|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00748 |
PRK00748 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
1-238 |
1.32e-122 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated
Pssm-ID: 179108 Cd Length: 233 Bit Score: 347.82 E-value: 1.32e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 1 MIIPALDLIDGTVVRLHQGDYGKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLIKTLVTGVNVPVQVGG 80
Cdd:PRK00748 2 IIIPAIDLKDGKCVRLYQGDYDQATVYSDDPVAQAKAWEDQGAKWLHLVDLDGAKAGKPVNLELIEAIVKAVDIPVQVGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 81 GVRSEEDVAALLEAGVARVVVGSTAVKSPEMVKGWFERFGaDALVLALDVRideqgNKQVAVSGWQENSGVSLEQLVETY 160
Cdd:PRK00748 82 GIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFP-GKIVVGLDAR-----DGKVATDGWLETSGVTAEDLAKRF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1572807911 161 LPVGLKHVLCTDISRDGTLAGSNVFLYEEVCARYPqVAFQSSGGIGDINDVAALRGTG-VRGVIVGRALLEGKFTVKEA 238
Cdd:PRK00748 156 EDAGVKAIIYTDISRDGTLSGPNVEATRELAAAVP-IPVIASGGVSSLDDIKALKGLGaVEGVIVGRALYEGKFDLAEA 233
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
1-243 |
6.15e-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: 315.82 E-value: 6.15e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 1 MIIPALDLIDGTVVRLHQGDYGKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLIKTLVTGVNVPVQVGG 80
Cdd:COG0106 1 IIIPAIDLKDGKCVRLVQGDYDQETVYSDDPVEVAKRWEDAGAEWLHLVDLDGAFAGKPVNLELIEEIAKATGLPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 81 GVRSEEDVAALLEAGVARVVVGSTAVKSPEMVKGWFERFGaDALVLALDVRideqgNKQVAVSGWQENSGVSLEQLVETY 160
Cdd:COG0106 81 GIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFP-ERIVVGLDAR-----DGKVATDGWQETSGVDLEELAKRF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 161 LPVGLKHVLCTDISRDGTLAGSNVFLYEEVCARYPqVAFQSSGGIGDINDVAALRGTGVRGVIVGRALLEGKFTVKEAIA 240
Cdd:COG0106 155 EDAGVAAILYTDISRDGTLQGPNLELYRELAAATG-IPVIASGGVSSLDDLRALKELGVEGAIVGKALYEGKIDLEEALA 233
|
...
gi 1572807911 241 CWQ 243
Cdd:COG0106 234 LAR 236
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
1-240 |
8.65e-110 |
|
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: 315.57 E-value: 8.65e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 1 MIIPALDLIDGTVVRLHQGDYGKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLIKTLVTGVNVPVQVGG 80
Cdd:cd04732 1 IIIPAIDLKDGKCVRLYQGDYDKKTVYSDDPVEVAKKWEEAGAKWLHVVDLDGAKGGEPVNLELIEEIVKAVGIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 81 GVRSEEDVAALLEAGVARVVVGSTAVKSPEMVKGWFERFGADALVLALDVRIDEqgnkqVAVSGWQENSGVSLEQLVETY 160
Cdd:cd04732 81 GIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGGERIVVGLDAKDGK-----VATKGWLETSEVSLEELAKRF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 161 LPVGLKHVLCTDISRDGTLAGSNVFLYEEVCARYpQVAFQSSGGIGDINDVAALRGTGVRGVIVGRALLEGKFTVKEAIA 240
Cdd:cd04732 156 EELGVKAIIYTDISRDGTLSGPNFELYKELAAAT-GIPVIASGGVSSLDDIKALKELGVAGVIVGKALYEGKITLEEALA 234
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
2-237 |
1.02e-101 |
|
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: 294.88 E-value: 1.02e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 2 IIPALDLIDGTVVRLHQGDYGKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLIKTLVTGVNVPVQVGGG 81
Cdd:TIGR00007 1 IIPAIDIKDGKCVRLYQGDYDKETVYGDDPVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQVGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 82 VRSEEDVAALLEAGVARVVVGSTAVKSPEMVKGWFERFGADALVLALDVRIDEqgnkqVAVSGWQENSGVSLEQLVETYL 161
Cdd:TIGR00007 81 IRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYGPERIVVSLDARGGE-----VAVKGWLEKSEVSLEELAKRLE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1572807911 162 PVGLKHVLCTDISRDGTLAGSNVFLYEEVCARyPQVAFQSSGGIGDINDVAALRGTGVRGVIVGRALLEGKFTVKE 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 |
2.13e-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: 278.59 E-value: 2.13e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 1 MIIPALDLIDGTVVRLHQGDYGKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLIKTLVTGVNVPVQVGG 80
Cdd:pfam00977 1 RIIPAIDLKDGRVVRLVKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 81 GVRSEEDVAALLEAGVARVVVGSTAVKSPEMVKGWFERFGADALVLALDVRideqgNKQVAVSGWQENSGVSLEQLVETY 160
Cdd:pfam00977 81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAIDAR-----RGKVAINGWREDTGIDAVEWAKEL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1572807911 161 LPVGLKHVLCTDISRDGTLAGSNVFLYEEVCARYpQVAFQSSGGIGDINDVAALRGTGVRGVIVGRALLEGKFT 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 |
1.32e-122 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated
Pssm-ID: 179108 Cd Length: 233 Bit Score: 347.82 E-value: 1.32e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 1 MIIPALDLIDGTVVRLHQGDYGKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLIKTLVTGVNVPVQVGG 80
Cdd:PRK00748 2 IIIPAIDLKDGKCVRLYQGDYDQATVYSDDPVAQAKAWEDQGAKWLHLVDLDGAKAGKPVNLELIEAIVKAVDIPVQVGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 81 GVRSEEDVAALLEAGVARVVVGSTAVKSPEMVKGWFERFGaDALVLALDVRideqgNKQVAVSGWQENSGVSLEQLVETY 160
Cdd:PRK00748 82 GIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFP-GKIVVGLDAR-----DGKVATDGWLETSGVTAEDLAKRF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1572807911 161 LPVGLKHVLCTDISRDGTLAGSNVFLYEEVCARYPqVAFQSSGGIGDINDVAALRGTG-VRGVIVGRALLEGKFTVKEA 238
Cdd:PRK00748 156 EDAGVKAIIYTDISRDGTLSGPNVEATRELAAAVP-IPVIASGGVSSLDDIKALKGLGaVEGVIVGRALYEGKFDLAEA 233
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
1-243 |
6.15e-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: 315.82 E-value: 6.15e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 1 MIIPALDLIDGTVVRLHQGDYGKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLIKTLVTGVNVPVQVGG 80
Cdd:COG0106 1 IIIPAIDLKDGKCVRLVQGDYDQETVYSDDPVEVAKRWEDAGAEWLHLVDLDGAFAGKPVNLELIEEIAKATGLPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 81 GVRSEEDVAALLEAGVARVVVGSTAVKSPEMVKGWFERFGaDALVLALDVRideqgNKQVAVSGWQENSGVSLEQLVETY 160
Cdd:COG0106 81 GIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFP-ERIVVGLDAR-----DGKVATDGWQETSGVDLEELAKRF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 161 LPVGLKHVLCTDISRDGTLAGSNVFLYEEVCARYPqVAFQSSGGIGDINDVAALRGTGVRGVIVGRALLEGKFTVKEAIA 240
Cdd:COG0106 155 EDAGVAAILYTDISRDGTLQGPNLELYRELAAATG-IPVIASGGVSSLDDLRALKELGVEGAIVGKALYEGKIDLEEALA 233
|
...
gi 1572807911 241 CWQ 243
Cdd:COG0106 234 LAR 236
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
1-240 |
8.65e-110 |
|
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: 315.57 E-value: 8.65e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 1 MIIPALDLIDGTVVRLHQGDYGKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLIKTLVTGVNVPVQVGG 80
Cdd:cd04732 1 IIIPAIDLKDGKCVRLYQGDYDKKTVYSDDPVEVAKKWEEAGAKWLHVVDLDGAKGGEPVNLELIEEIVKAVGIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 81 GVRSEEDVAALLEAGVARVVVGSTAVKSPEMVKGWFERFGADALVLALDVRIDEqgnkqVAVSGWQENSGVSLEQLVETY 160
Cdd:cd04732 81 GIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGGERIVVGLDAKDGK-----VATKGWLETSEVSLEELAKRF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 161 LPVGLKHVLCTDISRDGTLAGSNVFLYEEVCARYpQVAFQSSGGIGDINDVAALRGTGVRGVIVGRALLEGKFTVKEAIA 240
Cdd:cd04732 156 EELGVKAIIYTDISRDGTLSGPNFELYKELAAAT-GIPVIASGGVSSLDDIKALKELGVAGVIVGKALYEGKITLEEALA 234
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
2-237 |
1.02e-101 |
|
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: 294.88 E-value: 1.02e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 2 IIPALDLIDGTVVRLHQGDYGKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLIKTLVTGVNVPVQVGGG 81
Cdd:TIGR00007 1 IIPAIDIKDGKCVRLYQGDYDKETVYGDDPVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQVGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 82 VRSEEDVAALLEAGVARVVVGSTAVKSPEMVKGWFERFGADALVLALDVRIDEqgnkqVAVSGWQENSGVSLEQLVETYL 161
Cdd:TIGR00007 81 IRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYGPERIVVSLDARGGE-----VAVKGWLEKSEVSLEELAKRLE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1572807911 162 PVGLKHVLCTDISRDGTLAGSNVFLYEEVCARyPQVAFQSSGGIGDINDVAALRGTGVRGVIVGRALLEGKFTVKE 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 |
2.13e-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: 278.59 E-value: 2.13e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 1 MIIPALDLIDGTVVRLHQGDYGKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLIKTLVTGVNVPVQVGG 80
Cdd:pfam00977 1 RIIPAIDLKDGRVVRLVKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 81 GVRSEEDVAALLEAGVARVVVGSTAVKSPEMVKGWFERFGADALVLALDVRideqgNKQVAVSGWQENSGVSLEQLVETY 160
Cdd:pfam00977 81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAIDAR-----RGKVAINGWREDTGIDAVEWAKEL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1572807911 161 LPVGLKHVLCTDISRDGTLAGSNVFLYEEVCARYpQVAFQSSGGIGDINDVAALRGTGVRGVIVGRALLEGKFT 234
Cdd:pfam00977 156 EELGAGEILLTDIDRDGTLSGPDLELTRELAEAV-NIPVIASGGVGSLEDLKELFTEGVDGVIAGSALYEGEIT 228
|
|
| PRK13585 |
PRK13585 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ... |
2-240 |
8.07e-56 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase;
Pssm-ID: 184165 Cd Length: 241 Bit Score: 178.56 E-value: 8.07e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 2 IIPALDLIDGTVVRLHQGDYGKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLIKTLVTGVNVPVQVGGG 81
Cdd:PRK13585 5 VIPAVDMKGGKCVQLVQGEPGTETVSYGDPVEVAKRWVDAGAETLHLVDLDGAFEGERKNAEAIEKIIEAVGVPVQLGGG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 82 VRSEEDVAALLEAGVARVVVGSTAVKSPEMVKGWFERFGADALVLALDVRideqgNKQVAVSGWQENSGVSLEQLVETYL 161
Cdd:PRK13585 85 IRSAEDAASLLDLGVDRVILGTAAVENPEIVRELSEEFGSERVMVSLDAK-----DGEVVIKGWTEKTGYTPVEAAKRFE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 162 PVGLKHVLCTDISRDGTLAGSNVFLYEEVCARY--PQVAfqsSGGIGDINDVAALRGTGVRGVIVGRALLEGKFTVKEAI 239
Cdd:PRK13585 160 ELGAGSILFTNVDVEGLLEGVNTEPVKELVDSVdiPVIA---SGGVTTLDDLRALKEAGAAGVVVGSALYKGKFTLEEAI 236
|
.
gi 1572807911 240 A 240
Cdd:PRK13585 237 E 237
|
|
| PRK14024 |
PRK14024 |
phosphoribosyl isomerase A; Provisional |
2-240 |
1.40e-41 |
|
phosphoribosyl isomerase A; Provisional
Pssm-ID: 237589 Cd Length: 241 Bit Score: 142.02 E-value: 1.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 2 IIPALDLIDGTVVRLHQGDYGKQRDYGnDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQiPLIKTLVTGVNVPVQVGGG 81
Cdd:PRK14024 6 LLPAVDVVDGQAVRLVQGEAGSETSYG-SPLDAALAWQRDGAEWIHLVDLDAAFGRGSNR-ELLAEVVGKLDVKVELSGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 82 VRSEEDVAALLEAGVARVVVGSTAVKSPEMVKGWFERFGaDALVLALDVRideqgNKQVAVSGWQENSGvSLEQLVETYL 161
Cdd:PRK14024 84 IRDDESLEAALATGCARVNIGTAALENPEWCARVIAEHG-DRVAVGLDVR-----GHTLAARGWTRDGG-DLWEVLERLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 162 PVGLKHVLCTDISRDGTLAGSNVFLYEEVCARY--PQVAfqsSGGIGDINDVAALRG---TGVRGVIVGRALLEGKFTVK 236
Cdd:PRK14024 157 SAGCSRYVVTDVTKDGTLTGPNLELLREVCARTdaPVVA---SGGVSSLDDLRALAElvpLGVEGAIVGKALYAGAFTLP 233
|
....
gi 1572807911 237 EAIA 240
Cdd:PRK14024 234 EALA 237
|
|
| HisA_HisF |
cd04723 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ... |
1-240 |
3.25e-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: 117.37 E-value: 3.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 1 MIIPALDLIDGTVVRLHQGDYGKQRD------YGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAkRQIPLIKTLVTGVNV 74
Cdd:cd04723 1 RIIPVIDLKDGVVVHGVGGDRDNYRPitsnlcSTSDPLDVARAYKELGFRGLYIADLDAIMGRG-DNDEAIRELAAAWPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 75 PVQVGGGVRSEEDVAALLEAGVARVVVGSTAVKSpEMVKGWFERFGADALVLALDVRiDEQGNKQVAVSGWQEnsgvsLE 154
Cdd:cd04723 80 GLWVDGGIRSLENAQEWLKRGASRVIVGTETLPS-DDDEDRLAALGEQRLVLSLDFR-GGQLLKPTDFIGPEE-----LL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 155 QLVETYlpvgLKHVLCTDISRDGTLAGSNVFLYEEVCARYPqVAFQSSGGIGDINDVAALRGTGVRGVIVGRALLEGKFT 234
Cdd:cd04723 153 RRLAKW----PEELIVLDIDRVGSGQGPDLELLERLAARAD-IPVIAAGGVRSVEDLELLKKLGASGALVASALHDGGLT 227
|
....*.
gi 1572807911 235 VKEAIA 240
Cdd:cd04723 228 LEDVVR 233
|
|
| PRK04128 |
PRK04128 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
2-238 |
7.68e-32 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 167709 Cd Length: 228 Bit Score: 116.41 E-value: 7.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 2 IIPALDLIDGTVVRLHQGDYGKQRDYGnDPLP---RLQDYAaqgaEVLHLVDLTGAKDPAKRQIPLIKTLVTGVNVPVQV 78
Cdd:PRK04128 4 IYPAIDLMNGKAVRLYKGRKEEVKVYG-DPVEialRFSEYV----DKIHVVDLDGAFEGKPKNLDVVKNIIRETGLKVQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 79 GGGVRSEEDVAALLEAGVARVVVGSTAVKSpEMVKGWFERFgaDALVLALDVRideqgNKQVAVSGWQENSGVSLEQLVE 158
Cdd:PRK04128 79 GGGLRTYESIKDAYEIGVENVIIGTKAFDL-EFLEKVTSEF--EGITVSLDVK-----GGRIAVKGWLEESSIKVEDAYE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 159 TyLPVGLKHVLCTDISRDGTLAGsnvflYEEVCARYPQVAFQSSGGIGDINDVAALRGTGVRGVIVGRALLEGKFTVKEA 238
Cdd:PRK04128 151 M-LKNYVNRFIYTSIERDGTLTG-----IEEIERFWGDEEFIYAGGVSSAEDVKKLAEIGFSGVIIGKALYEGRISLEEL 224
|
|
| HisF |
cd04731 |
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ... |
2-240 |
3.25e-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: 3.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 2 IIPALDLIDGTVVRLHQgdYGKQRDYGnDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLIKTLVTGVNVPVQVGGG 81
Cdd:cd04731 3 IIPCLDVKDGRVVKGVN--FKNLRDAG-DPVELAKRYNEQGADELVFLDITASSEGRETMLDVVERVAEEVFIPLTVGGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 82 VRSEEDVAALLEAGVARVVVGSTAVKSPEMVKGWFERFGADALVLALDVRIDEQGNKQVAVSGWQENSGVSLEQLVETYL 161
Cdd:cd04731 80 IRSLEDARRLLRAGADKVSINSAAVENPELIREIAKRFGSQCVVVSIDAKRRGDGGYEVYTHGGRKPTGLDAVEWAKEVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 162 PVGLKHVLCTDISRDGTLAGSNVFLYEEVCAR--YPQVAfqsSGGIGDIND-VAALRGTGVRGVIVGRALLEGKFTVKEA 238
Cdd:cd04731 160 ELGAGEILLTSMDRDGTKKGYDLELIRAVSSAvnIPVIA---SGGAGKPEHfVEAFEEGGADAALAASIFHFGEYTIAEL 236
|
..
gi 1572807911 239 IA 240
Cdd:cd04731 237 KE 238
|
|
| PRK13587 |
PRK13587 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
4-227 |
8.36e-30 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Provisional
Pssm-ID: 172156 Cd Length: 234 Bit Score: 111.46 E-value: 8.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 4 PALDLIDGTVVRLHQGDYGKQRDYGNDPLPRLQDYAA-QGAEVLHLVDLTGAKDPAKRQIPLIKTLVTGVNVPVQVGGGV 82
Cdd:PRK13587 6 PAIDLIGSTSVRLTEGKYDSEEKMSRSAEESIAYYSQfECVNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIEVGGGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 83 RSEEDVAALLEAGVARVVVGSTAVKSPEMVKGWFERFgADALVLALDVRIDeqgnkQVAVSGWQENSGVSLEQLVETYLP 162
Cdd:PRK13587 86 RTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTF-PGRIYLSVDAYGE-----DIKVNGWEEDTELNLFSFVRQLSD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1572807911 163 VGLKHVLCTDISRDGTLAGSNVFLYEEVcARYPQVAFQSSGGIGDINDVAALRGTGVRGVIVGRA 227
Cdd:PRK13587 160 IPLGGIIYTDIAKDGKMSGPNFELTGQL-VKATTIPVIASGGIRHQQDIQRLASLNVHAAIIGKA 223
|
|
| PRK14114 |
PRK14114 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
1-236 |
1.08e-27 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 172604 Cd Length: 241 Bit Score: 105.87 E-value: 1.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 1 MIIPALDLIDGTVVRLHQGDYGKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLIKTLVTGVNvPVQVGG 80
Cdd:PRK14114 2 LVVPAIDLFRGKVARMVKGKKENTIFYEKDPAELVEKLIEEGFTLIHVVDLSKAIENSVENLPVLEKLSEFAE-HIQIGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 81 GVRSEEDVAALLEAGVARVVVGSTAVKSPEMVKgWFERFGADAlVLALDVRideqgNKQVAVSGWQENSGVSLEQLVETY 160
Cdd:PRK14114 81 GIRSLDYAEKLRKLGYRRQIVSSKVLEDPSFLK-FLKEIDVEP-VFSLDTR-----GGKVAFKGWLAEEEIDPVSLLKRL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 161 LPVGLKHVLCTDISRDGTLAGSNVFLYEEVcARYPQVAFQSSGGIGDINDVAAL-----RGTG-VRGVIVGRALLEGKFT 234
Cdd:PRK14114 154 KEYGLEEIVHTEIEKDGTLQEHDFSLTRKI-AIEAEVKVFAAGGISSENSLKTAqrvhrETNGlLKGVIVGRAFLEGILT 232
|
..
gi 1572807911 235 VK 236
Cdd:PRK14114 233 VE 234
|
|
| hisF |
TIGR00735 |
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ... |
2-206 |
1.33e-26 |
|
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273241 Cd Length: 254 Bit Score: 103.21 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 2 IIPALDLIDGTVVRlhqGDYGKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLIKTLVTGVNVPVQVGGG 81
Cdd:TIGR00735 6 IIPCLDVRDGRVVK---GVQFLNLRDAGDPVELAQRYDEEGADELVFLDITASSEGRTTMIDVVERTAETVFIPLTVGGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 82 VRSEEDVAALLEAGVARVVVGSTAVKSPEMVKGWFERFGADALVLALDVR---IDEQGNKQVAVSGWQENSGVSLEQLVE 158
Cdd:TIGR00735 83 IKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFGSQCIVVAIDAKrvyVNSYCWYEVYIYGGRESTGLDAVEWAK 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1572807911 159 TYLPVGLKHVLCTDISRDGTLAGSNVFLYEEVCARYPqVAFQSSGGIG 206
Cdd:TIGR00735 163 EVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEAVK-IPVIASGGAG 209
|
|
| HisF |
COG0107 |
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ... |
2-240 |
9.43e-25 |
|
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; Imidazole glycerol phosphate synthase subunit HisF is part of the Pathway/BioSystem: Histidine biosynthesis
Pssm-ID: 439877 Cd Length: 251 Bit Score: 98.17 E-value: 9.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 2 IIPALDLIDGTVVRlhqgdyGKQ----RDYGnDPLPRLQDYAAQGAEVLHLVDLTGAKDpaKRQIPL--IKTLVTGVNVP 75
Cdd:COG0107 5 IIPCLDVKDGRVVK------GVNfvnlRDAG-DPVELAKRYNEQGADELVFLDITASSE--GRKTMLdvVRRVAEEVFIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 76 VQVGGGVRSEEDVAALLEAGVARVVVGSTAVKSPEMVKGWFERFGADALVLALDVRIDEQGNKQVAVSGWQENSGVSLEQ 155
Cdd:COG0107 76 LTVGGGIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAIDAKRVPDGGWEVYTHGGRKPTGLDAVE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 156 LVetylpvglKHV--------LCTDISRDGTLAGSNVFLYEEVCA--RYPQVAfqsSGGIGDIND-VAALRGTGVRGVIV 224
Cdd:COG0107 156 WA--------KEAeelgageiLLTSMDRDGTKDGYDLELTRAVSEavSIPVIA---SGGAGTLEHfVEVFTEGGADAALA 224
|
250
....*....|....*.
gi 1572807911 225 GRALLEGKFTVKEAIA 240
Cdd:COG0107 225 ASIFHFGEITIAELKA 240
|
|
| PRK13586 |
PRK13586 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
2-232 |
8.21e-17 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 237439 Cd Length: 232 Bit Score: 76.70 E-value: 8.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 2 IIPALDLIDGTVVRLHQGDYGKQRDYGNdPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIpLIKTLVTGVNVPVQVGGG 81
Cdd:PRK13586 4 IIPSIDISLGKAVKRIRGVKGTGLILGN-PIEIASKLYNEGYTRIHVVDLDAAEGVGNNEM-YIKEISKIGFDWIQVGGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 82 VRSEEDVAALLEAGVARVVVGSTAVKSPEMVKGWFERFGADALVLAldvrIDEQGNKQVAVSGWQENSgVSLEQLVETYL 161
Cdd:PRK13586 82 IRDIEKAKRLLSLDVNALVFSTIVFTNFNLFHDIVREIGSNRVLVS----IDYDNTKRVLIRGWKEKS-MEVIDGIKKVN 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1572807911 162 PVGLKHVLCTDISRDGTLAG--SNVFLYeevcARYPQVAFQSSGGIGDINDVAALRGTGVRGVIVGRALLEGK 232
Cdd:PRK13586 157 ELELLGIIFTYISNEGTTKGidYNVKDY----ARLIRGLKEYAGGVSSDADLEYLKNVGFDYIIVGMAFYLGK 225
|
|
| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
64-116 |
1.38e-04 |
|
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to N-acetylglucosamine-6-phosphate. This reaction is part of the pathway that allows the usage of sialic acid as a carbohydrate source. Sialic acids are a family of related sugars that are found as a component of glycoproteins, gangliosides, and other sialoglycoconjugates.
Pssm-ID: 240080 [Multi-domain] Cd Length: 219 Bit Score: 41.79 E-value: 1.38e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1572807911 64 LIKTLVTGVNVPVQVGGGVRSEEDVAALLEAGVARVVVGsTAVKSPEMVKGWF 116
Cdd:cd04729 168 LLKELRKALGIPVIAEGRINSPEQAAKALELGADAVVVG-SAITRPEHITGWF 219
|
|
| trpA |
PRK13125 |
tryptophan synthase subunit alpha; Provisional |
52-136 |
6.30e-04 |
|
tryptophan synthase subunit alpha; Provisional
Pssm-ID: 237286 Cd Length: 244 Bit Score: 40.02 E-value: 6.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 52 TGAKDP--AKRQIPLIKTLVTgvNVPVQVGGGVRSEEDVAALLEAGVARVVVGSTAVKspEMVKGWFErfgaDALVLALD 129
Cdd:PRK13125 164 TGVPLPvsVERNIKRVRNLVG--NKYLVVGFGLDSPEDARDALSAGADGVVVGTAFIE--ELEKNGVE----SALNLLKK 235
|
....*....
gi 1572807911 130 VR--IDEQG 136
Cdd:PRK13125 236 IRgaLDEYK 244
|
|
| PRK01130 |
PRK01130 |
putative N-acetylmannosamine-6-phosphate 2-epimerase; |
64-116 |
9.48e-04 |
|
putative N-acetylmannosamine-6-phosphate 2-epimerase;
Pssm-ID: 234907 Cd Length: 221 Bit Score: 39.36 E-value: 9.48e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1572807911 64 LIKTLVTGVNVPVQVGGGVRSEEDVAALLEAGVARVVVGsTAVKSPEMVKGWF 116
Cdd:PRK01130 164 LLKELLKAVGCPVIAEGRINTPEQAKKALELGAHAVVVG-GAITRPEEITKWF 215
|
|
| trpA |
CHL00200 |
tryptophan synthase alpha subunit; Provisional |
34-107 |
3.01e-03 |
|
tryptophan synthase alpha subunit; Provisional
Pssm-ID: 214394 Cd Length: 263 Bit Score: 37.82 E-value: 3.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1572807911 34 RLQDYAAQGAEVLHLVD---LTGAKDPAKRQIP-LIKTLVTGVNVPVQVGGGVRSEEDVAALLEAGVARVVVGSTAVK 107
Cdd:CHL00200 159 RIQKIARAAPGCIYLVSttgVTGLKTELDKKLKkLIETIKKMTNKPIILGFGISTSEQIKQIKGWNINGIVIGSACVQ 236
|
|
| PEP_mutase |
pfam13714 |
Phosphoenolpyruvate phosphomutase; This domain includes the enzyme Phosphoenolpyruvate ... |
34-103 |
4.36e-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: 37.57 E-value: 4.36e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 34 RLQDYAAQGAEVLHLvdlTGAKDPakrqiPLIKTLVTGVNVPVQVGGGvRSEEDVAALLEAGVARVVVGS 103
Cdd:pfam13714 163 RARAYAEAGADGIFV---PGLLDP-----ADIAALVAAVPGPVNVLAG-PGTLSVAELAALGVARISYGN 223
|
|
| GGGP-family |
TIGR01768 |
geranylgeranylglyceryl phosphate synthase family protein; This model represents a family of ... |
33-110 |
4.91e-03 |
|
geranylgeranylglyceryl phosphate synthase family protein; This model represents a family of sequences including geranylgeranylglyceryl phosphate synthase which catalyzes the first committed step in the synthesis of ether-linked membrane lipids in archaea. The clade of bacterial sequences may have the same function or a closely related function. This model supercedes TIGR00265, which has been retired.
Pssm-ID: 273794 Cd Length: 223 Bit Score: 37.08 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572807911 33 PRLQDYAAQGAE-----VLHLVDLTGAKDPAKRQ-IPLIKTLVTgvNVPVQVGGGVRSEEDVAALLEAGVARVVVGSTAV 106
Cdd:TIGR01768 135 EDLAAYAAMAEEmlgmpIFYLEAGSGAPEPVPPElVAEVKKVLD--KARLFVGGGIRSVEKAREMAEAGADTVVTGNVIE 212
|
....
gi 1572807911 107 KSPE 110
Cdd:TIGR01768 213 ESVD 216
|
|
| PcrB |
COG1646 |
Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism]; |
73-113 |
5.74e-03 |
|
Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism];
Pssm-ID: 441252 Cd Length: 241 Bit Score: 37.06 E-value: 5.74e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1572807911 73 NVPVQVGGGVRSEEDVAALLEAGVARVVVGsTAV-KSPEMVK 113
Cdd:COG1646 196 DTPLIYGGGIRSPEKAREMAEAGADTIVVG-NAIeEDPDLAL 236
|
|
| |
