|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00748 |
PRK00748 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
1-231 |
1.52e-132 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated
Pssm-ID: 179108 Cd Length: 233 Bit Score: 372.86 E-value: 1.52e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 1 MEIFPAIDLKEGRCVRLYQGEFSKETVMNEDPVAQAIIFEKFGAKRLHIVDLDGAVAGESLNLSVIERICKAVRIPVQVG 80
Cdd:PRK00748 1 MIIIPAIDLKDGKCVRLYQGDYDQATVYSDDPVAQAKAWEDQGAKWLHLVDLDGAKAGKPVNLELIEAIVKAVDIPVQVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 81 GGIRSLVAVEKLFSVGVDKVILGTAALYDKTFLEEAVLLYKEKIIVGIDAKNGFVATRGWLDVSEISYIDLAKQMEKIGV 160
Cdd:PRK00748 81 GGIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFPGKIVVGLDARDGKVATDGWLETSGVTAEDLAKRFEDAGV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446324427 161 QTIVFTDISKDGTLGGPNVEQLELLQKSVAIRLIASGGVASIQDVKKLNDM-NIYGVIIGKALYEKTIDLEE 231
Cdd:PRK00748 161 KAIIYTDISRDGTLSGPNVEATRELAAAVPIPVIASGGVSSLDDIKALKGLgAVEGVIVGRALYEGKFDLAE 232
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
2-237 |
1.91e-122 |
|
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: 347.41 E-value: 1.91e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 2 EIFPAIDLKEGRCVRLYQGEFSKETVMNEDPVAQAIIFEKFGAKRLHIVDLDGAVAGESLNLSVIERICKAVRIPVQVGG 81
Cdd:COG0106 1 IIIPAIDLKDGKCVRLVQGDYDQETVYSDDPVEVAKRWEDAGAEWLHLVDLDGAFAGKPVNLELIEEIAKATGLPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 82 GIRSLVAVEKLFSVGVDKVILGTAALYDKTFLEEAVLLYKEKIIVGIDAKNGFVATRGWLDVSEISYIDLAKQMEKIGVQ 161
Cdd:COG0106 81 GIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFPERIVVGLDARDGKVATDGWQETSGVDLEELAKRFEDAGVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446324427 162 TIVFTDISKDGTLGGPNVEQLELLQKSVAIRLIASGGVASIQDVKKLNDMNIYGVIIGKALYEKTIDLEEVLEVTK 237
Cdd:COG0106 161 AILYTDISRDGTLQGPNLELYRELAAATGIPVIASGGVSSLDDLRALKELGVEGAIVGKALYEGKIDLEEALALAR 236
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
2-234 |
1.89e-118 |
|
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: 337.14 E-value: 1.89e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 2 EIFPAIDLKEGRCVRLYQGEFSKETVMNEDPVAQAIIFEKFGAKRLHIVDLDGAVAGESLNLSVIERICKAVRIPVQVGG 81
Cdd:cd04732 1 IIIPAIDLKDGKCVRLYQGDYDKKTVYSDDPVEVAKKWEEAGAKWLHVVDLDGAKGGEPVNLELIEEIVKAVGIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 82 GIRSLVAVEKLFSVGVDKVILGTAALYDKTFLEEAVLLY-KEKIIVGIDAKNGFVATRGWLDVSEISYIDLAKQMEKIGV 160
Cdd:cd04732 81 GIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYgGERIVVGLDAKDGKVATKGWLETSEVSLEELAKRFEELGV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446324427 161 QTIVFTDISKDGTLGGPNVEQLELLQKSVAIRLIASGGVASIQDVKKLNDMNIYGVIIGKALYEKTIDLEEVLE 234
Cdd:cd04732 161 KAIIYTDISRDGTLSGPNFELYKELAAATGIPVIASGGVSSLDDIKALKELGVAGVIVGKALYEGKITLEEALA 234
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
3-231 |
2.16e-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: 296.42 E-value: 2.16e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 3 IFPAIDLKEGRCVRLYQGEFSKETVMNEDPVAQAIIFEKFGAKRLHIVDLDGAVAGESLNLSVIERICKAVRIPVQVGGG 82
Cdd:TIGR00007 1 IIPAIDIKDGKCVRLYQGDYDKETVYGDDPVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQVGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 83 IRSLVAVEKLFSVGVDKVILGTAALYDKTFLEEAVLLYK-EKIIVGIDAKNGFVATRGWLDVSEISYIDLAKQMEKIGVQ 161
Cdd:TIGR00007 81 IRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYGpERIVVSLDARGGEVAVKGWLEKSEVSLEELAKRLEELGLE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 162 TIVFTDISKDGTLGGPNVEQLELLQKSVAIRLIASGGVASIQDVKKLNDMNIYGVIIGKALYEKTIDLEE 231
Cdd:TIGR00007 161 GIIYTDISRDGTLSGPNFELTKELVKAVNVPVIASGGVSSIDDLIALKKLGVYGVIVGKALYEGKITLEE 230
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
2-228 |
1.04e-101 |
|
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: 294.39 E-value: 1.04e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 2 EIFPAIDLKEGRCVRLYQGEFSKETVMNEDPVAQAIIFEKFGAKRLHIVDLDGAVAGESLNLSVIERICKAVRIPVQVGG 81
Cdd:pfam00977 1 RIIPAIDLKDGRVVRLVKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 82 GIRSLVAVEKLFSVGVDKVILGTAALYDKTFLEEAVLLY-KEKIIVGIDAKNGFVATRGWLDVSEISYIDLAKQMEKIGV 160
Cdd:pfam00977 81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFgSQCIVVAIDARRGKVAINGWREDTGIDAVEWAKELEELGA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446324427 161 QTIVFTDISKDGTLGGPNVEQLELLQKSVAIRLIASGGVASIQDVKKLNDMNIYGVIIGKALYEKTID 228
Cdd:pfam00977 161 GEILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELFTEGVDGVIAGSALYEGEIT 228
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00748 |
PRK00748 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
1-231 |
1.52e-132 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated
Pssm-ID: 179108 Cd Length: 233 Bit Score: 372.86 E-value: 1.52e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 1 MEIFPAIDLKEGRCVRLYQGEFSKETVMNEDPVAQAIIFEKFGAKRLHIVDLDGAVAGESLNLSVIERICKAVRIPVQVG 80
Cdd:PRK00748 1 MIIIPAIDLKDGKCVRLYQGDYDQATVYSDDPVAQAKAWEDQGAKWLHLVDLDGAKAGKPVNLELIEAIVKAVDIPVQVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 81 GGIRSLVAVEKLFSVGVDKVILGTAALYDKTFLEEAVLLYKEKIIVGIDAKNGFVATRGWLDVSEISYIDLAKQMEKIGV 160
Cdd:PRK00748 81 GGIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFPGKIVVGLDARDGKVATDGWLETSGVTAEDLAKRFEDAGV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446324427 161 QTIVFTDISKDGTLGGPNVEQLELLQKSVAIRLIASGGVASIQDVKKLNDM-NIYGVIIGKALYEKTIDLEE 231
Cdd:PRK00748 161 KAIIYTDISRDGTLSGPNVEATRELAAAVPIPVIASGGVSSLDDIKALKGLgAVEGVIVGRALYEGKFDLAE 232
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
2-237 |
1.91e-122 |
|
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: 347.41 E-value: 1.91e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 2 EIFPAIDLKEGRCVRLYQGEFSKETVMNEDPVAQAIIFEKFGAKRLHIVDLDGAVAGESLNLSVIERICKAVRIPVQVGG 81
Cdd:COG0106 1 IIIPAIDLKDGKCVRLVQGDYDQETVYSDDPVEVAKRWEDAGAEWLHLVDLDGAFAGKPVNLELIEEIAKATGLPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 82 GIRSLVAVEKLFSVGVDKVILGTAALYDKTFLEEAVLLYKEKIIVGIDAKNGFVATRGWLDVSEISYIDLAKQMEKIGVQ 161
Cdd:COG0106 81 GIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFPERIVVGLDARDGKVATDGWQETSGVDLEELAKRFEDAGVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446324427 162 TIVFTDISKDGTLGGPNVEQLELLQKSVAIRLIASGGVASIQDVKKLNDMNIYGVIIGKALYEKTIDLEEVLEVTK 237
Cdd:COG0106 161 AILYTDISRDGTLQGPNLELYRELAAATGIPVIASGGVSSLDDLRALKELGVEGAIVGKALYEGKIDLEEALALAR 236
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
2-234 |
1.89e-118 |
|
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: 337.14 E-value: 1.89e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 2 EIFPAIDLKEGRCVRLYQGEFSKETVMNEDPVAQAIIFEKFGAKRLHIVDLDGAVAGESLNLSVIERICKAVRIPVQVGG 81
Cdd:cd04732 1 IIIPAIDLKDGKCVRLYQGDYDKKTVYSDDPVEVAKKWEEAGAKWLHVVDLDGAKGGEPVNLELIEEIVKAVGIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 82 GIRSLVAVEKLFSVGVDKVILGTAALYDKTFLEEAVLLY-KEKIIVGIDAKNGFVATRGWLDVSEISYIDLAKQMEKIGV 160
Cdd:cd04732 81 GIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYgGERIVVGLDAKDGKVATKGWLETSEVSLEELAKRFEELGV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446324427 161 QTIVFTDISKDGTLGGPNVEQLELLQKSVAIRLIASGGVASIQDVKKLNDMNIYGVIIGKALYEKTIDLEEVLE 234
Cdd:cd04732 161 KAIIYTDISRDGTLSGPNFELYKELAAATGIPVIASGGVSSLDDIKALKELGVAGVIVGKALYEGKITLEEALA 234
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
3-231 |
2.16e-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: 296.42 E-value: 2.16e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 3 IFPAIDLKEGRCVRLYQGEFSKETVMNEDPVAQAIIFEKFGAKRLHIVDLDGAVAGESLNLSVIERICKAVRIPVQVGGG 82
Cdd:TIGR00007 1 IIPAIDIKDGKCVRLYQGDYDKETVYGDDPVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQVGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 83 IRSLVAVEKLFSVGVDKVILGTAALYDKTFLEEAVLLYK-EKIIVGIDAKNGFVATRGWLDVSEISYIDLAKQMEKIGVQ 161
Cdd:TIGR00007 81 IRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYGpERIVVSLDARGGEVAVKGWLEKSEVSLEELAKRLEELGLE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 162 TIVFTDISKDGTLGGPNVEQLELLQKSVAIRLIASGGVASIQDVKKLNDMNIYGVIIGKALYEKTIDLEE 231
Cdd:TIGR00007 161 GIIYTDISRDGTLSGPNFELTKELVKAVNVPVIASGGVSSIDDLIALKKLGVYGVIVGKALYEGKITLEE 230
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
2-228 |
1.04e-101 |
|
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: 294.39 E-value: 1.04e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 2 EIFPAIDLKEGRCVRLYQGEFSKETVMNEDPVAQAIIFEKFGAKRLHIVDLDGAVAGESLNLSVIERICKAVRIPVQVGG 81
Cdd:pfam00977 1 RIIPAIDLKDGRVVRLVKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 82 GIRSLVAVEKLFSVGVDKVILGTAALYDKTFLEEAVLLY-KEKIIVGIDAKNGFVATRGWLDVSEISYIDLAKQMEKIGV 160
Cdd:pfam00977 81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFgSQCIVVAIDARRGKVAINGWREDTGIDAVEWAKELEELGA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446324427 161 QTIVFTDISKDGTLGGPNVEQLELLQKSVAIRLIASGGVASIQDVKKLNDMNIYGVIIGKALYEKTID 228
Cdd:pfam00977 161 GEILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELFTEGVDGVIAGSALYEGEIT 228
|
|
| PRK13585 |
PRK13585 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ... |
1-237 |
7.27e-73 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase;
Pssm-ID: 184165 Cd Length: 241 Bit Score: 221.71 E-value: 7.27e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 1 MEIFPAIDLKEGRCVRLYQGEFSKETVMNEDPVAQAIIFEKFGAKRLHIVDLDGAVAGESLNLSVIERICKAVRIPVQVG 80
Cdd:PRK13585 3 FEVIPAVDMKGGKCVQLVQGEPGTETVSYGDPVEVAKRWVDAGAETLHLVDLDGAFEGERKNAEAIEKIIEAVGVPVQLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 81 GGIRSLVAVEKLFSVGVDKVILGTAALYDKTFLEE-AVLLYKEKIIVGIDAKNGFVATRGWLDVSEISYIDLAKQMEKIG 159
Cdd:PRK13585 83 GGIRSAEDAASLLDLGVDRVILGTAAVENPEIVRElSEEFGSERVMVSLDAKDGEVVIKGWTEKTGYTPVEAAKRFEELG 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446324427 160 VQTIVFTDISKDGTLGGPNVEQLELLQKSVAIRLIASGGVASIQDVKKLNDMNIYGVIIGKALYEKTIDLEEVLEVTK 237
Cdd:PRK13585 163 AGSILFTNVDVEGLLEGVNTEPVKELVDSVDIPVIASGGVTTLDDLRALKEAGAAGVVVGSALYKGKFTLEEAIEAVK 240
|
|
| PRK04128 |
PRK04128 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
1-235 |
7.33e-55 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 167709 Cd Length: 228 Bit Score: 175.35 E-value: 7.33e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 1 MEIFPAIDLKEGRCVRLYQGefSKETV-MNEDPVAQAIIFEKFGAKrLHIVDLDGAVAGESLNLSVIERICKAVRIPVQV 79
Cdd:PRK04128 2 MRIYPAIDLMNGKAVRLYKG--RKEEVkVYGDPVEIALRFSEYVDK-IHVVDLDGAFEGKPKNLDVVKNIIRETGLKVQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 80 GGGIRSLVAVEKLFSVGVDKVILGTAALyDKTFLEEAVLLYkEKIIVGIDAKNGFVATRGWLDVSEISYIDlAKQMEKIG 159
Cdd:PRK04128 79 GGGLRTYESIKDAYEIGVENVIIGTKAF-DLEFLEKVTSEF-EGITVSLDVKGGRIAVKGWLEESSIKVED-AYEMLKNY 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446324427 160 VQTIVFTDISKDGTLGGpnVEQLELLQKSVAIrlIASGGVASIQDVKKLNDMNIYGVIIGKALYEKTIDLEEVLEV 235
Cdd:PRK04128 156 VNRFIYTSIERDGTLTG--IEEIERFWGDEEF--IYAGGVSSAEDVKKLAEIGFSGVIIGKALYEGRISLEELLEV 227
|
|
| PRK14024 |
PRK14024 |
phosphoribosyl isomerase A; Provisional |
1-237 |
4.32e-47 |
|
phosphoribosyl isomerase A; Provisional
Pssm-ID: 237589 Cd Length: 241 Bit Score: 155.89 E-value: 4.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 1 MEIFPAIDLKEGRCVRLYQGEFSKETVMNeDPVAQAIIFEKFGAKRLHIVDLDGAVaGESLNLSVIERICKAVRIPVQVG 80
Cdd:PRK14024 4 LTLLPAVDVVDGQAVRLVQGEAGSETSYG-SPLDAALAWQRDGAEWIHLVDLDAAF-GRGSNRELLAEVVGKLDVKVELS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 81 GGIRSLVAVEKLFSVGVDKVILGTAALYDKTFLEEAVLLYKEKIIVGIDAKNGFVATRGWL----DVSEIsyidLAKqME 156
Cdd:PRK14024 82 GGIRDDESLEAALATGCARVNIGTAALENPEWCARVIAEHGDRVAVGLDVRGHTLAARGWTrdggDLWEV----LER-LD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 157 KIGVQTIVFTDISKDGTLGGPNVEqlelLQKSVAIR----LIASGGVASIQDV---KKLNDMNIYGVIIGKALYEKTIDL 229
Cdd:PRK14024 157 SAGCSRYVVTDVTKDGTLTGPNLE----LLREVCARtdapVVASGGVSSLDDLralAELVPLGVEGAIVGKALYAGAFTL 232
|
....*...
gi 446324427 230 EEVLEVTK 237
Cdd:PRK14024 233 PEALAVVR 240
|
|
| PRK13587 |
PRK13587 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
1-226 |
4.51e-42 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Provisional
Pssm-ID: 172156 Cd Length: 234 Bit Score: 143.05 E-value: 4.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 1 MEIFPAIDLKEGRCVRLYQGEFSKETVMNEDPVAQAIIFEKFG-AKRLHIVDLDGAVAGESLNLSVIERICKAVRIPVQV 79
Cdd:PRK13587 2 IELWPAIDLIGSTSVRLTEGKYDSEEKMSRSAEESIAYYSQFEcVNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 80 GGGIRSLVAVEKLFSVGVDKVILGTAALYDKTFLEEAVLLYKEKIIVGIDAKNGFVATRGWLDVSEISYIDLAKQMEKIG 159
Cdd:PRK13587 82 GGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGRIYLSVDAYGEDIKVNGWEEDTELNLFSFVRQLSDIP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446324427 160 VQTIVFTDISKDGTLGGPNVEQLELLQKSVAIRLIASGGVASIQDVKKLNDMNIYGVIIGKALYEKT 226
Cdd:PRK13587 162 LGGIIYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGGIRHQQDIQRLASLNVHAAIIGKAAHQAS 228
|
|
| HisA_HisF |
cd04723 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ... |
2-234 |
6.06e-40 |
|
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: 137.40 E-value: 6.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 2 EIFPAIDLKEGRCVRLYQGEFSKETVMNE------DPVAQAIIFEKFGAKRLHIVDLDgAVAGESLNLSVIERICKAVRI 75
Cdd:cd04723 1 RIIPVIDLKDGVVVHGVGGDRDNYRPITSnlcstsDPLDVARAYKELGFRGLYIADLD-AIMGRGDNDEAIRELAAAWPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 76 PVQVGGGIRSLVAVEKLFSVGVDKVILGTAALYDKTFLEEAVLLYKEKIIVGIDAKNGFVATRGW-LDVSEIsyIDLAKQ 154
Cdd:cd04723 80 GLWVDGGIRSLENAQEWLKRGASRVIVGTETLPSDDDEDRLAALGEQRLVLSLDFRGGQLLKPTDfIGPEEL--LRRLAK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 155 MekigVQTIVFTDISKDGTLGGPNVEQLELLQKSVAIRLIASGGVASIQDVKKLNDMNIYGVIIGKALYEKTIDLEEVLE 234
Cdd:cd04723 158 W----PEELIVLDIDRVGSGQGPDLELLERLAARADIPVIAAGGVRSVEDLELLKKLGASGALVASALHDGGLTLEDVVR 233
|
|
| HisF |
cd04731 |
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ... |
3-204 |
4.58e-36 |
|
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: 127.58 E-value: 4.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 3 IFPAIDLKEGRcvrLYQG-EFSKETVMNeDPVAQAIIFEKFGAKRLHIVDLDGAVAGESLNLSVIERICKAVRIPVQVGG 81
Cdd:cd04731 3 IIPCLDVKDGR---VVKGvNFKNLRDAG-DPVELAKRYNEQGADELVFLDITASSEGRETMLDVVERVAEEVFIPLTVGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 82 GIRSLVAVEKLFSVGVDKVILGTAALYDKTFLEEAVLLY-KEKIIVGIDAK-----NGFVATRGWLDVSEISYIDLAKQM 155
Cdd:cd04731 79 GIRSLEDARRLLRAGADKVSINSAAVENPELIREIAKRFgSQCVVVSIDAKrrgdgGYEVYTHGGRKPTGLDAVEWAKEV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446324427 156 EKIGVQTIVFTDISKDGTLGGPNVEQLELLQKSVAIRLIASGGVASIQD 204
Cdd:cd04731 159 EELGAGEILLTSMDRDGTKKGYDLELIRAVSSAVNIPVIASGGAGKPEH 207
|
|
| PRK14114 |
PRK14114 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
1-230 |
4.80e-34 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 172604 Cd Length: 241 Bit Score: 122.43 E-value: 4.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 1 MEIFPAIDLKEGRCVRLYQGEFSKETVMNEDPV--AQAIIFEKFGAkrLHIVDLDGAVAGESLNLSVIERICKAVRiPVQ 78
Cdd:PRK14114 1 MLVVPAIDLFRGKVARMVKGKKENTIFYEKDPAelVEKLIEEGFTL--IHVVDLSKAIENSVENLPVLEKLSEFAE-HIQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 79 VGGGIRSLVAVEKLFSVGVDKVILGTAALYDKTFLEEAVLLYKEKIIvGIDAKNGFVATRGWLDVSEISYIDLAKQMEKI 158
Cdd:PRK14114 78 IGGGIRSLDYAEKLRKLGYRRQIVSSKVLEDPSFLKFLKEIDVEPVF-SLDTRGGKVAFKGWLAEEEIDPVSLLKRLKEY 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446324427 159 GVQTIVFTDISKDGTLGGPNVEQLELLQKSVAIRLIASGGVAS------IQDVKKLNDMNIYGVIIGKALYEKTIDLE 230
Cdd:PRK14114 157 GLEEIVHTEIEKDGTLQEHDFSLTRKIAIEAEVKVFAAGGISSenslktAQRVHRETNGLLKGVIVGRAFLEGILTVE 234
|
|
| hisF |
TIGR00735 |
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ... |
3-203 |
8.46e-32 |
|
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273241 Cd Length: 254 Bit Score: 116.70 E-value: 8.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 3 IFPAIDLKEGRCVRLYQGEFSKETvmnEDPVAQAIIFEKFGAKRLHIVDLDGAVAGESLNLSVIERICKAVRIPVQVGGG 82
Cdd:TIGR00735 6 IIPCLDVRDGRVVKGVQFLNLRDA---GDPVELAQRYDEEGADELVFLDITASSEGRTTMIDVVERTAETVFIPLTVGGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 83 IRSLVAVEKLFSVGVDKVILGTAALYDKTFLEEAVLLY-KEKIIVGIDAKNGFVATRGWLDVS--------EISYIDLAK 153
Cdd:TIGR00735 83 IKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFgSQCIVVAIDAKRVYVNSYCWYEVYiyggrestGLDAVEWAK 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446324427 154 QMEKIGVQTIVFTDISKDGTLGGPNVEQLELLQKSVAIRLIASGGVASIQ 203
Cdd:TIGR00735 163 EVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEAVKIPVIASGGAGKPE 212
|
|
| HisF |
COG0107 |
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ... |
31-204 |
8.76e-30 |
|
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: 111.27 E-value: 8.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 31 DPVAQAIIFEKFGAKRLHIVDLDGAVAGESLNLSVIERICKAVRIPVQVGGGIRSLVAVEKLFSVGVDKVILGTAALYDK 110
Cdd:COG0107 30 DPVELAKRYNEQGADELVFLDITASSEGRKTMLDVVRRVAEEVFIPLTVGGGIRSVEDARRLLRAGADKVSINSAAVKNP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 111 TFLEEAVLLY-KEKIIVGIDAKngFVATRGW------------LDVseisyIDLAKQMEKIGVQTIVFTDISKDGTLGGP 177
Cdd:COG0107 110 ELITEAAERFgSQCIVVAIDAK--RVPDGGWevythggrkptgLDA-----VEWAKEAEELGAGEILLTSMDRDGTKDGY 182
|
170 180
....*....|....*....|....*..
gi 446324427 178 NVEQLELLQKSVAIRLIASGGVASIQD 204
Cdd:COG0107 183 DLELTRAVSEAVSIPVIASGGAGTLEH 209
|
|
| PRK13586 |
PRK13586 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
1-227 |
1.34e-26 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 237439 Cd Length: 232 Bit Score: 102.51 E-value: 1.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 1 MEIFPAIDLKEGRCVRLYQGEFSKETVMNeDPVAQAIIFEKFGAKRLHIVDLDGAvAGESLNLSVIERICKAVRIPVQVG 80
Cdd:PRK13586 2 SKIIPSIDISLGKAVKRIRGVKGTGLILG-NPIEIASKLYNEGYTRIHVVDLDAA-EGVGNNEMYIKEISKIGFDWIQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 81 GGIRSLVAVEKLFSVGVDKVILGTAALYD-KTFLEEAVLLYKEKIIVGID-AKNGFVATRGWLDVSeISYIDLAKQMEKI 158
Cdd:PRK13586 80 GGIRDIEKAKRLLSLDVNALVFSTIVFTNfNLFHDIVREIGSNRVLVSIDyDNTKRVLIRGWKEKS-MEVIDGIKKVNEL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446324427 159 GVQTIVFTDISKDGTLGGPNVEQLELLQKSVAIRLIAsGGVASIQDVKKLNDMNIYGVIIGKALYEKTI 227
Cdd:PRK13586 159 ELLGIIFTYISNEGTTKGIDYNVKDYARLIRGLKEYA-GGVSSDADLEYLKNVGFDYIIVGMAFYLGKL 226
|
|
| PLN02617 |
PLN02617 |
imidazole glycerol phosphate synthase hisHF |
63-198 |
9.87e-08 |
|
imidazole glycerol phosphate synthase hisHF
Pssm-ID: 178226 [Multi-domain] Cd Length: 538 Bit Score: 52.02 E-value: 9.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 63 LSVIERICKAVRIPVQVGGGIR-----------SLVAVEKLFSVGVDKVILGTAALY------------DKTFLEEAVLL 119
Cdd:PLN02617 303 LEVLRRASENVFVPLTVGGGIRdftdangryysSLEVASEYFRSGADKISIGSDAVYaaeeyiasgvktGKTSIEQISRV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 120 Y-KEKIIVGIDAKNGFVAT----------------------------RGWLDVSEISYIDLAKQMEKIGVQTIVFTDISK 170
Cdd:PLN02617 383 YgNQAVVVSIDPRRVYVKDpsdvpfktvkvtnpgpngeeyawyqctvKGGREGRPIGAYELAKAVEELGAGEILLNCIDC 462
|
170 180
....*....|....*....|....*...
gi 446324427 171 DGTLGGPNVEQLELLQKSVAIRLIASGG 198
Cdd:PLN02617 463 DGQGKGFDIELVKLVSDAVTIPVIASSG 490
|
|
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
15-109 |
3.32e-03 |
|
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.
Pssm-ID: 239201 [Multi-domain] Cd Length: 327 Bit Score: 37.94 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 15 VRLYQGEFSKETVMNEDPVAQAIIFEKFGAKRLHI---------VDLDGAVAGESLNLSVIERICKAVRIPVQVGGGIRS 85
Cdd:cd02803 213 VRLSADDFVPGGLTLEEAIEIAKALEEAGVDALHVsggsyesppPIIPPPYVPEGYFLELAEKIKKAVKIPVIAVGGIRD 292
|
90 100
....*....|....*....|....*
gi 446324427 86 LVAVEKLF-SVGVDKVILGTAALYD 109
Cdd:cd02803 293 PEVAEEILaEGKADLVALGRALLAD 317
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
61-109 |
7.70e-03 |
|
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. 1VHN, a putative flavin oxidoreductase, has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present.
Pssm-ID: 239200 [Multi-domain] Cd Length: 231 Bit Score: 36.70 E-value: 7.70e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 446324427 61 LNLSVIERICKAVRIPVQVGGGIRSLVAVEKLFSV-GVDKVILGTAALYD 109
Cdd:cd02801 170 ADWDYIAEIKEAVSIPVIANGDIFSLEDALRCLEQtGVDGVMIGRGALGN 219
|
|
| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
145-222 |
9.37e-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: 36.40 E-value: 9.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446324427 145 EISYIDLAKQMEKIGVQTIV-----FTDISKdgTLGGPNVEQLELLQKSVAIRLIASGGVASIQDVKKLNDMNIYGVIIG 219
Cdd:cd04729 129 DISTLEEALNAAKLGFDIIGttlsgYTEETA--KTEDPDFELLKELRKALGIPVIAEGRINSPEQAAKALELGADAVVVG 206
|
...
gi 446324427 220 KAL 222
Cdd:cd04729 207 SAI 209
|
|
| |
