|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00748 |
PRK00748 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
1-238 |
8.15e-124 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated
Pssm-ID: 179108 Cd Length: 233 Bit Score: 350.91 E-value: 8.15e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 1 MIIPALDLIDGTVVRLHQGDYGKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLIKTLVAGVNVPVQVGG 80
Cdd:PRK00748 2 IIIPAIDLKDGKCVRLYQGDYDQATVYSDDPVAQAKAWEDQGAKWLHLVDLDGAKAGKPVNLELIEAIVKAVDIPVQVGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 81 GVRSEEDVAALLEAGVARVVVGSTAVKSPDMVKGWFERFGaDALVLALDVRideqgNKQVAVSGWQENSGVSLEQLVETY 160
Cdd:PRK00748 82 GIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFP-GKIVVGLDAR-----DGKVATDGWLETSGVTAEDLAKRF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446508905 161 LPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYPqVAFQSSGGIGDIDDVAALRGTG-VRGVIVGRALLEGKFTVKEA 238
Cdd:PRK00748 156 EDAGVKAIIYTDISRDGTLSGPNVEATRELAAAVP-IPVIASGGVSSLDDIKALKGLGaVEGVIVGRALYEGKFDLAEA 233
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
1-243 |
2.78e-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: 319.29 E-value: 2.78e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 1 MIIPALDLIDGTVVRLHQGDYGKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLIKTLVAGVNVPVQVGG 80
Cdd:COG0106 1 IIIPAIDLKDGKCVRLVQGDYDQETVYSDDPVEVAKRWEDAGAEWLHLVDLDGAFAGKPVNLELIEEIAKATGLPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 81 GVRSEEDVAALLEAGVARVVVGSTAVKSPDMVKGWFERFGaDALVLALDVRideqgNKQVAVSGWQENSGVSLEQLVETY 160
Cdd:COG0106 81 GIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFP-ERIVVGLDAR-----DGKVATDGWQETSGVDLEELAKRF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 161 LPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYPqVAFQSSGGIGDIDDVAALRGTGVRGVIVGRALLEGKFTVKEAIA 240
Cdd:COG0106 155 EDAGVAAILYTDISRDGTLQGPNLELYRELAAATG-IPVIASGGVSSLDDLRALKELGVEGAIVGKALYEGKIDLEEALA 233
|
...
gi 446508905 241 CWQ 243
Cdd:COG0106 234 LAR 236
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
1-240 |
7.05e-111 |
|
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: 318.27 E-value: 7.05e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 1 MIIPALDLIDGTVVRLHQGDYGKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLIKTLVAGVNVPVQVGG 80
Cdd:cd04732 1 IIIPAIDLKDGKCVRLYQGDYDKKTVYSDDPVEVAKKWEEAGAKWLHVVDLDGAKGGEPVNLELIEEIVKAVGIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 81 GVRSEEDVAALLEAGVARVVVGSTAVKSPDMVKGWFERFGADALVLALDVRIDEqgnkqVAVSGWQENSGVSLEQLVETY 160
Cdd:cd04732 81 GIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGGERIVVGLDAKDGK-----VATKGWLETSEVSLEELAKRF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 161 LPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYpQVAFQSSGGIGDIDDVAALRGTGVRGVIVGRALLEGKFTVKEAIA 240
Cdd:cd04732 156 EELGVKAIIYTDISRDGTLSGPNFELYKELAAAT-GIPVIASGGVSSLDDIKALKELGVAGVIVGKALYEGKITLEEALA 234
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
2-237 |
1.24e-102 |
|
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: 297.19 E-value: 1.24e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 2 IIPALDLIDGTVVRLHQGDYGKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLIKTLVAGVNVPVQVGGG 81
Cdd:TIGR00007 1 IIPAIDIKDGKCVRLYQGDYDKETVYGDDPVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQVGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 82 VRSEEDVAALLEAGVARVVVGSTAVKSPDMVKGWFERFGADALVLALDVRIDEqgnkqVAVSGWQENSGVSLEQLVETYL 161
Cdd:TIGR00007 81 IRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYGPERIVVSLDARGGE-----VAVKGWLEKSEVSLEELAKRLE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446508905 162 PVGLKHVLCTDISRDGTLAGSNVSLYEEVCARyPQVAFQSSGGIGDIDDVAALRGTGVRGVIVGRALLEGKFTVKE 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 |
5.43e-96 |
|
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: 280.13 E-value: 5.43e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 1 MIIPALDLIDGTVVRLHQGDYGKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLIKTLVAGVNVPVQVGG 80
Cdd:pfam00977 1 RIIPAIDLKDGRVVRLVKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 81 GVRSEEDVAALLEAGVARVVVGSTAVKSPDMVKGWFERFGADALVLALDVRideqgNKQVAVSGWQENSGVSLEQLVETY 160
Cdd:pfam00977 81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAIDAR-----RGKVAINGWREDTGIDAVEWAKEL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446508905 161 LPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYpQVAFQSSGGIGDIDDVAALRGTGVRGVIVGRALLEGKFT 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 |
8.15e-124 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated
Pssm-ID: 179108 Cd Length: 233 Bit Score: 350.91 E-value: 8.15e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 1 MIIPALDLIDGTVVRLHQGDYGKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLIKTLVAGVNVPVQVGG 80
Cdd:PRK00748 2 IIIPAIDLKDGKCVRLYQGDYDQATVYSDDPVAQAKAWEDQGAKWLHLVDLDGAKAGKPVNLELIEAIVKAVDIPVQVGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 81 GVRSEEDVAALLEAGVARVVVGSTAVKSPDMVKGWFERFGaDALVLALDVRideqgNKQVAVSGWQENSGVSLEQLVETY 160
Cdd:PRK00748 82 GIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFP-GKIVVGLDAR-----DGKVATDGWLETSGVTAEDLAKRF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446508905 161 LPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYPqVAFQSSGGIGDIDDVAALRGTG-VRGVIVGRALLEGKFTVKEA 238
Cdd:PRK00748 156 EDAGVKAIIYTDISRDGTLSGPNVEATRELAAAVP-IPVIASGGVSSLDDIKALKGLGaVEGVIVGRALYEGKFDLAEA 233
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
1-243 |
2.78e-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: 319.29 E-value: 2.78e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 1 MIIPALDLIDGTVVRLHQGDYGKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLIKTLVAGVNVPVQVGG 80
Cdd:COG0106 1 IIIPAIDLKDGKCVRLVQGDYDQETVYSDDPVEVAKRWEDAGAEWLHLVDLDGAFAGKPVNLELIEEIAKATGLPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 81 GVRSEEDVAALLEAGVARVVVGSTAVKSPDMVKGWFERFGaDALVLALDVRideqgNKQVAVSGWQENSGVSLEQLVETY 160
Cdd:COG0106 81 GIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFP-ERIVVGLDAR-----DGKVATDGWQETSGVDLEELAKRF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 161 LPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYPqVAFQSSGGIGDIDDVAALRGTGVRGVIVGRALLEGKFTVKEAIA 240
Cdd:COG0106 155 EDAGVAAILYTDISRDGTLQGPNLELYRELAAATG-IPVIASGGVSSLDDLRALKELGVEGAIVGKALYEGKIDLEEALA 233
|
...
gi 446508905 241 CWQ 243
Cdd:COG0106 234 LAR 236
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
1-240 |
7.05e-111 |
|
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: 318.27 E-value: 7.05e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 1 MIIPALDLIDGTVVRLHQGDYGKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLIKTLVAGVNVPVQVGG 80
Cdd:cd04732 1 IIIPAIDLKDGKCVRLYQGDYDKKTVYSDDPVEVAKKWEEAGAKWLHVVDLDGAKGGEPVNLELIEEIVKAVGIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 81 GVRSEEDVAALLEAGVARVVVGSTAVKSPDMVKGWFERFGADALVLALDVRIDEqgnkqVAVSGWQENSGVSLEQLVETY 160
Cdd:cd04732 81 GIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGGERIVVGLDAKDGK-----VATKGWLETSEVSLEELAKRF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 161 LPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYpQVAFQSSGGIGDIDDVAALRGTGVRGVIVGRALLEGKFTVKEAIA 240
Cdd:cd04732 156 EELGVKAIIYTDISRDGTLSGPNFELYKELAAAT-GIPVIASGGVSSLDDIKALKELGVAGVIVGKALYEGKITLEEALA 234
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
2-237 |
1.24e-102 |
|
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: 297.19 E-value: 1.24e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 2 IIPALDLIDGTVVRLHQGDYGKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLIKTLVAGVNVPVQVGGG 81
Cdd:TIGR00007 1 IIPAIDIKDGKCVRLYQGDYDKETVYGDDPVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQVGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 82 VRSEEDVAALLEAGVARVVVGSTAVKSPDMVKGWFERFGADALVLALDVRIDEqgnkqVAVSGWQENSGVSLEQLVETYL 161
Cdd:TIGR00007 81 IRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYGPERIVVSLDARGGE-----VAVKGWLEKSEVSLEELAKRLE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446508905 162 PVGLKHVLCTDISRDGTLAGSNVSLYEEVCARyPQVAFQSSGGIGDIDDVAALRGTGVRGVIVGRALLEGKFTVKE 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 |
5.43e-96 |
|
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: 280.13 E-value: 5.43e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 1 MIIPALDLIDGTVVRLHQGDYGKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLIKTLVAGVNVPVQVGG 80
Cdd:pfam00977 1 RIIPAIDLKDGRVVRLVKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 81 GVRSEEDVAALLEAGVARVVVGSTAVKSPDMVKGWFERFGADALVLALDVRideqgNKQVAVSGWQENSGVSLEQLVETY 160
Cdd:pfam00977 81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAIDAR-----RGKVAINGWREDTGIDAVEWAKEL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446508905 161 LPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYpQVAFQSSGGIGDIDDVAALRGTGVRGVIVGRALLEGKFT 234
Cdd:pfam00977 156 EELGAGEILLTDIDRDGTLSGPDLELTRELAEAV-NIPVIASGGVGSLEDLKELFTEGVDGVIAGSALYEGEIT 228
|
|
| PRK13585 |
PRK13585 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ... |
2-240 |
8.84e-57 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase;
Pssm-ID: 184165 Cd Length: 241 Bit Score: 180.87 E-value: 8.84e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 2 IIPALDLIDGTVVRLHQGDYGKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLIKTLVAGVNVPVQVGGG 81
Cdd:PRK13585 5 VIPAVDMKGGKCVQLVQGEPGTETVSYGDPVEVAKRWVDAGAETLHLVDLDGAFEGERKNAEAIEKIIEAVGVPVQLGGG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 82 VRSEEDVAALLEAGVARVVVGSTAVKSPDMVKGWFERFGADALVLALDVRideqgNKQVAVSGWQENSGVSLEQLVETYL 161
Cdd:PRK13585 85 IRSAEDAASLLDLGVDRVILGTAAVENPEIVRELSEEFGSERVMVSLDAK-----DGEVVIKGWTEKTGYTPVEAAKRFE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 162 PVGLKHVLCTDISRDGTLAGSNVSLYEEVCARY--PQVAfqsSGGIGDIDDVAALRGTGVRGVIVGRALLEGKFTVKEAI 239
Cdd:PRK13585 160 ELGAGSILFTNVDVEGLLEGVNTEPVKELVDSVdiPVIA---SGGVTTLDDLRALKEAGAAGVVVGSALYKGKFTLEEAI 236
|
.
gi 446508905 240 A 240
Cdd:PRK13585 237 E 237
|
|
| PRK14024 |
PRK14024 |
phosphoribosyl isomerase A; Provisional |
2-240 |
2.19e-42 |
|
phosphoribosyl isomerase A; Provisional
Pssm-ID: 237589 Cd Length: 241 Bit Score: 143.95 E-value: 2.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 2 IIPALDLIDGTVVRLHQGDYGKQRDYGnDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQiPLIKTLVAGVNVPVQVGGG 81
Cdd:PRK14024 6 LLPAVDVVDGQAVRLVQGEAGSETSYG-SPLDAALAWQRDGAEWIHLVDLDAAFGRGSNR-ELLAEVVGKLDVKVELSGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 82 VRSEEDVAALLEAGVARVVVGSTAVKSPDMVKGWFERFGaDALVLALDVRideqgNKQVAVSGWQENSGvSLEQLVETYL 161
Cdd:PRK14024 84 IRDDESLEAALATGCARVNIGTAALENPEWCARVIAEHG-DRVAVGLDVR-----GHTLAARGWTRDGG-DLWEVLERLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 162 PVGLKHVLCTDISRDGTLAGSNVSLYEEVCARY--PQVAfqsSGGIGDIDDVAALRG---TGVRGVIVGRALLEGKFTVK 236
Cdd:PRK14024 157 SAGCSRYVVTDVTKDGTLTGPNLELLREVCARTdaPVVA---SGGVSSLDDLRALAElvpLGVEGAIVGKALYAGAFTLP 233
|
....
gi 446508905 237 EAIA 240
Cdd:PRK14024 234 EALA 237
|
|
| HisA_HisF |
cd04723 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ... |
1-240 |
1.36e-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: 121.22 E-value: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 1 MIIPALDLIDGTVVRLHQGDYGKQRD------YGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAkRQIPLIKTLVAGVNV 74
Cdd:cd04723 1 RIIPVIDLKDGVVVHGVGGDRDNYRPitsnlcSTSDPLDVARAYKELGFRGLYIADLDAIMGRG-DNDEAIRELAAAWPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 75 PVQVGGGVRSEEDVAALLEAGVARVVVGSTAVKSPDMVKGwFERFGADALVLALDVRiDEQGNKQVAVSGWQEnsgvsLE 154
Cdd:cd04723 80 GLWVDGGIRSLENAQEWLKRGASRVIVGTETLPSDDDEDR-LAALGEQRLVLSLDFR-GGQLLKPTDFIGPEE-----LL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 155 QLVETYlpvgLKHVLCTDISRDGTLAGSNVSLYEEVCARYPqVAFQSSGGIGDIDDVAALRGTGVRGVIVGRALLEGKFT 234
Cdd:cd04723 153 RRLAKW----PEELIVLDIDRVGSGQGPDLELLERLAARAD-IPVIAAGGVRSVEDLELLKKLGASGALVASALHDGGLT 227
|
....*.
gi 446508905 235 VKEAIA 240
Cdd:cd04723 228 LEDVVR 233
|
|
| HisF |
cd04731 |
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ... |
2-240 |
1.20e-31 |
|
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: 116.41 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 2 IIPALDLIDGTVVRLHQgdYGKQRDYGnDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLIKTLVAGVNVPVQVGGG 81
Cdd:cd04731 3 IIPCLDVKDGRVVKGVN--FKNLRDAG-DPVELAKRYNEQGADELVFLDITASSEGRETMLDVVERVAEEVFIPLTVGGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 82 VRSEEDVAALLEAGVARVVVGSTAVKSPDMVKGWFERFGADALVLALDVRIDEQGNKQVAVSGWQENSGVSLEQLVETYL 161
Cdd:cd04731 80 IRSLEDARRLLRAGADKVSINSAAVENPELIREIAKRFGSQCVVVSIDAKRRGDGGYEVYTHGGRKPTGLDAVEWAKEVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 162 PVGLKHVLCTDISRDGTLAGSNVSLYEEVCAR--YPQVAfqsSGGIGDIDD-VAALRGTGVRGVIVGRALLEGKFTVKEA 238
Cdd:cd04731 160 ELGAGEILLTSMDRDGTKKGYDLELIRAVSSAvnIPVIA---SGGAGKPEHfVEAFEEGGADAALAASIFHFGEYTIAEL 236
|
..
gi 446508905 239 IA 240
Cdd:cd04731 237 KE 238
|
|
| PRK04128 |
PRK04128 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
2-238 |
2.22e-31 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 167709 Cd Length: 228 Bit Score: 115.25 E-value: 2.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 2 IIPALDLIDGTVVRLHQGDYGKQRDYGnDPLP---RLQDYAaqgaEVLHLVDLTGAKDPAKRQIPLIKTLVAGVNVPVQV 78
Cdd:PRK04128 4 IYPAIDLMNGKAVRLYKGRKEEVKVYG-DPVEialRFSEYV----DKIHVVDLDGAFEGKPKNLDVVKNIIRETGLKVQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 79 GGGVRSEEDVAALLEAGVARVVVGSTAVKSpDMVKGWFERFgaDALVLALDVRideqgNKQVAVSGWQENSGVSLEQLVE 158
Cdd:PRK04128 79 GGGLRTYESIKDAYEIGVENVIIGTKAFDL-EFLEKVTSEF--EGITVSLDVK-----GGRIAVKGWLEESSIKVEDAYE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 159 TyLPVGLKHVLCTDISRDGTLAGsnvslYEEVCARYPQVAFQSSGGIGDIDDVAALRGTGVRGVIVGRALLEGKFTVKEA 238
Cdd:PRK04128 151 M-LKNYVNRFIYTSIERDGTLTG-----IEEIERFWGDEEFIYAGGVSSAEDVKKLAEIGFSGVIIGKALYEGRISLEEL 224
|
|
| PRK13587 |
PRK13587 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
4-227 |
2.87e-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: 2.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 4 PALDLIDGTVVRLHQGDYGKQRDYGNDPLPRLQDYAA-QGAEVLHLVDLTGAKDPAKRQIPLIKTLVAGVNVPVQVGGGV 82
Cdd:PRK13587 6 PAIDLIGSTSVRLTEGKYDSEEKMSRSAEESIAYYSQfECVNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIEVGGGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 83 RSEEDVAALLEAGVARVVVGSTAVKSPDMVKGWFERFgADALVLALDVRIDeqgnkQVAVSGWQENSGVSLEQLVETYLP 162
Cdd:PRK13587 86 RTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTF-PGRIYLSVDAYGE-----DIKVNGWEEDTELNLFSFVRQLSD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446508905 163 VGLKHVLCTDISRDGTLAGSNVSLYEEVcARYPQVAFQSSGGIGDIDDVAALRGTGVRGVIVGRA 227
Cdd:PRK13587 160 IPLGGIIYTDIAKDGKMSGPNFELTGQL-VKATTIPVIASGGIRHQQDIQRLASLNVHAAIIGKA 223
|
|
| PRK14114 |
PRK14114 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
1-236 |
4.85e-28 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 172604 Cd Length: 241 Bit Score: 107.02 E-value: 4.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 1 MIIPALDLIDGTVVRLHQGDYGKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLIKTLVAGVNvPVQVGG 80
Cdd:PRK14114 2 LVVPAIDLFRGKVARMVKGKKENTIFYEKDPAELVEKLIEEGFTLIHVVDLSKAIENSVENLPVLEKLSEFAE-HIQIGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 81 GVRSEEDVAALLEAGVARVVVGSTAVKSPDMVKgWFERFGADAlVLALDVRideqgNKQVAVSGWQENSGVSLEQLVETY 160
Cdd:PRK14114 81 GIRSLDYAEKLRKLGYRRQIVSSKVLEDPSFLK-FLKEIDVEP-VFSLDTR-----GGKVAFKGWLAEEEIDPVSLLKRL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 161 LPVGLKHVLCTDISRDGTLAGSNVSLYEEVcARYPQVAFQSSGGIGDIDDVAAL-----RGTG-VRGVIVGRALLEGKFT 234
Cdd:PRK14114 154 KEYGLEEIVHTEIEKDGTLQEHDFSLTRKI-AIEAEVKVFAAGGISSENSLKTAqrvhrETNGlLKGVIVGRAFLEGILT 232
|
..
gi 446508905 235 VK 236
Cdd:PRK14114 233 VE 234
|
|
| hisF |
TIGR00735 |
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ... |
2-237 |
4.66e-27 |
|
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273241 Cd Length: 254 Bit Score: 104.37 E-value: 4.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 2 IIPALDLIDGTVVRlhqGDYGKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLIKTLVAGVNVPVQVGGG 81
Cdd:TIGR00735 6 IIPCLDVRDGRVVK---GVQFLNLRDAGDPVELAQRYDEEGADELVFLDITASSEGRTTMIDVVERTAETVFIPLTVGGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 82 VRSEEDVAALLEAGVARVVVGSTAVKSPDMVKGWFERFGADALVLALDVR---IDEQGNKQVAVSGWQENSGVSLEQLVE 158
Cdd:TIGR00735 83 IKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFGSQCIVVAIDAKrvyVNSYCWYEVYIYGGRESTGLDAVEWAK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 159 TYLPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYPqVAFQSSGGIGDIDDVA-ALRGTGVRGVIVGRALLEGKFTVKE 237
Cdd:TIGR00735 163 EVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEAVK-IPVIASGGAGKPEHFYeAFTKGKADAALAASVFHYREITIGE 241
|
|
| HisF |
COG0107 |
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ... |
2-240 |
1.56e-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: 100.48 E-value: 1.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 2 IIPALDLIDGTVVRlhqgdyGKQ----RDYGnDPLPRLQDYAAQGAEVLHLVDLTGAKDpaKRQIPL--IKTLVAGVNVP 75
Cdd:COG0107 5 IIPCLDVKDGRVVK------GVNfvnlRDAG-DPVELAKRYNEQGADELVFLDITASSE--GRKTMLdvVRRVAEEVFIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 76 VQVGGGVRSEEDVAALLEAGVARVVVGSTAVKSPDMVKGWFERFGADALVLALDVRIDEQGNKQVAVSGWQENSGVSLEQ 155
Cdd:COG0107 76 LTVGGGIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAIDAKRVPDGGWEVYTHGGRKPTGLDAVE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 156 LVetylpvglKHV--------LCTDISRDGTLAGSNVSLYEEVCA--RYPQVAfqsSGGIGDIDD-VAALRGTGVRGVIV 224
Cdd:COG0107 156 WA--------KEAeelgageiLLTSMDRDGTKDGYDLELTRAVSEavSIPVIA---SGGAGTLEHfVEVFTEGGADAALA 224
|
250
....*....|....*.
gi 446508905 225 GRALLEGKFTVKEAIA 240
Cdd:COG0107 225 ASIFHFGEITIAELKA 240
|
|
| PRK13586 |
PRK13586 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
2-232 |
1.57e-17 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 237439 Cd Length: 232 Bit Score: 78.63 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 2 IIPALDLIDGTVVRLHQGDYGKQRDYGNdPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIpLIKTLVAGVNVPVQVGGG 81
Cdd:PRK13586 4 IIPSIDISLGKAVKRIRGVKGTGLILGN-PIEIASKLYNEGYTRIHVVDLDAAEGVGNNEM-YIKEISKIGFDWIQVGGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 82 VRSEEDVAALLEAGVARVVVGSTAVKSPDMVKGWFERFGADALVLAldvrIDEQGNKQVAVSGWQENSgVSLEQLVETYL 161
Cdd:PRK13586 82 IRDIEKAKRLLSLDVNALVFSTIVFTNFNLFHDIVREIGSNRVLVS----IDYDNTKRVLIRGWKEKS-MEVIDGIKKVN 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446508905 162 PVGLKHVLCTDISRDGTLAG--SNVSLYeevcARYPQVAFQSSGGIGDIDDVAALRGTGVRGVIVGRALLEGK 232
Cdd:PRK13586 157 ELELLGIIFTYISNEGTTKGidYNVKDY----ARLIRGLKEYAGGVSSDADLEYLKNVGFDYIIVGMAFYLGK 225
|
|
| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
64-116 |
7.21e-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: 42.56 E-value: 7.21e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 446508905 64 LIKTLVAGVNVPVQVGGGVRSEEDVAALLEAGVARVVVGsTAVKSPDMVKGWF 116
Cdd:cd04729 168 LLKELRKALGIPVIAEGRINSPEQAAKALELGADAVVVG-SAITRPEHITGWF 219
|
|
| PRK01130 |
PRK01130 |
putative N-acetylmannosamine-6-phosphate 2-epimerase; |
64-116 |
2.47e-04 |
|
putative N-acetylmannosamine-6-phosphate 2-epimerase;
Pssm-ID: 234907 Cd Length: 221 Bit Score: 40.90 E-value: 2.47e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 446508905 64 LIKTLVAGVNVPVQVGGGVRSEEDVAALLEAGVARVVVGsTAVKSPDMVKGWF 116
Cdd:PRK01130 164 LLKELLKAVGCPVIAEGRINTPEQAKKALELGAHAVVVG-GAITRPEEITKWF 215
|
|
| PEP_mutase |
pfam13714 |
Phosphoenolpyruvate phosphomutase; This domain includes the enzyme Phosphoenolpyruvate ... |
34-103 |
1.49e-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: 38.72 E-value: 1.49e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 34 RLQDYAAQGAEVLHLvdlTGAKDPakrqiPLIKTLVAGVNVPVQVGGGvRSEEDVAALLEAGVARVVVGS 103
Cdd:pfam13714 163 RARAYAEAGADGIFV---PGLLDP-----ADIAALVAAVPGPVNVLAG-PGTLSVAELAALGVARISYGN 223
|
|
| trpA |
PRK13125 |
tryptophan synthase subunit alpha; Provisional |
52-103 |
1.75e-03 |
|
tryptophan synthase subunit alpha; Provisional
Pssm-ID: 237286 Cd Length: 244 Bit Score: 38.48 E-value: 1.75e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 446508905 52 TGAKDP--AKRQIPLIKTLVAgvNVPVQVGGGVRSEEDVAALLEAGVARVVVGS 103
Cdd:PRK13125 164 TGVPLPvsVERNIKRVRNLVG--NKYLVVGFGLDSPEDARDALSAGADGVVVGT 215
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
37-103 |
4.05e-03 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 37.18 E-value: 4.05e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 37 DYAAQGAEVLHLVD---LTGAKDPAKRQIPLIKTLVAGVNVPVQVGGGVRSEEDVAALLEAGVARVVVGS 103
Cdd:cd04722 131 AAEEAGVDEVGLGNgggGGGGRDAVPIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| GGGP-family |
TIGR01768 |
geranylgeranylglyceryl phosphate synthase family protein; This model represents a family of ... |
33-110 |
4.60e-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: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 33 PRLQDYAAQGAE-----VLHLVDLTGAKDPAKRQ-IPLIKTLVAgvNVPVQVGGGVRSEEDVAALLEAGVARVVVGSTAV 106
Cdd:TIGR01768 135 EDLAAYAAMAEEmlgmpIFYLEAGSGAPEPVPPElVAEVKKVLD--KARLFVGGGIRSVEKAREMAEAGADTVVTGNVIE 212
|
....
gi 446508905 107 KSPD 110
Cdd:TIGR01768 213 ESVD 216
|
|
| PcrB |
COG1646 |
Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism]; |
73-113 |
4.65e-03 |
|
Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism];
Pssm-ID: 441252 Cd Length: 241 Bit Score: 37.45 E-value: 4.65e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 446508905 73 NVPVQVGGGVRSEEDVAALLEAGVARVVVGsTAV-KSPDMVK 113
Cdd:COG1646 196 DTPLIYGGGIRSPEKAREMAEAGADTIVVG-NAIeEDPDLAL 236
|
|
| PRK04302 |
PRK04302 |
triosephosphate isomerase; Provisional |
73-110 |
5.59e-03 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 235274 Cd Length: 223 Bit Score: 37.15 E-value: 5.59e-03
10 20 30
....*....|....*....|....*....|....*...
gi 446508905 73 NVPVQVGGGVRSEEDVAALLEAGVARVVVGSTAVKSPD 110
Cdd:PRK04302 173 DVKVLCGAGISTGEDVKAALELGADGVLLASGVVKAKD 210
|
|
| KGPDC_HPS |
cd04726 |
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ... |
39-110 |
5.95e-03 |
|
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: 36.79 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446508905 39 AAQGAEVLHLVDLTGAKDPAKRQ--------------------------IPLIKTLVAGVNVPVQVGGGVrSEEDVAALL 92
Cdd:cd04726 98 AAKKYGKEVQVDLIGVEDPEKRAkllklgvdivilhrgidaqaaggwwpEDDLKKVKKLLGVKVAVAGGI-TPDTLPEFK 176
|
90
....*....|....*...
gi 446508905 93 EAGVARVVVGSTAVKSPD 110
Cdd:cd04726 177 KAGADIVIVGRAITGAAD 194
|
|
| trpA |
CHL00200 |
tryptophan synthase alpha subunit; Provisional |
34-107 |
7.23e-03 |
|
tryptophan synthase alpha subunit; Provisional
Pssm-ID: 214394 Cd Length: 263 Bit Score: 36.67 E-value: 7.23e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446508905 34 RLQDYAAQGAEVLHLVD---LTGAKDPAKRQIP-LIKTLVAGVNVPVQVGGGVRSEEDVAALLEAGVARVVVGSTAVK 107
Cdd:CHL00200 159 RIQKIARAAPGCIYLVSttgVTGLKTELDKKLKkLIETIKKMTNKPIILGFGISTSEQIKQIKGWNINGIVIGSACVQ 236
|
|
| |
