e-121 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated
Pssm-ID: 179108 Cd Length: 233 Bit Score: 343.97 E-value: 3.76e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 1 MIIPALDLIDGTVVRLHQGDYARQRDYGNDPLPRLQDYAAQGAGVLHLVDLTGAKDPAKRQIPLIKTLVAGVNVPVQVGG 80
Cdd:PRK00748 2 IIIPAIDLKDGKCVRLYQGDYDQATVYSDDPVAQAKAWEDQGAKWLHLVDLDGAKAGKPVNLELIEAIVKAVDIPVQVGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 81 GVRTEEDVAALLKAGVARVVIGSTAVKSPDVVKGWFERFGAQaLVLALDVRidehgTKQVAVSGWQENSGVSLEQLVETY 160
Cdd:PRK00748 82 GIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFPGK-IVVGLDAR-----DGKVATDGWLETSGVTAEDLAKRF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446508881 161 LPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYPqIAFQSSGGIGDIDDIAALRGTG-VRGVIVGRALLEGKFTVKEA 238
Cdd:PRK00748 156 EDAGVKAIIYTDISRDGTLSGPNVEATRELAAAVP-IPVIASGGVSSLDDIKALKGLGaVEGVIVGRALYEGKFDLAEA 233
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
1-240 |
1.39e-108 |
|
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: 312.49 E-value: 1.39e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 1 MIIPALDLIDGTVVRLHQGDYARQRDYGNDPLPRLQDYAAQGAGVLHLVDLTGAKDPAKRQIPLIKTLVAGVNVPVQVGG 80
Cdd:cd04732 1 IIIPAIDLKDGKCVRLYQGDYDKKTVYSDDPVEVAKKWEEAGAKWLHVVDLDGAKGGEPVNLELIEEIVKAVGIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 81 GVRTEEDVAALLKAGVARVVIGSTAVKSPDVVKGWFERFGAQALVLALDVRIDEhgtkqVAVSGWQENSGVSLEQLVETY 160
Cdd:cd04732 81 GIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGGERIVVGLDAKDGK-----VATKGWLETSEVSLEELAKRF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 161 LPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYpQIAFQSSGGIGDIDDIAALRGTGVRGVIVGRALLEGKFTVKEAIQ 240
Cdd:cd04732 156 EELGVKAIIYTDISRDGTLSGPNFELYKELAAAT-GIPVIASGGVSSLDDIKALKELGVAGVIVGKALYEGKITLEEALA 234
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
1-243 |
2.28e-108 |
|
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: 311.97 E-value: 2.28e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 1 MIIPALDLIDGTVVRLHQGDYARQRDYGNDPLPRLQDYAAQGAGVLHLVDLTGAKDPAKRQIPLIKTLVAGVNVPVQVGG 80
Cdd:COG0106 1 IIIPAIDLKDGKCVRLVQGDYDQETVYSDDPVEVAKRWEDAGAEWLHLVDLDGAFAGKPVNLELIEEIAKATGLPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 81 GVRTEEDVAALLKAGVARVVIGSTAVKSPDVVKGWFERFGAQaLVLALDVRidehgTKQVAVSGWQENSGVSLEQLVETY 160
Cdd:COG0106 81 GIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFPER-IVVGLDAR-----DGKVATDGWQETSGVDLEELAKRF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 161 LPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYPqIAFQSSGGIGDIDDIAALRGTGVRGVIVGRALLEGKFTVKEAIQ 240
Cdd:COG0106 155 EDAGVAAILYTDISRDGTLQGPNLELYRELAAATG-IPVIASGGVSSLDDLRALKELGVEGAIVGKALYEGKIDLEEALA 233
|
...
gi 446508881 241 CWQ 243
Cdd:COG0106 234 LAR 236
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
2-237 |
1.23e-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: 289.48 E-value: 1.23e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 2 IIPALDLIDGTVVRLHQGDYARQRDYGNDPLPRLQDYAAQGAGVLHLVDLTGAKDPAKRQIPLIKTLVAGVNVPVQVGGG 81
Cdd:TIGR00007 1 IIPAIDIKDGKCVRLYQGDYDKETVYGDDPVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQVGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 82 VRTEEDVAALLKAGVARVVIGSTAVKSPDVVKGWFERFGAQALVLALDVRIDEhgtkqVAVSGWQENSGVSLEQLVETYL 161
Cdd:TIGR00007 81 IRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYGPERIVVSLDARGGE-----VAVKGWLEKSEVSLEELAKRLE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446508881 162 PVGLKHVLCTDISRDGTLAGSNVSLYEEVCARyPQIAFQSSGGIGDIDDIAALRGTGVRGVIVGRALLEGKFTVKE 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 |
1.64e-95 |
|
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: 278.98 E-value: 1.64e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 1 MIIPALDLIDGTVVRLHQGDYARQRDYGNDPLPRLQDYAAQGAGVLHLVDLTGAKDPAKRQIPLIKTLVAGVNVPVQVGG 80
Cdd:pfam00977 1 RIIPAIDLKDGRVVRLVKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 81 GVRTEEDVAALLKAGVARVVIGSTAVKSPDVVKGWFERFGAQALVLALDVRIDEhgtkqVAVSGWQENSGVSLEQLVETY 160
Cdd:pfam00977 81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAIDARRGK-----VAINGWREDTGIDAVEWAKEL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446508881 161 LPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYpQIAFQSSGGIGDIDDIAALRGTGVRGVIVGRALLEGKFT 234
Cdd:pfam00977 156 EELGAGEILLTDIDRDGTLSGPDLELTRELAEAV-NIPVIASGGVGSLEDLKELFTEGVDGVIAGSALYEGEIT 228
|
|
| PRK13585 |
PRK13585 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ... |
2-239 |
7.99e-53 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase;
Pssm-ID: 184165 Cd Length: 241 Bit Score: 170.86 E-value: 7.99e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 2 IIPALDLIDGTVVRLHQGDYARQRDYGNDPLPRLQDYAAQGAGVLHLVDLTGAKDPAKRQIPLIKTLVAGVNVPVQVGGG 81
Cdd:PRK13585 5 VIPAVDMKGGKCVQLVQGEPGTETVSYGDPVEVAKRWVDAGAETLHLVDLDGAFEGERKNAEAIEKIIEAVGVPVQLGGG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 82 VRTEEDVAALLKAGVARVVIGSTAVKSPDVVKGWFERFGAQALVLALDVRIDEhgtkqVAVSGWQENSGVSLEQLVETYL 161
Cdd:PRK13585 85 IRSAEDAASLLDLGVDRVILGTAAVENPEIVRELSEEFGSERVMVSLDAKDGE-----VVIKGWTEKTGYTPVEAAKRFE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 162 PVGLKHVLCTDISRDGTLAGSNVSLYEEVCARY--PQIAfqsSGGIGDIDDIAALRGTGVRGVIVGRALLEGKFTVKEAI 239
Cdd:PRK13585 160 ELGAGSILFTNVDVEGLLEGVNTEPVKELVDSVdiPVIA---SGGVTTLDDLRALKEAGAAGVVVGSALYKGKFTLEEAI 236
|
|
| PRK14024 |
PRK14024 |
phosphoribosyl isomerase A; Provisional |
2-239 |
2.87e-39 |
|
phosphoribosyl isomerase A; Provisional
Pssm-ID: 237589 Cd Length: 241 Bit Score: 135.86 E-value: 2.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 2 IIPALDLIDGTVVRLHQGDYARQRDYGnDPLPRLQDYAAQGAGVLHLVDLTGAKDPAKRQiPLIKTLVAGVNVPVQVGGG 81
Cdd:PRK14024 6 LLPAVDVVDGQAVRLVQGEAGSETSYG-SPLDAALAWQRDGAEWIHLVDLDAAFGRGSNR-ELLAEVVGKLDVKVELSGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 82 VRTEEDVAALLKAGVARVVIGSTAVKSPDVVKGWFERFGAQALVlALDVRidehGTkQVAVSGWQENSGvSLEQLVETYL 161
Cdd:PRK14024 84 IRDDESLEAALATGCARVNIGTAALENPEWCARVIAEHGDRVAV-GLDVR----GH-TLAARGWTRDGG-DLWEVLERLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 162 PVGLKHVLCTDISRDGTLAGSNVSLYEEVCARY--PQIAfqsSGGIGDIDDIAALRG---TGVRGVIVGRALLEGKFTVK 236
Cdd:PRK14024 157 SAGCSRYVVTDVTKDGTLTGPNLELLREVCARTdaPVVA---SGGVSSLDDLRALAElvpLGVEGAIVGKALYAGAFTLP 233
|
...
gi 446508881 237 EAI 239
Cdd:PRK14024 234 EAL 236
|
|
| HisA_HisF |
cd04723 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ... |
1-240 |
4.40e-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: 119.68 E-value: 4.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 1 MIIPALDLIDGTVVRLHQGDYARQRD------YGNDPLPRLQDYAAQGAGVLHLVDLTGAKDPAkRQIPLIKTLVAGVNV 74
Cdd:cd04723 1 RIIPVIDLKDGVVVHGVGGDRDNYRPitsnlcSTSDPLDVARAYKELGFRGLYIADLDAIMGRG-DNDEAIRELAAAWPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 75 PVQVGGGVRTEEDVAALLKAGVARVVIGSTAVKSPDVVKGwFERFGAQALVLALDVRidehgTKQVAVSGWQENSgVSLE 154
Cdd:cd04723 80 GLWVDGGIRSLENAQEWLKRGASRVIVGTETLPSDDDEDR-LAALGEQRLVLSLDFR-----GGQLLKPTDFIGP-EELL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 155 QLVETYLpvglKHVLCTDISRDGTLAGSNVSLYEEVCARYPqIAFQSSGGIGDIDDIAALRGTGVRGVIVGRALLEGKFT 234
Cdd:cd04723 153 RRLAKWP----EELIVLDIDRVGSGQGPDLELLERLAARAD-IPVIAAGGVRSVEDLELLKKLGASGALVASALHDGGLT 227
|
....*.
gi 446508881 235 VKEAIQ 240
Cdd:cd04723 228 LEDVVR 233
|
|
| HisF |
cd04731 |
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ... |
2-240 |
4.86e-33 |
|
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: 119.88 E-value: 4.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 2 IIPALDLIDGTVVRLHQgdYARQRDYGnDPLPRLQDYAAQGAGVLHLVDLTGAKDPAKRQIPLIKTLVAGVNVPVQVGGG 81
Cdd:cd04731 3 IIPCLDVKDGRVVKGVN--FKNLRDAG-DPVELAKRYNEQGADELVFLDITASSEGRETMLDVVERVAEEVFIPLTVGGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 82 VRTEEDVAALLKAGVARVVIGSTAVKSPDVVKGWFERFGAQALVLALDVRIDEHGTKQVAVSGWQENSGVSLEQLVETYL 161
Cdd:cd04731 80 IRSLEDARRLLRAGADKVSINSAAVENPELIREIAKRFGSQCVVVSIDAKRRGDGGYEVYTHGGRKPTGLDAVEWAKEVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 162 PVGLKHVLCTDISRDGTLAGSNVSLYEEVCAR--YPQIAfqsSGGIGDIDDI-AALRGTGVRGVIVGRALLEGKFTVKEA 238
Cdd:cd04731 160 ELGAGEILLTSMDRDGTKKGYDLELIRAVSSAvnIPVIA---SGGAGKPEHFvEAFEEGGADAALAASIFHFGEYTIAEL 236
|
..
gi 446508881 239 IQ 240
Cdd:cd04731 237 KE 238
|
|
| PRK04128 |
PRK04128 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
2-238 |
3.48e-31 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 167709 Cd Length: 228 Bit Score: 114.87 E-value: 3.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 2 IIPALDLIDGTVVRLHQGDYARQRDYGnDPLP---RLQDYAAQgagvLHLVDLTGAKDPAKRQIPLIKTLVAGVNVPVQV 78
Cdd:PRK04128 4 IYPAIDLMNGKAVRLYKGRKEEVKVYG-DPVEialRFSEYVDK----IHVVDLDGAFEGKPKNLDVVKNIIRETGLKVQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 79 GGGVRTEEDVAALLKAGVARVVIGSTAVKSpDVVKGWFERFGaqALVLALDVRIDehgtkQVAVSGWQENSGVSLEQLVE 158
Cdd:PRK04128 79 GGGLRTYESIKDAYEIGVENVIIGTKAFDL-EFLEKVTSEFE--GITVSLDVKGG-----RIAVKGWLEESSIKVEDAYE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 159 TyLPVGLKHVLCTDISRDGTLAGsnvslYEEVCARYPQIAFQSSGGIGDIDDIAALRGTGVRGVIVGRALLEGKFTVKEA 238
Cdd:PRK04128 151 M-LKNYVNRFIYTSIERDGTLTG-----IEEIERFWGDEEFIYAGGVSSAEDVKKLAEIGFSGVIIGKALYEGRISLEEL 224
|
|
| PRK13587 |
PRK13587 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
4-227 |
2.34e-30 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Provisional
Pssm-ID: 172156 Cd Length: 234 Bit Score: 112.62 E-value: 2.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 4 PALDLIDGTVVRLHQGDYARQRDYGNDPLPRLQDYAA-QGAGVLHLVDLTGAKDPAKRQIPLIKTLVAGVNVPVQVGGGV 82
Cdd:PRK13587 6 PAIDLIGSTSVRLTEGKYDSEEKMSRSAEESIAYYSQfECVNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIEVGGGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 83 RTEEDVAALLKAGVARVVIGSTAVKSPDVVKGWFERFGAQaLVLALDVRIDehgtkQVAVSGWQENSGVSLEQLVETYLP 162
Cdd:PRK13587 86 RTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGR-IYLSVDAYGE-----DIKVNGWEEDTELNLFSFVRQLSD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446508881 163 VGLKHVLCTDISRDGTLAGSNVSLYEEVcARYPQIAFQSSGGIGDIDDIAALRGTGVRGVIVGRA 227
Cdd:PRK13587 160 IPLGGIIYTDIAKDGKMSGPNFELTGQL-VKATTIPVIASGGIRHQQDIQRLASLNVHAAIIGKA 223
|
|
| hisF |
TIGR00735 |
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ... |
2-237 |
3.72e-29 |
|
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273241 Cd Length: 254 Bit Score: 110.15 E-value: 3.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 2 IIPALDLIDGTVVRlhqGDYARQRDYGNDPLPRLQDYAAQGAGVLHLVDLTGAKDPAKRQIPLIKTLVAGVNVPVQVGGG 81
Cdd:TIGR00735 6 IIPCLDVRDGRVVK---GVQFLNLRDAGDPVELAQRYDEEGADELVFLDITASSEGRTTMIDVVERTAETVFIPLTVGGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 82 VRTEEDVAALLKAGVARVVIGSTAVKSPDVVKGWFERFGAQALVLALDVR---IDEHGTKQVAVSGWQENSGVSLEQLVE 158
Cdd:TIGR00735 83 IKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFGSQCIVVAIDAKrvyVNSYCWYEVYIYGGRESTGLDAVEWAK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 159 TYLPVGLKHVLCTDISRDGTLAGSNVSLYEEVCA--RYPQIAfqsSGGIGDIDDIA-ALRGTGVRGVIVGRALLEGKFTV 235
Cdd:TIGR00735 163 EVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEavKIPVIA---SGGAGKPEHFYeAFTKGKADAALAASVFHYREITI 239
|
..
gi 446508881 236 KE 237
Cdd:TIGR00735 240 GE 241
|
|
| PRK14114 |
PRK14114 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
1-236 |
1.58e-27 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 172604 Cd Length: 241 Bit Score: 105.48 E-value: 1.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 1 MIIPALDLIDGTVVRLHQGDYARQRDYGNDPLPRLQDYAAQGAGVLHLVDLTGAKDPAKRQIPLIKTLVAGVNvPVQVGG 80
Cdd:PRK14114 2 LVVPAIDLFRGKVARMVKGKKENTIFYEKDPAELVEKLIEEGFTLIHVVDLSKAIENSVENLPVLEKLSEFAE-HIQIGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 81 GVRTEEDVAALLKAGVARVVIGSTAVKSPDVVKgWFERFGAQAlVLALDVRidehgTKQVAVSGWQENSGVSLEQLVETY 160
Cdd:PRK14114 81 GIRSLDYAEKLRKLGYRRQIVSSKVLEDPSFLK-FLKEIDVEP-VFSLDTR-----GGKVAFKGWLAEEEIDPVSLLKRL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 161 LPVGLKHVLCTDISRDGTLAGSNVSLYEEVcARYPQIAFQSSGGIGDIDDIAAL-----RGTG-VRGVIVGRALLEGKFT 234
Cdd:PRK14114 154 KEYGLEEIVHTEIEKDGTLQEHDFSLTRKI-AIEAEVKVFAAGGISSENSLKTAqrvhrETNGlLKGVIVGRAFLEGILT 232
|
..
gi 446508881 235 VK 236
Cdd:PRK14114 233 VE 234
|
|
| HisF |
COG0107 |
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ... |
2-240 |
8.11e-27 |
|
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: 103.95 E-value: 8.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 2 IIPALDLIDGTVVRLHQgdYARQRDYGnDPLPRLQDYAAQGAGVLHLVDLTGAKDpaKRQIPL--IKTLVAGVNVPVQVG 79
Cdd:COG0107 5 IIPCLDVKDGRVVKGVN--FVNLRDAG-DPVELAKRYNEQGADELVFLDITASSE--GRKTMLdvVRRVAEEVFIPLTVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 80 GGVRTEEDVAALLKAGVARVVIGSTAVKSPDVVKGWFERFGAQALVLALDVRIDEHGTKQVAVSGWQENSGVSLEQLVet 159
Cdd:COG0107 80 GGIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAIDAKRVPDGGWEVYTHGGRKPTGLDAVEWA-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 160 ylpvglKHV--------LCTDISRDGTLAGSNVSLYEEVCA--RYPQIAfqsSGGIGDIDDIA-ALRGTGVRGVIVGRAL 228
Cdd:COG0107 158 ------KEAeelgageiLLTSMDRDGTKDGYDLELTRAVSEavSIPVIA---SGGAGTLEHFVeVFTEGGADAALAASIF 228
|
250
....*....|..
gi 446508881 229 LEGKFTVKEAIQ 240
Cdd:COG0107 229 HFGEITIAELKA 240
|
|
| PRK13586 |
PRK13586 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
2-232 |
6.45e-15 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 237439 Cd Length: 232 Bit Score: 71.31 E-value: 6.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 2 IIPALDLIDGTVVRLHQGDYARQRDYGNdPLPRLQDYAAQGAGVLHLVDLTGAKDPAKRQIpLIKTLVAGVNVPVQVGGG 81
Cdd:PRK13586 4 IIPSIDISLGKAVKRIRGVKGTGLILGN-PIEIASKLYNEGYTRIHVVDLDAAEGVGNNEM-YIKEISKIGFDWIQVGGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 82 VRTEEDVAALLKAGVARVVIGSTAVKSPDVVKGWFERFGAQALVLAldvrIDEHGTKQVAVSGWQENSgVSLEQLVETYL 161
Cdd:PRK13586 82 IRDIEKAKRLLSLDVNALVFSTIVFTNFNLFHDIVREIGSNRVLVS----IDYDNTKRVLIRGWKEKS-MEVIDGIKKVN 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446508881 162 PVGLKHVLCTDISRDGTLAG--SNVSLYeevcARYPQIAFQSSGGIGDIDDIAALRGTGVRGVIVGRALLEGK 232
Cdd:PRK13586 157 ELELLGIIFTYISNEGTTKGidYNVKDY----ARLIRGLKEYAGGVSSDADLEYLKNVGFDYIIVGMAFYLGK 225
|
|
| KGPDC_HPS |
cd04726 |
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ... |
39-112 |
1.39e-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: 41.80 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 39 AAQGAGVLHLVDLTGAKDPAKRQ--------------------------IPLIKTLVAGVNVPVQVGGGVrTEEDVAALL 92
Cdd:cd04726 98 AAKKYGKEVQVDLIGVEDPEKRAkllklgvdivilhrgidaqaaggwwpEDDLKKVKKLLGVKVAVAGGI-TPDTLPEFK 176
|
90 100
....*....|....*....|
gi 446508881 93 KAGVARVVIGSTAVKSPDVV 112
Cdd:cd04726 177 KAGADIVIVGRAITGAADPA 196
|
|
| trpA |
CHL00200 |
tryptophan synthase alpha subunit; Provisional |
34-107 |
7.58e-04 |
|
tryptophan synthase alpha subunit; Provisional
Pssm-ID: 214394 Cd Length: 263 Bit Score: 39.75 E-value: 7.58e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446508881 34 RLQDYAAQGAGVLHLVD---LTGAKDPAKRQIP-LIKTLVAGVNVPVQVGGGVRTEEDVAALLKAGVARVVIGSTAVK 107
Cdd:CHL00200 159 RIQKIARAAPGCIYLVSttgVTGLKTELDKKLKkLIETIKKMTNKPIILGFGISTSEQIKQIKGWNINGIVIGSACVQ 236
|
|
| PRK01130 |
PRK01130 |
putative N-acetylmannosamine-6-phosphate 2-epimerase; |
64-116 |
1.37e-03 |
|
putative N-acetylmannosamine-6-phosphate 2-epimerase;
Pssm-ID: 234907 Cd Length: 221 Bit Score: 38.98 E-value: 1.37e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 446508881 64 LIKTLVAGVNVPVQVGGGVRTEEDVAALLKAGVARVVIGsTAVKSPDVVKGWF 116
Cdd:PRK01130 164 LLKELLKAVGCPVIAEGRINTPEQAKKALELGAHAVVVG-GAITRPEEITKWF 215
|
|
| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
64-116 |
1.48e-03 |
|
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: 38.71 E-value: 1.48e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 446508881 64 LIKTLVAGVNVPVQVGGGVRTEEDVAALLKAGVARVVIGsTAVKSPDVVKGWF 116
Cdd:cd04729 168 LLKELRKALGIPVIAEGRINSPEQAAKALELGADAVVVG-SAITRPEHITGWF 219
|
|
| PEP_mutase |
pfam13714 |
Phosphoenolpyruvate phosphomutase; This domain includes the enzyme Phosphoenolpyruvate ... |
34-103 |
2.86e-03 |
|
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: 37.95 E-value: 2.86e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 34 RLQDYAAQGAGVLHLvdlTGAKDPakrqiPLIKTLVAGVNVPVQVGGGVRTEeDVAALLKAGVARVVIGS 103
Cdd:pfam13714 163 RARAYAEAGADGIFV---PGLLDP-----ADIAALVAAVPGPVNVLAGPGTL-SVAELAALGVARISYGN 223
|
|
| PRK04302 |
PRK04302 |
triosephosphate isomerase; Provisional |
73-113 |
4.24e-03 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 235274 Cd Length: 223 Bit Score: 37.15 E-value: 4.24e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 446508881 73 NVPVQVGGGVRTEEDVAALLKAGVARVVIGSTAVKSPDVVK 113
Cdd:PRK04302 173 DVKVLCGAGISTGEDVKAALELGADGVLLASGVVKAKDPEA 213
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
37-103 |
5.50e-03 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 36.80 E-value: 5.50e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508881 37 DYAAQGAGVLHLVD---LTGAKDPAKRQIPLIKTLVAGVNVPVQVGGGVRTEEDVAALLKAGVARVVIGS 103
Cdd:cd04722 131 AAEEAGVDEVGLGNgggGGGGRDAVPIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| |
