|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13587 |
PRK13587 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
1-234 |
4.34e-164 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Provisional
Pssm-ID: 172156 Cd Length: 234 Bit Score: 452.36 E-value: 4.34e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 1 MIELWPAIDLIGSTSVRLTEGKYDSEEKMSRSAEESIAYYSQFECVNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIE 80
Cdd:PRK13587 1 MIELWPAIDLIGSTSVRLTEGKYDSEEKMSRSAEESIAYYSQFECVNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 81 VGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGRIYLSVDAYGEDIKVNGWEEDTELNLFSFVRRLSDI 160
Cdd:PRK13587 81 VGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGRIYLSVDAYGEDIKVNGWEEDTELNLFSFVRQLSDI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 88196627 161 PLGGIIYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGGIRHQQDIQRLASLNVHAAIIGKAAHQASFWEGLK 234
Cdd:PRK13587 161 PLGGIIYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGGIRHQQDIQRLASLNVHAAIIGKAAHQASFWEGLS 234
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
4-230 |
2.67e-97 |
|
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: 283.32 E-value: 2.67e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 4 LWPAIDLIGSTSVRLTEGKYDSEEKMSRSAEESIAYYSQfECVNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIEVGG 83
Cdd:TIGR00007 1 IIPAIDIKDGKCVRLYQGDYDKETVYGDDPVEAAKKWEE-EGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQVGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 84 GIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTF-PGRIYLSVDAYGEDIKVNGWEEDTELNLFSFVRRLSDIPL 162
Cdd:TIGR00007 80 GIRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYgPERIVVSLDARGGEVAVKGWLEKSEVSLEELAKRLEELGL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 88196627 163 GGIIYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGGIRHQQDIQRLASLNVHAAIIGKAAHQASFW 230
Cdd:TIGR00007 160 EGIIYTDISRDGTLSGPNFELTKELVKAVNVPVIASGGVSSIDDLIALKKLGVYGVIVGKALYEGKIT 227
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
3-229 |
1.99e-80 |
|
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: 240.46 E-value: 1.99e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 3 ELWPAIDLIGSTSVRLTEGKYDSEEKMSRSAEESIAYYsQFECVNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIEVG 82
Cdd:pfam00977 1 RIIPAIDLKDGRVVRLVKGDYFQNTVYAGDPVELAKRY-EEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 83 GGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPG-RIYLSVDAYGEDIKVNGWEEDTELNLFSFVRRLSDIP 161
Cdd:pfam00977 80 GGIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSqCIVVAIDARRGKVAINGWREDTGIDAVEWAKELEELG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 88196627 162 LGGIIYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGGIRHQQDIQRLASLNVHAAIIGKAAHQASF 229
Cdd:pfam00977 160 AGEILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELFTEGVDGVIAGSALYEGEI 227
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
3-223 |
1.28e-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: 238.40 E-value: 1.28e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 3 ELWPAIDLIGSTSVRLTEGKYDSEekmSRSAEESIAYYSQFE--CVNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIE 80
Cdd:COG0106 1 IIIPAIDLKDGKCVRLVQGDYDQE---TVYSDDPVEVAKRWEdaGAEWLHLVDLDGAFAGKPVNLELIEEIAKATGLPVQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 81 VGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGRIYLSVDAYGEDIKVNGWEEDTELNLFSFVRRLSDI 160
Cdd:COG0106 78 VGGGIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFPERIVVGLDARDGKVATDGWQETSGVDLEELAKRFEDA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 88196627 161 PLGGIIYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGGIRHQQDIQRLASLNVHAAIIGKA 223
Cdd:COG0106 158 GVAAILYTDISRDGTLQGPNLELYRELAAATGIPVIASGGVSSLDDLRALKELGVEGAIVGKA 220
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
3-223 |
2.70e-72 |
|
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: 220.04 E-value: 2.70e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 3 ELWPAIDLIGSTSVRLTEGKYDSEE-------KMSRSAEESIAyysqfecvNRIHIVDLIGAKAQHAREFDYIKSLRRLT 75
Cdd:cd04732 1 IIIPAIDLKDGKCVRLYQGDYDKKTvysddpvEVAKKWEEAGA--------KWLHVVDLDGAKGGEPVNLELIEEIVKAV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 76 TKDIEVGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPG-RIYLSVDAYGEDIKVNGWEEDTELNLFSFV 154
Cdd:cd04732 73 GIPVQVGGGIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGGeRIVVGLDAKDGKVATKGWLETSEVSLEELA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 88196627 155 RRLSDIPLGGIIYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGGIRHQQDIQRLASLNVHAAIIGKA 223
Cdd:cd04732 153 KRFEELGVKAIIYTDISRDGTLSGPNFELYKELAAATGIPVIASGGVSSLDDIKALKELGVAGVIVGKA 221
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13587 |
PRK13587 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
1-234 |
4.34e-164 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Provisional
Pssm-ID: 172156 Cd Length: 234 Bit Score: 452.36 E-value: 4.34e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 1 MIELWPAIDLIGSTSVRLTEGKYDSEEKMSRSAEESIAYYSQFECVNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIE 80
Cdd:PRK13587 1 MIELWPAIDLIGSTSVRLTEGKYDSEEKMSRSAEESIAYYSQFECVNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 81 VGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGRIYLSVDAYGEDIKVNGWEEDTELNLFSFVRRLSDI 160
Cdd:PRK13587 81 VGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGRIYLSVDAYGEDIKVNGWEEDTELNLFSFVRQLSDI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 88196627 161 PLGGIIYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGGIRHQQDIQRLASLNVHAAIIGKAAHQASFWEGLK 234
Cdd:PRK13587 161 PLGGIIYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGGIRHQQDIQRLASLNVHAAIIGKAAHQASFWEGLS 234
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
4-230 |
2.67e-97 |
|
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: 283.32 E-value: 2.67e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 4 LWPAIDLIGSTSVRLTEGKYDSEEKMSRSAEESIAYYSQfECVNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIEVGG 83
Cdd:TIGR00007 1 IIPAIDIKDGKCVRLYQGDYDKETVYGDDPVEAAKKWEE-EGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQVGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 84 GIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTF-PGRIYLSVDAYGEDIKVNGWEEDTELNLFSFVRRLSDIPL 162
Cdd:TIGR00007 80 GIRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYgPERIVVSLDARGGEVAVKGWLEKSEVSLEELAKRLEELGL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 88196627 163 GGIIYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGGIRHQQDIQRLASLNVHAAIIGKAAHQASFW 230
Cdd:TIGR00007 160 EGIIYTDISRDGTLSGPNFELTKELVKAVNVPVIASGGVSSIDDLIALKKLGVYGVIVGKALYEGKIT 227
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
3-229 |
1.99e-80 |
|
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: 240.46 E-value: 1.99e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 3 ELWPAIDLIGSTSVRLTEGKYDSEEKMSRSAEESIAYYsQFECVNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIEVG 82
Cdd:pfam00977 1 RIIPAIDLKDGRVVRLVKGDYFQNTVYAGDPVELAKRY-EEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 83 GGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPG-RIYLSVDAYGEDIKVNGWEEDTELNLFSFVRRLSDIP 161
Cdd:pfam00977 80 GGIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSqCIVVAIDARRGKVAINGWREDTGIDAVEWAKELEELG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 88196627 162 LGGIIYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGGIRHQQDIQRLASLNVHAAIIGKAAHQASF 229
Cdd:pfam00977 160 AGEILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELFTEGVDGVIAGSALYEGEI 227
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
3-223 |
1.28e-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: 238.40 E-value: 1.28e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 3 ELWPAIDLIGSTSVRLTEGKYDSEekmSRSAEESIAYYSQFE--CVNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIE 80
Cdd:COG0106 1 IIIPAIDLKDGKCVRLVQGDYDQE---TVYSDDPVEVAKRWEdaGAEWLHLVDLDGAFAGKPVNLELIEEIAKATGLPVQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 81 VGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGRIYLSVDAYGEDIKVNGWEEDTELNLFSFVRRLSDI 160
Cdd:COG0106 78 VGGGIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFPERIVVGLDARDGKVATDGWQETSGVDLEELAKRFEDA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 88196627 161 PLGGIIYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGGIRHQQDIQRLASLNVHAAIIGKA 223
Cdd:COG0106 158 GVAAILYTDISRDGTLQGPNLELYRELAAATGIPVIASGGVSSLDDLRALKELGVEGAIVGKA 220
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
3-223 |
2.70e-72 |
|
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: 220.04 E-value: 2.70e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 3 ELWPAIDLIGSTSVRLTEGKYDSEE-------KMSRSAEESIAyysqfecvNRIHIVDLIGAKAQHAREFDYIKSLRRLT 75
Cdd:cd04732 1 IIIPAIDLKDGKCVRLYQGDYDKKTvysddpvEVAKKWEEAGA--------KWLHVVDLDGAKGGEPVNLELIEEIVKAV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 76 TKDIEVGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPG-RIYLSVDAYGEDIKVNGWEEDTELNLFSFV 154
Cdd:cd04732 73 GIPVQVGGGIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGGeRIVVGLDAKDGKVATKGWLETSEVSLEELA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 88196627 155 RRLSDIPLGGIIYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGGIRHQQDIQRLASLNVHAAIIGKA 223
Cdd:cd04732 153 KRFEELGVKAIIYTDISRDGTLSGPNFELYKELAAATGIPVIASGGVSSLDDIKALKELGVAGVIVGKA 221
|
|
| PRK00748 |
PRK00748 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
3-223 |
8.92e-71 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated
Pssm-ID: 179108 Cd Length: 233 Bit Score: 216.09 E-value: 8.92e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 3 ELWPAIDLIGSTSVRLTEGKYDSEEKMSRS-AEESIAYYSQ-FEcvnRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIE 80
Cdd:PRK00748 2 IIIPAIDLKDGKCVRLYQGDYDQATVYSDDpVAQAKAWEDQgAK---WLHLVDLDGAKAGKPVNLELIEAIVKAVDIPVQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 81 VGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGRIYLSVDAYGEDIKVNGWEEDTELNLFSFVRRLSDI 160
Cdd:PRK00748 79 VGGGIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFPGKIVVGLDARDGKVATDGWLETSGVTAEDLAKRFEDA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 88196627 161 PLGGIIYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGGIRHQQDIQRLASL-NVHAAIIGKA 223
Cdd:PRK00748 159 GVKAIIYTDISRDGTLSGPNVEATRELAAAVPIPVIASGGVSSLDDIKALKGLgAVEGVIVGRA 222
|
|
| PRK13585 |
PRK13585 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ... |
1-223 |
1.34e-32 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase;
Pssm-ID: 184165 Cd Length: 241 Bit Score: 118.47 E-value: 1.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 1 MIELWPAIDLIGSTSVRLTEGKYDSEekmsrsaeeSIAYYSQFECVNR--------IHIVDLIGAKAQHAREFDYIKSLR 72
Cdd:PRK13585 2 SFEVIPAVDMKGGKCVQLVQGEPGTE---------TVSYGDPVEVAKRwvdagaetLHLVDLDGAFEGERKNAEAIEKII 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 73 RLTTKDIEVGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTF-PGRIYLSVDAYGEDIKVNGWEEDTELNLF 151
Cdd:PRK13585 73 EAVGVPVQLGGGIRSAEDAASLLDLGVDRVILGTAAVENPEIVRELSEEFgSERVMVSLDAKDGEVVIKGWTEKTGYTPV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 88196627 152 SFVRRLSDIPLGGIIYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGGIRHQQDIQRLASLNVHAAIIGKA 223
Cdd:PRK13585 153 EAAKRFEELGAGSILFTNVDVEGLLEGVNTEPVKELVDSVDIPVIASGGVTTLDDLRALKEAGAAGVVVGSA 224
|
|
| PRK04128 |
PRK04128 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
1-226 |
5.06e-31 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 167709 Cd Length: 228 Bit Score: 114.10 E-value: 5.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 1 MIELWPAIDLIGSTSVRLTEGKYDSEEKMSrsaeESIAYYSQF-ECVNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDI 79
Cdd:PRK04128 1 MMRIYPAIDLMNGKAVRLYKGRKEEVKVYG----DPVEIALRFsEYVDKIHVVDLDGAFEGKPKNLDVVKNIIRETGLKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 80 EVGGGIRTKSQIMDYFAAGINYCIVGTKGIqDTDWLKEMAHTFPGrIYLSVDAYGEDIKVNGWEEDTELNLFSFVRRLSD 159
Cdd:PRK04128 77 QVGGGLRTYESIKDAYEIGVENVIIGTKAF-DLEFLEKVTSEFEG-ITVSLDVKGGRIAVKGWLEESSIKVEDAYEMLKN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 88196627 160 IpLGGIIYTDIAKDGKMSGpnFELTGQLVKATTIpvIASGGIRHQQDIQRLASLNVHAAIIGKAAHQ 226
Cdd:PRK04128 155 Y-VNRFIYTSIERDGTLTG--IEEIERFWGDEEF--IYAGGVSSAEDVKKLAEIGFSGVIIGKALYE 216
|
|
| HisA_HisF |
cd04723 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ... |
49-225 |
3.46e-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: 109.28 E-value: 3.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 49 IHIVDLiGAKAQHAREFDYIKSLRRLTTKDIEVGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGRIYL 128
Cdd:cd04723 52 LYIADL-DAIMGRGDNDEAIRELAAAWPLGLWVDGGIRSLENAQEWLKRGASRVIVGTETLPSDDDEDRLAALGEQRLVL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 129 SVDAYGEDIKVNGWEEDTElnlfSFVRRLSDIPlGGIIYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGGIRHQQDIQ 208
Cdd:cd04723 131 SLDFRGGQLLKPTDFIGPE----ELLRRLAKWP-EELIVLDIDRVGSGQGPDLELLERLAARADIPVIAAGGVRSVEDLE 205
|
170
....*....|....*..
gi 88196627 209 RLASLNVHAAIIGKAAH 225
Cdd:cd04723 206 LLKKLGASGALVASALH 222
|
|
| PRK14024 |
PRK14024 |
phosphoribosyl isomerase A; Provisional |
3-229 |
4.51e-27 |
|
phosphoribosyl isomerase A; Provisional
Pssm-ID: 237589 Cd Length: 241 Bit Score: 103.88 E-value: 4.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 3 ELWPAIDLIGSTSVRLTEGKYDSEEKMSRSAEESIAYysQFECVNRIHIVDLiGAKAQHAREFDYIKSLRRLTTKDIEVG 82
Cdd:PRK14024 5 TLLPAVDVVDGQAVRLVQGEAGSETSYGSPLDAALAW--QRDGAEWIHLVDL-DAAFGRGSNRELLAEVVGKLDVKVELS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 83 GGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGRIYLSVDAYGEDIKVNGWEEDTElNLFSFVRRLSDIPL 162
Cdd:PRK14024 82 GGIRDDESLEAALATGCARVNIGTAALENPEWCARVIAEHGDRVAVGLDVRGHTLAARGWTRDGG-DLWEVLERLDSAGC 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 163 GGIIYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGGIRHQQDIQRLASL---NVHAAIIGKAAHQASF 229
Cdd:PRK14024 161 SRYVVTDVTKDGTLTGPNLELLREVCARTDAPVVASGGVSSLDDLRALAELvplGVEGAIVGKALYAGAF 230
|
|
| PRK14114 |
PRK14114 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
6-233 |
2.19e-21 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 172604 Cd Length: 241 Bit Score: 88.92 E-value: 2.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 6 PAIDLIGSTSVRLTEGKYDSEEKMSRSAEESIAYYSQfECVNRIHIVDLIGAKAQHAREFDYIKSLRRLTtKDIEVGGGI 85
Cdd:PRK14114 5 PAIDLFRGKVARMVKGKKENTIFYEKDPAELVEKLIE-EGFTLIHVVDLSKAIENSVENLPVLEKLSEFA-EHIQIGGGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 86 RTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGRIYlSVDAYGEDIKVNGWEEDTELNLFSFVRRLSDIPLGGI 165
Cdd:PRK14114 83 RSLDYAEKLRKLGYRRQIVSSKVLEDPSFLKFLKEIDVEPVF-SLDTRGGKVAFKGWLAEEEIDPVSLLKRLKEYGLEEI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 88196627 166 IYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGGIRHQQDIQrlASLNVH--------AAIIGKAahqasFWEGL 233
Cdd:PRK14114 162 VHTEIEKDGTLQEHDFSLTRKIAIEAEVKVFAAGGISSENSLK--TAQRVHretngllkGVIVGRA-----FLEGI 230
|
|
| HisF |
cd04731 |
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ... |
81-207 |
2.24e-16 |
|
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: 75.19 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 81 VGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFpGR--IYLSVDAYGEDikVNGWE-------EDTELNLF 151
Cdd:cd04731 76 VGGGIRSLEDARRLLRAGADKVSINSAAVENPELIREIAKRF-GSqcVVVSIDAKRRG--DGGYEvythggrKPTGLDAV 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 88196627 152 SFVRRLSDIPLGGIIYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGGIRHQQDI 207
Cdd:cd04731 153 EWAKEVEELGAGEILLTSMDRDGTKKGYDLELIRAVSSAVNIPVIASGGAGKPEHF 208
|
|
| hisA-trpF |
TIGR01919 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
4-229 |
2.08e-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: 69.99 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 4 LWPAIDLIGSTSVRLTEGKydSEEKMSRSAEESIAYYSQFECVNRIHIVDLIGAKAQHAREfDYIKSLRRLTTKDIEVGG 83
Cdd:TIGR01919 5 LLPAVDVNGGAAVRLQQGA--GGSKTYYGSLESAARWWEQGGAEWIHLVDLDAAFGGGNNE-EMLEEVVGLLDVVEELSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 84 GIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGRIYLSVDAY---GEDIKVNGWEEDTELNLFSFVRRLSDI 160
Cdd:TIGR01919 82 GRRDDSSLRAALTGGCARVNGGTAALENPWWAARVIREGGDIVAVGLDVLeigEWHTLGNRGWSDGGGDLEVLERLLDSG 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 88196627 161 PLGGIIYTDIAKDGKMSGPNFELTgQLVKATTIPVIASGGIRHQQDIQRLASLNVH---AAIIGKAAHQASF 229
Cdd:TIGR01919 162 GCSRVVVTDSKKDGLLGGPNLLLL-AVVAARTDAIVAASGGSSLLDDLRAIKYLDEggvSVAIGGKLLYARF 232
|
|
| PRK13586 |
PRK13586 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
1-228 |
3.02e-14 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 237439 Cd Length: 232 Bit Score: 69.38 E-value: 3.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 1 MIELWPAIDLIGSTSVRLTEGKYDSEEKMSRSAEesIAYYSQFECVNRIHIVDLIGAKAQHAREfDYIKSLRRLTTKDIE 80
Cdd:PRK13586 1 MSKIIPSIDISLGKAVKRIRGVKGTGLILGNPIE--IASKLYNEGYTRIHVVDLDAAEGVGNNE-MYIKEISKIGFDWIQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 81 VGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPG-RIYLSVDaYGEDIKV--NGWEEDTeLNLFSFVRRL 157
Cdd:PRK13586 78 VGGGIRDIEKAKRLLSLDVNALVFSTIVFTNFNLFHDIVREIGSnRVLVSID-YDNTKRVliRGWKEKS-MEVIDGIKKV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 88196627 158 SDIPLGGIIYTDIAKDGKMSGPNFELtGQLVKATTIPVIASGGIRHQQDIQRLASLNVHAAIIGKAAHQAS 228
Cdd:PRK13586 156 NELELLGIIFTYISNEGTTKGIDYNV-KDYARLIRGLKEYAGGVSSDADLEYLKNVGFDYIIVGMAFYLGK 225
|
|
| hisF |
TIGR00735 |
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ... |
81-200 |
6.17e-14 |
|
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273241 Cd Length: 254 Bit Score: 68.93 E-value: 6.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 81 VGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFpGR--IYLSVDAYGEDIKVNGW--------EEDTELNL 150
Cdd:TIGR00735 79 VGGGIKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRF-GSqcIVVAIDAKRVYVNSYCWyevyiyggRESTGLDA 157
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 88196627 151 FSFVRRLSDIPLGGIIYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGG 200
Cdd:TIGR00735 158 VEWAKEVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEAVKIPVIASGG 207
|
|
| HisF |
COG0107 |
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ... |
81-200 |
2.48e-13 |
|
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: 66.97 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 81 VGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFpGR--IYLSVDAygedIKV--NGWE-------EDTELN 149
Cdd:COG0107 78 VGGGIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERF-GSqcIVVAIDA----KRVpdGGWEvythggrKPTGLD 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 88196627 150 LFSFVRRLSDIPLGGIIYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGG 200
Cdd:COG0107 153 AVEWAKEAEELGAGEILLTSMDRDGTKDGYDLELTRAVSEAVSIPVIASGG 203
|
|
| PRK00748 |
PRK00748 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
171-224 |
1.04e-05 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated
Pssm-ID: 179108 Cd Length: 233 Bit Score: 45.06 E-value: 1.04e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 88196627 171 AKDGKMSgpNFELTGQLVKATTIPVIASGGIRHQQDIQRLASLNVHAAIIGKAA 224
Cdd:PRK00748 55 AKAGKPV--NLELIEAIVKAVDIPVQVGGGIRSLETVEALLDAGVSRVIIGTAA 106
|
|
| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
167-223 |
4.34e-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: 42.95 E-value: 4.34e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 88196627 167 YTDIAKdgKMSGPNFELTGQLVKATTIPVIASGGIRHQQDIQRLASLNVHAAIIGKA 223
Cdd:cd04729 154 YTEETA--KTEDPDFELLKELRKALGIPVIAEGRINSPEQAAKALELGADAVVVGSA 208
|
|
| PRK01130 |
PRK01130 |
putative N-acetylmannosamine-6-phosphate 2-epimerase; |
167-223 |
5.76e-05 |
|
putative N-acetylmannosamine-6-phosphate 2-epimerase;
Pssm-ID: 234907 Cd Length: 221 Bit Score: 42.83 E-value: 5.76e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 88196627 167 YTDIAKdgKMSGPNFELTGQLVKATTIPVIASGGIRHQQDIQRLASLNVHAAIIGKA 223
Cdd:PRK01130 150 YTEETK--KPEEPDFALLKELLKAVGCPVIAEGRINTPEQAKKALELGAHAVVVGGA 204
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
169-224 |
9.09e-05 |
|
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: 42.47 E-value: 9.09e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 88196627 169 DIAKDGKMSgpNFELTGQLVKATTIPVIASGGIRHQQDIQRLASLNVHAAIIGKAA 224
Cdd:cd04732 52 DGAKGGEPV--NLELIEEIVKAVGIPVQVGGGIRSLEDIERLLDLGVSRVIIGTAA 105
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
171-224 |
1.81e-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: 41.56 E-value: 1.81e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 88196627 171 AKDGKMSgpNFELTGQLVKATTIPVIASGGIRHQQDIQRLASLNVHAAIIGKAA 224
Cdd:COG0106 54 AFAGKPV--NLELIEEIAKATGLPVQVGGGIRSLEDIERLLDAGASRVILGTAA 105
|
|
| Dus |
pfam01207 |
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
130-224 |
2.23e-04 |
|
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: 41.54 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 130 VDAYgeDIKVN-----GWEeDTELNLFSFVRRLSDiplGGIiyTDIAKDGKMSGPNFELT------GQLVKATTIPVIAS 198
Cdd:pfam01207 118 VKAV--GIPVTvkiriGWD-DSHENAVEIAKIVED---AGA--QALTVHGRTRAQNYEGTadwdaiKQVKQAVSIPVIAN 189
|
90 100
....*....|....*....|....*..
gi 88196627 199 GGIRHQQDIQR-LASLNVHAAIIGKAA 224
Cdd:pfam01207 190 GDITDPEDAQRcLAYTGADGVMIGRGA 216
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
141-224 |
3.08e-04 |
|
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: 40.56 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 141 GWEEDTelNLFSFVRRLSDIPLGGII---------YTDIAkdgkmsgpNFELTGQLVKATTIPVIASGGIRHQQDIQRLA 211
Cdd:cd02801 133 GWDDEE--ETLELAKALEDAGASALTvhgrtreqrYSGPA--------DWDYIAEIKEAVSIPVIANGDIFSLEDALRCL 202
|
90
....*....|....
gi 88196627 212 SL-NVHAAIIGKAA 224
Cdd:cd02801 203 EQtGVDGVMIGRGA 216
|
|
| DusA |
COG0042 |
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
141-224 |
1.13e-03 |
|
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; tRNA-dihydrouridine synthase is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 439812 [Multi-domain] Cd Length: 310 Bit Score: 39.31 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196627 141 GWEEDtELNLFSFVRRLSDIPLGGII---------YtdiakdgkmSGP-NFELTGQLVKATTIPVIASGGIRHQQDIQR- 209
Cdd:COG0042 140 GWDDD-DENALEFARIAEDAGAAALTvhgrtreqrY---------KGPaDWDAIARVKEAVSIPVIGNGDIFSPEDAKRm 209
|
90
....*....|....*
gi 88196627 210 LASLNVHAAIIGKAA 224
Cdd:COG0042 210 LEETGCDGVMIGRGA 224
|
|
| |
