|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14024 |
PRK14024 |
phosphoribosyl isomerase A; Provisional |
1-245 |
1.53e-162 |
|
phosphoribosyl isomerase A; Provisional
Pssm-ID: 237589 Cd Length: 241 Bit Score: 449.02 E-value: 1.53e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 1 MMPLILLPAVDVVEGRAVRLVQGKAGSQTEYGSAVDAALGWQRDGAEWIHLVDLDAAFGRGSNHELLAEVVGKLDVQVEL 80
Cdd:PRK14024 1 TMSLTLLPAVDVVDGQAVRLVQGEAGSETSYGSPLDAALAWQRDGAEWIHLVDLDAAFGRGSNRELLAEVVGKLDVKVEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 81 SGGIRDDESLAAALATGCARVNVGTAALENPQWCARVIGEHGDQVAVGLDVqiidGEHRLRGRGWETDGGDLWDVLERLD 160
Cdd:PRK14024 81 SGGIRDDESLEAALATGCARVNIGTAALENPEWCARVIAEHGDRVAVGLDV----RGHTLAARGWTRDGGDLWEVLERLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 161 SEGCSRFVVTDITKDGTLGGPNLDLLAGVADRTDAPVIASGGVSSLDDLRAIATLTHRGVEGAIVGKALYARRFTLPQAL 240
Cdd:PRK14024 157 SAGCSRYVVTDVTKDGTLTGPNLELLREVCARTDAPVVASGGVSSLDDLRALAELVPLGVEGAIVGKALYAGAFTLPEAL 236
|
....*
gi 15608741 241 AAVRD 245
Cdd:PRK14024 237 AVVRR 241
|
|
| hisA-trpF |
TIGR01919 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
2-244 |
6.80e-115 |
|
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: 328.84 E-value: 6.80e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 2 MPLILLPAVDVVEGRAVRLVQGKAGSQTEYGSAVDAALGWQRDGAEWIHLVDLDAAFGRGSNHELLAEVVGKLDVQVELS 81
Cdd:TIGR01919 1 MPLILLPAVDVNGGAAVRLQQGAGGSKTYYGSLESAARWWEQGGAEWIHLVDLDAAFGGGNNEEMLEEVVGLLDVVEELS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 82 GGIRDDESLAAALATGCARVNVGTAALENPQWCARVIGEHGDQVAVGLDVQIIDGEHRLRGRGWETDGGDLWDVLERLDS 161
Cdd:TIGR01919 81 GGRRDDSSLRAALTGGCARVNGGTAALENPWWAARVIREGGDIVAVGLDVLEIGEWHTLGNRGWSDGGGDLEVLERLLDS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 162 EGCSRFVVTDITKDGTLGGPNLDLLAGVADRTDAPVIASGGVSSLDDLRAIATLTHRGVEGAIVGKALYARRFTLPQALA 241
Cdd:TIGR01919 161 GGCSRVVVTDSKKDGLLGGPNLLLLAVVAARTDAIVAASGGSSLLDDLRAIKYLDEGGVSVAIGGKLLYARFFTLEAALA 240
|
...
gi 15608741 242 AVR 244
Cdd:TIGR01919 241 VEK 243
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
5-244 |
8.15e-101 |
|
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: 292.71 E-value: 8.15e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 5 ILLPAVDVVEGRAVRLVQGKAGSQTEYG-SAVDAALGWQRDGAEWIHLVDLDAAF-GRGSNHELLAEVVGKLDVQVELSG 82
Cdd:COG0106 1 IIIPAIDLKDGKCVRLVQGDYDQETVYSdDPVEVAKRWEDAGAEWLHLVDLDGAFaGKPVNLELIEEIAKATGLPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 83 GIRDDESLAAALATGCARVNVGTAALENPQWCARVIGEHGDQVAVGLDVQiidgEHRLRGRGWETDGG-DLWDVLERLDS 161
Cdd:COG0106 81 GIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFPERIVVGLDAR----DGKVATDGWQETSGvDLEELAKRFED 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 162 EGCSRFVVTDITKDGTLGGPNLDLLAGVADRTDAPVIASGGVSSLDDLRAIATLthrGVEGAIVGKALYARRFTLPQALA 241
Cdd:COG0106 157 AGVAAILYTDISRDGTLQGPNLELYRELAAATGIPVIASGGVSSLDDLRALKEL---GVEGAIVGKALYEGKIDLEEALA 233
|
...
gi 15608741 242 AVR 244
Cdd:COG0106 234 LAR 236
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
5-241 |
9.00e-90 |
|
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: 264.73 E-value: 9.00e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 5 ILLPAVDVVEGRAVRLVQGKAGSQTEY-GSAVDAALGWQRDGAEWIHLVDLDAAF-GRGSNHELLAEVVGKLDVQVELSG 82
Cdd:cd04732 1 IIIPAIDLKDGKCVRLYQGDYDKKTVYsDDPVEVAKKWEEAGAKWLHVVDLDGAKgGEPVNLELIEEIVKAVGIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 83 GIRDDESLAAALATGCARVNVGTAALENPQWCARVIGEHG-DQVAVGLDVqiIDGEHRLRGrGWETDGGDLWDVLERLDS 161
Cdd:cd04732 81 GIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGgERIVVGLDA--KDGKVATKG-WLETSEVSLEELAKRFEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 162 EGCSRFVVTDITKDGTLGGPNLDLLAGVADRTDAPVIASGGVSSLDDLRAIATLthrGVEGAIVGKALYARRFTLPQALA 241
Cdd:cd04732 158 LGVKAIIYTDISRDGTLSGPNFELYKELAAATGIPVIASGGVSSLDDIKALKEL---GVAGVIVGKALYEGKITLEEALA 234
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
5-235 |
2.29e-72 |
|
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: 220.43 E-value: 2.29e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 5 ILLPAVDVVEGRAVRLVQGKAGSQTEY-GSAVDAALGWQRDGAEWIHLVDLDAAF-GRGSNHELLAEVVGKLDVQVELSG 82
Cdd:pfam00977 1 RIIPAIDLKDGRVVRLVKGDYFQNTVYaGDPVELAKRYEEEGADELHFVDLDAAKeGRPVNLDVVEEIAEEVFIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 83 GIRDDESLAAALATGCARVNVGTAALENPQWCARVIGEHGDQ-VAVGLDVqiIDGEhrLRGRGW-ETDGGDLWDVLERLD 160
Cdd:pfam00977 81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQcIVVAIDA--RRGK--VAINGWrEDTGIDAVEWAKELE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15608741 161 SEGCSRFVVTDITKDGTLGGPNLDLLAGVADRTDAPVIASGGVSSLDDLRAIATLthrGVEGAIVGKALYARRFT 235
Cdd:pfam00977 157 ELGAGEILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELFTE---GVDGVIAGSALYEGEIT 228
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14024 |
PRK14024 |
phosphoribosyl isomerase A; Provisional |
1-245 |
1.53e-162 |
|
phosphoribosyl isomerase A; Provisional
Pssm-ID: 237589 Cd Length: 241 Bit Score: 449.02 E-value: 1.53e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 1 MMPLILLPAVDVVEGRAVRLVQGKAGSQTEYGSAVDAALGWQRDGAEWIHLVDLDAAFGRGSNHELLAEVVGKLDVQVEL 80
Cdd:PRK14024 1 TMSLTLLPAVDVVDGQAVRLVQGEAGSETSYGSPLDAALAWQRDGAEWIHLVDLDAAFGRGSNRELLAEVVGKLDVKVEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 81 SGGIRDDESLAAALATGCARVNVGTAALENPQWCARVIGEHGDQVAVGLDVqiidGEHRLRGRGWETDGGDLWDVLERLD 160
Cdd:PRK14024 81 SGGIRDDESLEAALATGCARVNIGTAALENPEWCARVIAEHGDRVAVGLDV----RGHTLAARGWTRDGGDLWEVLERLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 161 SEGCSRFVVTDITKDGTLGGPNLDLLAGVADRTDAPVIASGGVSSLDDLRAIATLTHRGVEGAIVGKALYARRFTLPQAL 240
Cdd:PRK14024 157 SAGCSRYVVTDVTKDGTLTGPNLELLREVCARTDAPVVASGGVSSLDDLRALAELVPLGVEGAIVGKALYAGAFTLPEAL 236
|
....*
gi 15608741 241 AAVRD 245
Cdd:PRK14024 237 AVVRR 241
|
|
| hisA-trpF |
TIGR01919 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
2-244 |
6.80e-115 |
|
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: 328.84 E-value: 6.80e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 2 MPLILLPAVDVVEGRAVRLVQGKAGSQTEYGSAVDAALGWQRDGAEWIHLVDLDAAFGRGSNHELLAEVVGKLDVQVELS 81
Cdd:TIGR01919 1 MPLILLPAVDVNGGAAVRLQQGAGGSKTYYGSLESAARWWEQGGAEWIHLVDLDAAFGGGNNEEMLEEVVGLLDVVEELS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 82 GGIRDDESLAAALATGCARVNVGTAALENPQWCARVIGEHGDQVAVGLDVQIIDGEHRLRGRGWETDGGDLWDVLERLDS 161
Cdd:TIGR01919 81 GGRRDDSSLRAALTGGCARVNGGTAALENPWWAARVIREGGDIVAVGLDVLEIGEWHTLGNRGWSDGGGDLEVLERLLDS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 162 EGCSRFVVTDITKDGTLGGPNLDLLAGVADRTDAPVIASGGVSSLDDLRAIATLTHRGVEGAIVGKALYARRFTLPQALA 241
Cdd:TIGR01919 161 GGCSRVVVTDSKKDGLLGGPNLLLLAVVAARTDAIVAASGGSSLLDDLRAIKYLDEGGVSVAIGGKLLYARFFTLEAALA 240
|
...
gi 15608741 242 AVR 244
Cdd:TIGR01919 241 VEK 243
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
5-244 |
8.15e-101 |
|
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: 292.71 E-value: 8.15e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 5 ILLPAVDVVEGRAVRLVQGKAGSQTEYG-SAVDAALGWQRDGAEWIHLVDLDAAF-GRGSNHELLAEVVGKLDVQVELSG 82
Cdd:COG0106 1 IIIPAIDLKDGKCVRLVQGDYDQETVYSdDPVEVAKRWEDAGAEWLHLVDLDGAFaGKPVNLELIEEIAKATGLPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 83 GIRDDESLAAALATGCARVNVGTAALENPQWCARVIGEHGDQVAVGLDVQiidgEHRLRGRGWETDGG-DLWDVLERLDS 161
Cdd:COG0106 81 GIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFPERIVVGLDAR----DGKVATDGWQETSGvDLEELAKRFED 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 162 EGCSRFVVTDITKDGTLGGPNLDLLAGVADRTDAPVIASGGVSSLDDLRAIATLthrGVEGAIVGKALYARRFTLPQALA 241
Cdd:COG0106 157 AGVAAILYTDISRDGTLQGPNLELYRELAAATGIPVIASGGVSSLDDLRALKEL---GVEGAIVGKALYEGKIDLEEALA 233
|
...
gi 15608741 242 AVR 244
Cdd:COG0106 234 LAR 236
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
5-241 |
9.00e-90 |
|
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: 264.73 E-value: 9.00e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 5 ILLPAVDVVEGRAVRLVQGKAGSQTEY-GSAVDAALGWQRDGAEWIHLVDLDAAF-GRGSNHELLAEVVGKLDVQVELSG 82
Cdd:cd04732 1 IIIPAIDLKDGKCVRLYQGDYDKKTVYsDDPVEVAKKWEEAGAKWLHVVDLDGAKgGEPVNLELIEEIVKAVGIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 83 GIRDDESLAAALATGCARVNVGTAALENPQWCARVIGEHG-DQVAVGLDVqiIDGEHRLRGrGWETDGGDLWDVLERLDS 161
Cdd:cd04732 81 GIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGgERIVVGLDA--KDGKVATKG-WLETSEVSLEELAKRFEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 162 EGCSRFVVTDITKDGTLGGPNLDLLAGVADRTDAPVIASGGVSSLDDLRAIATLthrGVEGAIVGKALYARRFTLPQALA 241
Cdd:cd04732 158 LGVKAIIYTDISRDGTLSGPNFELYKELAAATGIPVIASGGVSSLDDIKALKEL---GVAGVIVGKALYEGKITLEEALA 234
|
|
| PRK00748 |
PRK00748 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
5-239 |
1.46e-84 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated
Pssm-ID: 179108 Cd Length: 233 Bit Score: 251.52 E-value: 1.46e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 5 ILLPAVDVVEGRAVRLVQGKAGSQTEYG-SAVDAALGWQRDGAEWIHLVDLDAAF-GRGSNHELLAEVVGKLDVQVELSG 82
Cdd:PRK00748 2 IIIPAIDLKDGKCVRLYQGDYDQATVYSdDPVAQAKAWEDQGAKWLHLVDLDGAKaGKPVNLELIEAIVKAVDIPVQVGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 83 GIRDDESLAAALATGCARVNVGTAALENPQWCARVIGEHGDQVAVGLDVqiIDGehRLRGRGW-ETDGGDLWDVLERLDS 161
Cdd:PRK00748 82 GIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFPGKIVVGLDA--RDG--KVATDGWlETSGVTAEDLAKRFED 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15608741 162 EGCSRFVVTDITKDGTLGGPNLDLLAGVADRTDAPVIASGGVSSLDDLRAIATLthRGVEGAIVGKALYARRFTLPQA 239
Cdd:PRK00748 158 AGVKAIIYTDISRDGTLSGPNVEATRELAAAVPIPVIASGGVSSLDDIKALKGL--GAVEGVIVGRALYEGKFDLAEA 233
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
5-235 |
2.29e-72 |
|
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: 220.43 E-value: 2.29e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 5 ILLPAVDVVEGRAVRLVQGKAGSQTEY-GSAVDAALGWQRDGAEWIHLVDLDAAF-GRGSNHELLAEVVGKLDVQVELSG 82
Cdd:pfam00977 1 RIIPAIDLKDGRVVRLVKGDYFQNTVYaGDPVELAKRYEEEGADELHFVDLDAAKeGRPVNLDVVEEIAEEVFIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 83 GIRDDESLAAALATGCARVNVGTAALENPQWCARVIGEHGDQ-VAVGLDVqiIDGEhrLRGRGW-ETDGGDLWDVLERLD 160
Cdd:pfam00977 81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQcIVVAIDA--RRGK--VAINGWrEDTGIDAVEWAKELE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15608741 161 SEGCSRFVVTDITKDGTLGGPNLDLLAGVADRTDAPVIASGGVSSLDDLRAIATLthrGVEGAIVGKALYARRFT 235
Cdd:pfam00977 157 ELGAGEILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELFTE---GVDGVIAGSALYEGEIT 228
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
6-236 |
2.22e-64 |
|
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: 200.12 E-value: 2.22e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 6 LLPAVDVVEGRAVRLVQGKAGSQTEYG-SAVDAALGWQRDGAEWIHLVDLDAAF-GRGSNHELLAEVVGKLDVQVELSGG 83
Cdd:TIGR00007 1 IIPAIDIKDGKCVRLYQGDYDKETVYGdDPVEAAKKWEEEGAERIHVVDLDGAKeGGPVNLPVIKKIVRETGVPVQVGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 84 IRDDESLAAALATGCARVNVGTAALENPQWCARVIGEHG-DQVAVGLDVQiiDGEhrLRGRGW-ETDGGDLWDVLERLDS 161
Cdd:TIGR00007 81 IRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYGpERIVVSLDAR--GGE--VAVKGWlEKSEVSLEELAKRLEE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15608741 162 EGCSRFVVTDITKDGTLGGPNLDLLAGVADRTDAPVIASGGVSSLDDLRAIATLthrGVEGAIVGKALYARRFTL 236
Cdd:TIGR00007 157 LGLEGIIYTDISRDGTLSGPNFELTKELVKAVNVPVIASGGVSSIDDLIALKKL---GVYGVIVGKALYEGKITL 228
|
|
| PRK13585 |
PRK13585 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ... |
2-245 |
4.86e-52 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase;
Pssm-ID: 184165 Cd Length: 241 Bit Score: 168.93 E-value: 4.86e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 2 MPLILLPAVDVVEGRAVRLVQGKAGSQT-EYGSAVDAALGWQRDGAEWIHLVDLDAAF-GRGSNHELLAEVVGKLDVQVE 79
Cdd:PRK13585 1 MSFEVIPAVDMKGGKCVQLVQGEPGTETvSYGDPVEVAKRWVDAGAETLHLVDLDGAFeGERKNAEAIEKIIEAVGVPVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 80 LSGGIRDDESLAAALATGCARVNVGTAALENPQWCARVIGE-HGDQVAVGLDVQiiDGEHRLrgRGW-ETDGGDLWDVLE 157
Cdd:PRK13585 81 LGGGIRSAEDAASLLDLGVDRVILGTAAVENPEIVRELSEEfGSERVMVSLDAK--DGEVVI--KGWtEKTGYTPVEAAK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 158 RLDSEGCSRFVVTDITKDGTLGGPNLDLLAGVADRTDAPVIASGGVSSLDDLRAIATLthrGVEGAIVGKALYARRFTLP 237
Cdd:PRK13585 157 RFEELGAGSILFTNVDVEGLLEGVNTEPVKELVDSVDIPVIASGGVTTLDDLRALKEA---GAAGVVVGSALYKGKFTLE 233
|
....*...
gi 15608741 238 QALAAVRD 245
Cdd:PRK13585 234 EAIEAVKG 241
|
|
| HisA_HisF |
cd04723 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ... |
6-236 |
3.76e-46 |
|
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: 153.58 E-value: 3.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 6 LLPAVDVVEGRAVRLVQG-------KAGSQTEYGSAVDAALGWQRDGAEWIHLVDLDAAFGRGSNHELLAEVVGKLDVQV 78
Cdd:cd04723 2 IIPVIDLKDGVVVHGVGGdrdnyrpITSNLCSTSDPLDVARAYKELGFRGLYIADLDAIMGRGDNDEAIRELAAAWPLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 79 ELSGGIRDDESLAAALATGCARVNVGTAALENPQWCARVIGEHGDQVAVGLDvqiidgeHRLRGRGWETDGGDLWDVLER 158
Cdd:cd04723 82 WVDGGIRSLENAQEWLKRGASRVIVGTETLPSDDDEDRLAALGEQRLVLSLD-------FRGGQLLKPTDFIGPEELLRR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15608741 159 LDSEgCSRFVVTDITKDGTLGGPNLDLLAGVADRTDAPVIASGGVSSLDDLRAIATLthrGVEGAIVGKALYARRFTL 236
Cdd:cd04723 155 LAKW-PEELIVLDIDRVGSGQGPDLELLERLAARADIPVIAAGGVRSVEDLELLKKL---GASGALVASALHDGGLTL 228
|
|
| PRK04128 |
PRK04128 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
8-240 |
3.80e-32 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 167709 Cd Length: 228 Bit Score: 117.18 E-value: 3.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 8 PAVDVVEGRAVRLVQGKAGSQTEYGSAVDAALGWQrDGAEWIHLVDLDAAF-GRGSNHELLAEVVGKLDVQVELSGGIRD 86
Cdd:PRK04128 6 PAIDLMNGKAVRLYKGRKEEVKVYGDPVEIALRFS-EYVDKIHVVDLDGAFeGKPKNLDVVKNIIRETGLKVQVGGGLRT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 87 DESLAAALATGCARVNVGTAALeNPQWCARVIGEHGDqVAVGLDVQiiDGehRLRGRGW-ETDGGDLWDVLERLdSEGCS 165
Cdd:PRK04128 85 YESIKDAYEIGVENVIIGTKAF-DLEFLEKVTSEFEG-ITVSLDVK--GG--RIAVKGWlEESSIKVEDAYEML-KNYVN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15608741 166 RFVVTDITKDGTLGG-PNLDLLAGvadrtDAPVIASGGVSSLDDlraIATLTHRGVEGAIVGKALYARRFTLPQAL 240
Cdd:PRK04128 158 RFIYTSIERDGTLTGiEEIERFWG-----DEEFIYAGGVSSAED---VKKLAEIGFSGVIIGKALYEGRISLEELL 225
|
|
| PRK13587 |
PRK13587 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
6-234 |
2.87e-30 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Provisional
Pssm-ID: 172156 Cd Length: 234 Bit Score: 112.62 E-value: 2.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 6 LLPAVDVVEGRAVRLVQGKAGSQTEYGSAVDAALGW--QRDGAEWIHLVDLDAAFGRGS-NHELLAEVVGKLDVQVELSG 82
Cdd:PRK13587 4 LWPAIDLIGSTSVRLTEGKYDSEEKMSRSAEESIAYysQFECVNRIHIVDLIGAKAQHArEFDYIKSLRRLTTKDIEVGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 83 GIRDDESLAAALATGCARVNVGTAALENPQWCARVIGEHGDQVAVGLDVQIIDgehrLRGRGWETDGG-DLWDVLERLDS 161
Cdd:PRK13587 84 GIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGRIYLSVDAYGED----IKVNGWEEDTElNLFSFVRQLSD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15608741 162 EGCSRFVVTDITKDGTLGGPNLDLLAGVADRTDAPVIASGGVSSLDDLRAIATLthrGVEGAIVGKALYARRF 234
Cdd:PRK13587 160 IPLGGIIYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGGIRHQQDIQRLASL---NVHAAIIGKAAHQASF 229
|
|
| PRK13586 |
PRK13586 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
1-231 |
4.88e-24 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 237439 Cd Length: 232 Bit Score: 95.96 E-value: 4.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 1 MMPLIllPAVDVVEGRAVRLVQGKAGSQTEYGSAVDAALGWQRDGAEWIHLVDLDAAFGRGSNHELLAEVVgKLDVQ-VE 79
Cdd:PRK13586 1 MSKII--PSIDISLGKAVKRIRGVKGTGLILGNPIEIASKLYNEGYTRIHVVDLDAAEGVGNNEMYIKEIS-KIGFDwIQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 80 LSGGIRDDESLAAALATGCARVNVGTAALENPQWCARVIGEHG-DQVAVGLDVqiiDGEHRLRGRGWETDGGDLWDVLER 158
Cdd:PRK13586 78 VGGGIRDIEKAKRLLSLDVNALVFSTIVFTNFNLFHDIVREIGsNRVLVSIDY---DNTKRVLIRGWKEKSMEVIDGIKK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15608741 159 LDSEGCSRFVVTDITKDGTLGG--PNL----DLLAGVADRtdapviaSGGVSSLDDLRaiaTLTHRGVEGAIVGKALYA 231
Cdd:PRK13586 155 VNELELLGIIFTYISNEGTTKGidYNVkdyaRLIRGLKEY-------AGGVSSDADLE---YLKNVGFDYIIVGMAFYL 223
|
|
| HisF |
cd04731 |
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ... |
6-239 |
5.67e-21 |
|
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: 87.91 E-value: 5.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 6 LLPAVDVVEGRAVRLVQGKagSQTEYGSAVDAALGWQRDGAEWIHLVDLDAAF-GRGSNHELLAEVVGKLDVQVELSGGI 84
Cdd:cd04731 3 IIPCLDVKDGRVVKGVNFK--NLRDAGDPVELAKRYNEQGADELVFLDITASSeGRETMLDVVERVAEEVFIPLTVGGGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 85 RDDESLAAALATGCARVNVGTAALENPQWCARVIGEHGDQ-VAVGLDVQIIDGehrlrgRGWE--TDGG------DLWDV 155
Cdd:cd04731 81 RSLEDARRLLRAGADKVSINSAAVENPELIREIAKRFGSQcVVVSIDAKRRGD------GGYEvyTHGGrkptglDAVEW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 156 LERLDSEGCSRFVVTDITKDGTLGGPNLDLLAGVADRTDAPVIASGGVSSLDDLRAIatLTHRGVEGAIVGKALYARRFT 235
Cdd:cd04731 155 AKEVEELGAGEILLTSMDRDGTKKGYDLELIRAVSSAVNIPVIASGGAGKPEHFVEA--FEEGGADAALAASIFHFGEYT 232
|
....
gi 15608741 236 LPQA 239
Cdd:cd04731 233 IAEL 236
|
|
| PRK14114 |
PRK14114 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
4-229 |
7.19e-19 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 172604 Cd Length: 241 Bit Score: 82.37 E-value: 7.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 4 LILLPAVDVVEGRAVRLVQGKAGSQTEY-GSAVDAALGWQRDGAEWIHLVDLDAAFGRGSNHELLAEVVGKLDVQVELSG 82
Cdd:PRK14114 1 MLVVPAIDLFRGKVARMVKGKKENTIFYeKDPAELVEKLIEEGFTLIHVVDLSKAIENSVENLPVLEKLSEFAEHIQIGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 83 GIRDDESLAAALATGCARVNVGTAALENPQWCaRVIGEHGDQVAVGLDVQiidgEHRLRGRGW-ETDGGDLWDVLERLDS 161
Cdd:PRK14114 81 GIRSLDYAEKLRKLGYRRQIVSSKVLEDPSFL-KFLKEIDVEPVFSLDTR----GGKVAFKGWlAEEEIDPVSLLKRLKE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15608741 162 EGCSRFVVTDITKDGTLGGPNLDLLAGVADRTDAPVIASGGVSSLDDLRAiATLTHRG----VEGAIVGKAL 229
Cdd:PRK14114 156 YGLEEIVHTEIEKDGTLQEHDFSLTRKIAIEAEVKVFAAGGISSENSLKT-AQRVHREtnglLKGVIVGRAF 226
|
|
| HisF |
COG0107 |
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ... |
32-217 |
2.11e-16 |
|
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: 75.83 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 32 GSAVDAALGWQRDGAEWIHLVDLDAAF-GRGSNHELLAEVVGKLDVQVELSGGIRDDESLAAALATGCARVNVGTAALEN 110
Cdd:COG0107 29 GDPVELAKRYNEQGADELVFLDITASSeGRKTMLDVVRRVAEEVFIPLTVGGGIRSVEDARRLLRAGADKVSINSAAVKN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 111 PQWCARVIGEHGDQ-VAVGLDVQiidgehRLRGRGWE--TDGGDL---WDVLE---RLDSEGCSRFVVTDITKDGTLGGP 181
Cdd:COG0107 109 PELITEAAERFGSQcIVVAIDAK------RVPDGGWEvyTHGGRKptgLDAVEwakEAEELGAGEILLTSMDRDGTKDGY 182
|
170 180 190
....*....|....*....|....*....|....*.
gi 15608741 182 NLDLLAGVADRTDAPVIASGGVSSLDDLRAIATLTH 217
Cdd:COG0107 183 DLELTRAVSEAVSIPVIASGGAGTLEHFVEVFTEGG 218
|
|
| hisF |
TIGR00735 |
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ... |
6-203 |
2.41e-14 |
|
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273241 Cd Length: 254 Bit Score: 70.09 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 6 LLPAVDVVEGRAVRLVQGKagSQTEYGSAVDAALGWQRDGAEWIHLVDLDA-AFGRGSNHELLAEVVGKLDVQVELSGGI 84
Cdd:TIGR00735 6 IIPCLDVRDGRVVKGVQFL--NLRDAGDPVELAQRYDEEGADELVFLDITAsSEGRTTMIDVVERTAETVFIPLTVGGGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 85 RDDESLAAALATGCARVNVGTAALENPQwcarVIGEHGDQVAVGLDVQIIDGEHRLRGR----------GWETDGGDLWD 154
Cdd:TIGR00735 84 KSIEDVDKLLRAGADKVSINTAAVKNPE----LIYELADRFGSQCIVVAIDAKRVYVNSycwyevyiygGRESTGLDAVE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15608741 155 VLERLDSEGCSRFVVTDITKDGTLGGPNLDLLAGVADRTDAPVIASGGV 203
Cdd:TIGR00735 160 WAKEVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEAVKIPVIASGGA 208
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
138-232 |
2.31e-05 |
|
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: 44.02 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 138 HRLrgrGWEtDGGDLWDVLERLDSEGCSRFVV---TdiTKDGTLGGPNLDLLAGVADRTDAPVIASGGVSSLDDLRAIAT 214
Cdd:cd02801 130 IRL---GWD-DEEETLELAKALEDAGASALTVhgrT--REQRYSGPADWDYIAEIKEAVSIPVIANGDIFSLEDALRCLE 203
|
90
....*....|....*...
gi 15608741 215 LThrGVEGAIVGKALYAR 232
Cdd:cd02801 204 QT--GVDGVMIGRGALGN 219
|
|
| DusA |
COG0042 |
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
138-232 |
5.97e-04 |
|
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: 40.08 E-value: 5.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608741 138 HRLrgrGWETDGGDLWDVLERLDSEGCSRFVV---TdiTKDGTLGGPNLDLLAGVADRTDAPVIASGGVSSLDDlrAIAT 214
Cdd:COG0042 137 IRL---GWDDDDENALEFARIAEDAGAAALTVhgrT--REQRYKGPADWDAIARVKEAVSIPVIGNGDIFSPED--AKRM 209
|
90
....*....|....*...
gi 15608741 215 LTHRGVEGAIVGKALYAR 232
Cdd:COG0042 210 LEETGCDGVMIGRGALGN 227
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
63-120 |
1.50e-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: 1.50e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 15608741 63 NHELLAEVVGKLDVQVELSGGIRDDESLAAALA-TGCARVNVGTAALENPqWCARVIGE 120
Cdd:cd02801 171 DWDYIAEIKEAVSIPVIANGDIFSLEDALRCLEqTGVDGVMIGRGALGNP-WLFREIKE 228
|
|
| YrpB |
COG2070 |
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
66-106 |
2.36e-03 |
|
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];
Pssm-ID: 441673 [Multi-domain] Cd Length: 302 Bit Score: 38.55 E-value: 2.36e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 15608741 66 LLAEVVGKLDVQVELSGGIRDDESLAAALATGCARVNVGTA 106
Cdd:COG2070 149 LVPEVRDAVDIPVIAAGGIADGRGIAAALALGADGVQMGTR 189
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
65-106 |
2.63e-03 |
|
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.
Pssm-ID: 240081 [Multi-domain] Cd Length: 236 Bit Score: 37.85 E-value: 2.63e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 15608741 65 ELLAEVVGKLDVQVELSGGIRDDESLAAALATGCARVNVGTA 106
Cdd:cd04730 146 ALVPEVRDAVDIPVIAAGGIADGRGIAAALALGADGVQMGTR 187
|
|
| |
