|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13587 |
PRK13587 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
1-234 |
2.18e-161 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Provisional
Pssm-ID: 172156 Cd Length: 234 Bit Score: 445.43 E-value: 2.18e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 1 MIELWPAIDLIGSTSVRLTEGKYDSEEKMSRSAEESIAYYSQFESVNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIE 80
Cdd:PRK13587 1 MIELWPAIDLIGSTSVRLTEGKYDSEEKMSRSAEESIAYYSQFECVNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 81 VGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGRIYLSVDAYGEDIKVNGWEEDTELNLFSFVRQLSDI 160
Cdd:PRK13587 81 VGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGRIYLSVDAYGEDIKVNGWEEDTELNLFSFVRQLSDI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493891 161 PLGGIIYTDIAKDGKMSGPNFELTGQLVKTTTIPVIASGGIRHQQDIQRLASLNVHAAIIGKAAHQASFWEGLK 234
Cdd:PRK13587 161 PLGGIIYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGGIRHQQDIQRLASLNVHAAIIGKAAHQASFWEGLS 234
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
4-230 |
1.80e-95 |
|
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: 278.70 E-value: 1.80e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 4 LWPAIDLIGSTSVRLTEGKYDSEEKMSRSAEESIAYYSQfESVNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIEVGG 83
Cdd:TIGR00007 1 IIPAIDIKDGKCVRLYQGDYDKETVYGDDPVEAAKKWEE-EGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQVGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 84 GIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTF-PGRIYLSVDAYGEDIKVNGWEEDTELNLFSFVRQLSDIPL 162
Cdd:TIGR00007 80 GIRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYgPERIVVSLDARGGEVAVKGWLEKSEVSLEELAKRLEELGL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493891 163 GGIIYTDIAKDGKMSGPNFELTGQLVKTTTIPVIASGGIRHQQDIQRLASLNVHAAIIGKAAHQASFW 230
Cdd:TIGR00007 160 EGIIYTDISRDGTLSGPNFELTKELVKAVNVPVIASGGVSSIDDLIALKKLGVYGVIVGKALYEGKIT 227
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
3-223 |
1.84e-79 |
|
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: 238.01 E-value: 1.84e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 3 ELWPAIDLIGSTSVRLTEGKYDSEekmSRSAEESIAYYSQFES--VNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIE 80
Cdd:COG0106 1 IIIPAIDLKDGKCVRLVQGDYDQE---TVYSDDPVEVAKRWEDagAEWLHLVDLDGAFAGKPVNLELIEEIAKATGLPVQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 81 VGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGRIYLSVDAYGEDIKVNGWEEDTELNLFSFVRQLSDI 160
Cdd:COG0106 78 VGGGIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFPERIVVGLDARDGKVATDGWQETSGVDLEELAKRFEDA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493891 161 PLGGIIYTDIAKDGKMSGPNFELTGQLVKTTTIPVIASGGIRHQQDIQRLASLNVHAAIIGKA 223
Cdd:COG0106 158 GVAAILYTDISRDGTLQGPNLELYRELAAATGIPVIASGGVSSLDDLRALKELGVEGAIVGKA 220
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
3-229 |
5.51e-79 |
|
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: 236.61 E-value: 5.51e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 3 ELWPAIDLIGSTSVRLTEGKYDSEEKMSRSAEESIAYYsQFESVNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIEVG 82
Cdd:pfam00977 1 RIIPAIDLKDGRVVRLVKGDYFQNTVYAGDPVELAKRY-EEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 83 GGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPG-RIYLSVDAYGEDIKVNGWEEDTELNLFSFVRQLSDIP 161
Cdd:pfam00977 80 GGIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSqCIVVAIDARRGKVAINGWREDTGIDAVEWAKELEELG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493891 162 LGGIIYTDIAKDGKMSGPNFELTGQLVKTTTIPVIASGGIRHQQDIQRLASLNVHAAIIGKAAHQASF 229
Cdd:pfam00977 160 AGEILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELFTEGVDGVIAGSALYEGEI 227
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
3-223 |
1.07e-71 |
|
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: 218.50 E-value: 1.07e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 3 ELWPAIDLIGSTSVRLTEGKYDSEEKMSRSAEEsIAYYSQFESVNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIEVG 82
Cdd:cd04732 1 IIIPAIDLKDGKCVRLYQGDYDKKTVYSDDPVE-VAKKWEEAGAKWLHVVDLDGAKGGEPVNLELIEEIVKAVGIPVQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 83 GGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPG-RIYLSVDAYGEDIKVNGWEEDTELNLFSFVRQLSDIP 161
Cdd:cd04732 80 GGIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGGeRIVVGLDAKDGKVATKGWLETSEVSLEELAKRFEELG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493891 162 LGGIIYTDIAKDGKMSGPNFELTGQLVKTTTIPVIASGGIRHQQDIQRLASLNVHAAIIGKA 223
Cdd:cd04732 160 VKAIIYTDISRDGTLSGPNFELYKELAAATGIPVIASGGVSSLDDIKALKELGVAGVIVGKA 221
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13587 |
PRK13587 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
1-234 |
2.18e-161 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Provisional
Pssm-ID: 172156 Cd Length: 234 Bit Score: 445.43 E-value: 2.18e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 1 MIELWPAIDLIGSTSVRLTEGKYDSEEKMSRSAEESIAYYSQFESVNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIE 80
Cdd:PRK13587 1 MIELWPAIDLIGSTSVRLTEGKYDSEEKMSRSAEESIAYYSQFECVNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 81 VGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGRIYLSVDAYGEDIKVNGWEEDTELNLFSFVRQLSDI 160
Cdd:PRK13587 81 VGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGRIYLSVDAYGEDIKVNGWEEDTELNLFSFVRQLSDI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493891 161 PLGGIIYTDIAKDGKMSGPNFELTGQLVKTTTIPVIASGGIRHQQDIQRLASLNVHAAIIGKAAHQASFWEGLK 234
Cdd:PRK13587 161 PLGGIIYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGGIRHQQDIQRLASLNVHAAIIGKAAHQASFWEGLS 234
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
4-230 |
1.80e-95 |
|
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: 278.70 E-value: 1.80e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 4 LWPAIDLIGSTSVRLTEGKYDSEEKMSRSAEESIAYYSQfESVNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIEVGG 83
Cdd:TIGR00007 1 IIPAIDIKDGKCVRLYQGDYDKETVYGDDPVEAAKKWEE-EGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQVGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 84 GIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTF-PGRIYLSVDAYGEDIKVNGWEEDTELNLFSFVRQLSDIPL 162
Cdd:TIGR00007 80 GIRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYgPERIVVSLDARGGEVAVKGWLEKSEVSLEELAKRLEELGL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493891 163 GGIIYTDIAKDGKMSGPNFELTGQLVKTTTIPVIASGGIRHQQDIQRLASLNVHAAIIGKAAHQASFW 230
Cdd:TIGR00007 160 EGIIYTDISRDGTLSGPNFELTKELVKAVNVPVIASGGVSSIDDLIALKKLGVYGVIVGKALYEGKIT 227
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
3-223 |
1.84e-79 |
|
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: 238.01 E-value: 1.84e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 3 ELWPAIDLIGSTSVRLTEGKYDSEekmSRSAEESIAYYSQFES--VNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIE 80
Cdd:COG0106 1 IIIPAIDLKDGKCVRLVQGDYDQE---TVYSDDPVEVAKRWEDagAEWLHLVDLDGAFAGKPVNLELIEEIAKATGLPVQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 81 VGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGRIYLSVDAYGEDIKVNGWEEDTELNLFSFVRQLSDI 160
Cdd:COG0106 78 VGGGIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFPERIVVGLDARDGKVATDGWQETSGVDLEELAKRFEDA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493891 161 PLGGIIYTDIAKDGKMSGPNFELTGQLVKTTTIPVIASGGIRHQQDIQRLASLNVHAAIIGKA 223
Cdd:COG0106 158 GVAAILYTDISRDGTLQGPNLELYRELAAATGIPVIASGGVSSLDDLRALKELGVEGAIVGKA 220
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
3-229 |
5.51e-79 |
|
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: 236.61 E-value: 5.51e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 3 ELWPAIDLIGSTSVRLTEGKYDSEEKMSRSAEESIAYYsQFESVNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIEVG 82
Cdd:pfam00977 1 RIIPAIDLKDGRVVRLVKGDYFQNTVYAGDPVELAKRY-EEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 83 GGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPG-RIYLSVDAYGEDIKVNGWEEDTELNLFSFVRQLSDIP 161
Cdd:pfam00977 80 GGIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSqCIVVAIDARRGKVAINGWREDTGIDAVEWAKELEELG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493891 162 LGGIIYTDIAKDGKMSGPNFELTGQLVKTTTIPVIASGGIRHQQDIQRLASLNVHAAIIGKAAHQASF 229
Cdd:pfam00977 160 AGEILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELFTEGVDGVIAGSALYEGEI 227
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
3-223 |
1.07e-71 |
|
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: 218.50 E-value: 1.07e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 3 ELWPAIDLIGSTSVRLTEGKYDSEEKMSRSAEEsIAYYSQFESVNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIEVG 82
Cdd:cd04732 1 IIIPAIDLKDGKCVRLYQGDYDKKTVYSDDPVE-VAKKWEEAGAKWLHVVDLDGAKGGEPVNLELIEEIVKAVGIPVQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 83 GGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPG-RIYLSVDAYGEDIKVNGWEEDTELNLFSFVRQLSDIP 161
Cdd:cd04732 80 GGIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGGeRIVVGLDAKDGKVATKGWLETSEVSLEELAKRFEELG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493891 162 LGGIIYTDIAKDGKMSGPNFELTGQLVKTTTIPVIASGGIRHQQDIQRLASLNVHAAIIGKA 223
Cdd:cd04732 160 VKAIIYTDISRDGTLSGPNFELYKELAAATGIPVIASGGVSSLDDIKALKELGVAGVIVGKA 221
|
|
| PRK00748 |
PRK00748 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
3-223 |
4.19e-70 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated
Pssm-ID: 179108 Cd Length: 233 Bit Score: 214.16 E-value: 4.19e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 3 ELWPAIDLIGSTSVRLTEGKYDSEEKMSRS-AEESIAYYSQfeSVNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIEV 81
Cdd:PRK00748 2 IIIPAIDLKDGKCVRLYQGDYDQATVYSDDpVAQAKAWEDQ--GAKWLHLVDLDGAKAGKPVNLELIEAIVKAVDIPVQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 82 GGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGRIYLSVDAYGEDIKVNGWEEDTELNLFSFVRQLSDIP 161
Cdd:PRK00748 80 GGGIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFPGKIVVGLDARDGKVATDGWLETSGVTAEDLAKRFEDAG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493891 162 LGGIIYTDIAKDGKMSGPNFELTGQLVKTTTIPVIASGGIRHQQDIQRLASL-NVHAAIIGKA 223
Cdd:PRK00748 160 VKAIIYTDISRDGTLSGPNVEATRELAAAVPIPVIASGGVSSLDDIKALKGLgAVEGVIVGRA 222
|
|
| PRK04128 |
PRK04128 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
1-226 |
2.88e-31 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 167709 Cd Length: 228 Bit Score: 114.48 E-value: 2.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 1 MIELWPAIDLIGSTSVRLTEGKYDSEEKMSrsaeESIAYYSQF-ESVNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDI 79
Cdd:PRK04128 1 MMRIYPAIDLMNGKAVRLYKGRKEEVKVYG----DPVEIALRFsEYVDKIHVVDLDGAFEGKPKNLDVVKNIIRETGLKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 80 EVGGGIRTKSQIMDYFAAGINYCIVGTKGIqDTDWLKEMAHTFPGrIYLSVDAYGEDIKVNGWEEDTELNLFSFVRQLSD 159
Cdd:PRK04128 77 QVGGGLRTYESIKDAYEIGVENVIIGTKAF-DLEFLEKVTSEFEG-ITVSLDVKGGRIAVKGWLEESSIKVEDAYEMLKN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446493891 160 IpLGGIIYTDIAKDGKMSGpnFELTGQLVKTTTIpvIASGGIRHQQDIQRLASLNVHAAIIGKAAHQ 226
Cdd:PRK04128 155 Y-VNRFIYTSIERDGTLTG--IEEIERFWGDEEF--IYAGGVSSAEDVKKLAEIGFSGVIIGKALYE 216
|
|
| PRK13585 |
PRK13585 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ... |
1-223 |
4.92e-31 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase;
Pssm-ID: 184165 Cd Length: 241 Bit Score: 114.23 E-value: 4.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 1 MIELWPAIDLIGSTSVRLTEGKYDSEeKMSRSAEESIAYYSQFESVNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIE 80
Cdd:PRK13585 2 SFEVIPAVDMKGGKCVQLVQGEPGTE-TVSYGDPVEVAKRWVDAGAETLHLVDLDGAFEGERKNAEAIEKIIEAVGVPVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 81 VGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTF-PGRIYLSVDAYGEDIKVNGWEEDTELNLFSFVRQLSD 159
Cdd:PRK13585 81 LGGGIRSAEDAASLLDLGVDRVILGTAAVENPEIVRELSEEFgSERVMVSLDAKDGEVVIKGWTEKTGYTPVEAAKRFEE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493891 160 IPLGGIIYTDIAKDGKMSGPNFELTGQLVKTTTIPVIASGGIRHQQDIQRLASLNVHAAIIGKA 223
Cdd:PRK13585 161 LGAGSILFTNVDVEGLLEGVNTEPVKELVDSVDIPVIASGGVTTLDDLRALKEAGAAGVVVGSA 224
|
|
| HisA_HisF |
cd04723 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ... |
49-225 |
6.27e-29 |
|
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: 108.51 E-value: 6.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 49 IHIVDLiGAKAQHAREFDYIKSLRRLTTKDIEVGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGRIYL 128
Cdd:cd04723 52 LYIADL-DAIMGRGDNDEAIRELAAAWPLGLWVDGGIRSLENAQEWLKRGASRVIVGTETLPSDDDEDRLAALGEQRLVL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 129 SVDAYGEDIKVNGWEEDTElnlfSFVRQLSDIPlGGIIYTDIAKDGKMSGPNFELTGQLVKTTTIPVIASGGIRHQQDIQ 208
Cdd:cd04723 131 SLDFRGGQLLKPTDFIGPE----ELLRRLAKWP-EELIVLDIDRVGSGQGPDLELLERLAARADIPVIAAGGVRSVEDLE 205
|
170
....*....|....*..
gi 446493891 209 RLASLNVHAAIIGKAAH 225
Cdd:cd04723 206 LLKKLGASGALVASALH 222
|
|
| PRK14024 |
PRK14024 |
phosphoribosyl isomerase A; Provisional |
3-229 |
1.25e-25 |
|
phosphoribosyl isomerase A; Provisional
Pssm-ID: 237589 Cd Length: 241 Bit Score: 100.03 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 3 ELWPAIDLIGSTSVRLTEGKYDSEEKMSRSAEESIAYysQFESVNRIHIVDLiGAKAQHAREFDYIKSLRRLTTKDIEVG 82
Cdd:PRK14024 5 TLLPAVDVVDGQAVRLVQGEAGSETSYGSPLDAALAW--QRDGAEWIHLVDL-DAAFGRGSNRELLAEVVGKLDVKVELS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 83 GGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGRIYLSVDAYGEDIKVNGWEEDTElNLFSFVRQLSDIPL 162
Cdd:PRK14024 82 GGIRDDESLEAALATGCARVNIGTAALENPEWCARVIAEHGDRVAVGLDVRGHTLAARGWTRDGG-DLWEVLERLDSAGC 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 163 GGIIYTDIAKDGKMSGPNFELTGQLVKTTTIPVIASGGIRHQQDIQRLASL---NVHAAIIGKAAHQASF 229
Cdd:PRK14024 161 SRYVVTDVTKDGTLTGPNLELLREVCARTDAPVVASGGVSSLDDLRALAELvplGVEGAIVGKALYAGAF 230
|
|
| PRK14114 |
PRK14114 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
6-233 |
6.18e-21 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 172604 Cd Length: 241 Bit Score: 87.76 E-value: 6.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 6 PAIDLIGSTSVRLTEGKYDSEEKMSRSAEESIAYYSQfESVNRIHIVDLIGAKAQHAREFDYIKSLRRLTtKDIEVGGGI 85
Cdd:PRK14114 5 PAIDLFRGKVARMVKGKKENTIFYEKDPAELVEKLIE-EGFTLIHVVDLSKAIENSVENLPVLEKLSEFA-EHIQIGGGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 86 RTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGRIYlSVDAYGEDIKVNGWEEDTELNLFSFVRQLSDIPLGGI 165
Cdd:PRK14114 83 RSLDYAEKLRKLGYRRQIVSSKVLEDPSFLKFLKEIDVEPVF-SLDTRGGKVAFKGWLAEEEIDPVSLLKRLKEYGLEEI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446493891 166 IYTDIAKDGKMSGPNFELTGQLVKTTTIPVIASGGIRHQQDIQrlASLNVH--------AAIIGKAahqasFWEGL 233
Cdd:PRK14114 162 VHTEIEKDGTLQEHDFSLTRKIAIEAEVKVFAAGGISSENSLK--TAQRVHretngllkGVIVGRA-----FLEGI 230
|
|
| HisF |
cd04731 |
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ... |
81-207 |
1.39e-15 |
|
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: 73.27 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 81 VGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFpGR--IYLSVDAYGEDikVNGWE-------EDTELNLF 151
Cdd:cd04731 76 VGGGIRSLEDARRLLRAGADKVSINSAAVENPELIREIAKRF-GSqcVVVSIDAKRRG--DGGYEvythggrKPTGLDAV 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 446493891 152 SFVRQLSDIPLGGIIYTDIAKDGKMSGPNFELTGQLVKTTTIPVIASGGIRHQQDI 207
Cdd:cd04731 153 EWAKEVEELGAGEILLTSMDRDGTKKGYDLELIRAVSSAVNIPVIASGGAGKPEHF 208
|
|
| PRK13586 |
PRK13586 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
1-228 |
1.49e-14 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 237439 Cd Length: 232 Bit Score: 70.15 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 1 MIELWPAIDLIGSTSVRLTEGKYDSEEKMSRSAEesIAYYSQFESVNRIHIVDLIGAKAQHAREfDYIKSLRRLTTKDIE 80
Cdd:PRK13586 1 MSKIIPSIDISLGKAVKRIRGVKGTGLILGNPIE--IASKLYNEGYTRIHVVDLDAAEGVGNNE-MYIKEISKIGFDWIQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 81 VGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPG-RIYLSVDaYGEDIKV--NGWEEDTeLNLFSFVRQL 157
Cdd:PRK13586 78 VGGGIRDIEKAKRLLSLDVNALVFSTIVFTNFNLFHDIVREIGSnRVLVSID-YDNTKRVliRGWKEKS-MEVIDGIKKV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493891 158 SDIPLGGIIYTDIAKDGKMSGPNFELtGQLVKTTTIPVIASGGIRHQQDIQRLASLNVHAAIIGKAAHQAS 228
Cdd:PRK13586 156 NELELLGIIFTYISNEGTTKGIDYNV-KDYARLIRGLKEYAGGVSSDADLEYLKNVGFDYIIVGMAFYLGK 225
|
|
| hisA-trpF |
TIGR01919 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
4-229 |
4.69e-14 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase/N-(5'phosphoribosyl)anthranilate isomerase; This model represents a bifunctional protein posessing both hisA (1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase) and trpF (N-(5'phosphoribosyl)anthranilate isomerase) activities. Thus, it is involved in both the histidine and tryptophan biosynthetic pathways. Enzymes with this property have been described only in the Actinobacteria (High-GC gram-positive). The enzyme is closely related to the monofunctional HisA proteins (TIGR00007) and in Actinobacteria, the classical monofunctional TrpF is generally absent.
Pssm-ID: 273875 Cd Length: 243 Bit Score: 69.22 E-value: 4.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 4 LWPAIDLIGSTSVRLTEGKydSEEKMSRSAEESIAYYSQFESVNRIHIVDLIGAKAQHAREfDYIKSLRRLTTKDIEVGG 83
Cdd:TIGR01919 5 LLPAVDVNGGAAVRLQQGA--GGSKTYYGSLESAARWWEQGGAEWIHLVDLDAAFGGGNNE-EMLEEVVGLLDVVEELSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 84 GIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGRIYLSVDAY---GEDIKVNGWEEDTELNLFSFVRQLSDI 160
Cdd:TIGR01919 82 GRRDDSSLRAALTGGCARVNGGTAALENPWWAARVIREGGDIVAVGLDVLeigEWHTLGNRGWSDGGGDLEVLERLLDSG 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493891 161 PLGGIIYTDIAKDGKMSGPNFELTGQLVKTTTIPVIASGGIRHQQDIQRLASLN--VHAAIIGKAAHQASF 229
Cdd:TIGR01919 162 GCSRVVVTDSKKDGLLGGPNLLLLAVVAARTDAIVAASGGSSLLDDLRAIKYLDegGVSVAIGGKLLYARF 232
|
|
| hisF |
TIGR00735 |
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ... |
81-200 |
5.55e-13 |
|
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273241 Cd Length: 254 Bit Score: 66.24 E-value: 5.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 81 VGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFpGR--IYLSVDAYGEDIKVNGW--------EEDTELNL 150
Cdd:TIGR00735 79 VGGGIKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRF-GSqcIVVAIDAKRVYVNSYCWyevyiyggRESTGLDA 157
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 446493891 151 FSFVRQLSDIPLGGIIYTDIAKDGKMSGPNFELTGQLVKTTTIPVIASGG 200
Cdd:TIGR00735 158 VEWAKEVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEAVKIPVIASGG 207
|
|
| HisF |
COG0107 |
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ... |
81-200 |
2.05e-12 |
|
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: 64.66 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 81 VGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFpGR--IYLSVDAygedIKV--NGWE-------EDTELN 149
Cdd:COG0107 78 VGGGIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERF-GSqcIVVAIDA----KRVpdGGWEvythggrKPTGLD 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 446493891 150 LFSFVRQLSDIPLGGIIYTDIAKDGKMSGPNFELTGQLVKTTTIPVIASGG 200
Cdd:COG0107 153 AVEWAKEAEELGAGEILLTSMDRDGTKDGYDLELTRAVSEAVSIPVIASGG 203
|
|
| PRK00748 |
PRK00748 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
171-224 |
2.56e-05 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated
Pssm-ID: 179108 Cd Length: 233 Bit Score: 43.90 E-value: 2.56e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 446493891 171 AKDGKMSgpNFELTGQLVKTTTIPVIASGGIRHQQDIQRLASLNVHAAIIGKAA 224
Cdd:PRK00748 55 AKAGKPV--NLELIEAIVKAVDIPVQVGGGIRSLETVEALLDAGVSRVIIGTAA 106
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
169-224 |
1.68e-04 |
|
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: 41.31 E-value: 1.68e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 446493891 169 DIAKDGKMSgpNFELTGQLVKTTTIPVIASGGIRHQQDIQRLASLNVHAAIIGKAA 224
Cdd:cd04732 52 DGAKGGEPV--NLELIEEIVKAVGIPVQVGGGIRSLEDIERLLDLGVSRVIIGTAA 105
|
|
| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
167-223 |
2.56e-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: 41.02 E-value: 2.56e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 446493891 167 YTDIAKdgKMSGPNFELTGQLVKTTTIPVIASGGIRHQQDIQRLASLNVHAAIIGKA 223
Cdd:cd04729 154 YTEETA--KTEDPDFELLKELRKALGIPVIAEGRINSPEQAAKALELGADAVVVGSA 208
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
171-224 |
3.84e-04 |
|
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: 40.41 E-value: 3.84e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 446493891 171 AKDGKMSgpNFELTGQLVKTTTIPVIASGGIRHQQDIQRLASLNVHAAIIGKAA 224
Cdd:COG0106 54 AFAGKPV--NLELIEEIAKATGLPVQVGGGIRSLEDIERLLDAGASRVILGTAA 105
|
|
| PRK01130 |
PRK01130 |
putative N-acetylmannosamine-6-phosphate 2-epimerase; |
167-223 |
4.20e-04 |
|
putative N-acetylmannosamine-6-phosphate 2-epimerase;
Pssm-ID: 234907 Cd Length: 221 Bit Score: 40.13 E-value: 4.20e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 446493891 167 YTDIAKdgKMSGPNFELTGQLVKTTTIPVIASGGIRHQQDIQRLASLNVHAAIIGKA 223
Cdd:PRK01130 150 YTEETK--KPEEPDFALLKELLKAVGCPVIAEGRINTPEQAKKALELGAHAVVVGGA 204
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
141-224 |
1.72e-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: 38.63 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 141 GWEEDTelNLFSFVRQLSDIPLGGII---------YTDIAkdgkmsgpNFELTGQLVKTTTIPVIASGGIRHQQDIQRLA 211
Cdd:cd02801 133 GWDDEE--ETLELAKALEDAGASALTvhgrtreqrYSGPA--------DWDYIAEIKEAVSIPVIANGDIFSLEDALRCL 202
|
90
....*....|....
gi 446493891 212 SL-NVHAAIIGKAA 224
Cdd:cd02801 203 EQtGVDGVMIGRGA 216
|
|
| Dus |
pfam01207 |
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
130-224 |
5.68e-03 |
|
Dihydrouridine synthase (Dus); 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 archae. 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. Dus 1 from Saccharomyces cerevisiae acts on pre-tRNA-Phe, while Dus 2 acts on pre-tRNA-Tyr and pre-tRNA-Leu. Dus 1 is active as a single subunit, requiring NADPH or NADH, and is stimulated by the presence of FAD. Some family members may be targeted to the mitochondria and even have a role in mitochondria.
Pssm-ID: 426126 Cd Length: 309 Bit Score: 37.31 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493891 130 VDAYgeDIKVN-----GWEeDTELNLFSFVRQLSDiplGGIiyTDIAKDGKMSGPNFELT------GQLVKTTTIPVIAS 198
Cdd:pfam01207 118 VKAV--GIPVTvkiriGWD-DSHENAVEIAKIVED---AGA--QALTVHGRTRAQNYEGTadwdaiKQVKQAVSIPVIAN 189
|
90 100
....*....|....*....|....*..
gi 446493891 199 GGIRHQQDIQR-LASLNVHAAIIGKAA 224
Cdd:pfam01207 190 GDITDPEDAQRcLAYTGADGVMIGRGA 216
|
|
| |
