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Conserved domains on  [gi|896138474|ref|WP_049158381|]
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MULTISPECIES: bifunctional 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase/phosphoribosylanthranilate isomerase PriA [Micrococcus]

Protein Classification

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase( domain architecture ID 10793950)

phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase catalyzes the fourth step in histidine biosynthesis.

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK14024 PRK14024
phosphoribosyl isomerase A; Provisional
 5-245 5.00e-156

phosphoribosyl isomerase A; Provisional


:

Pssm-ID: 237589  Cd Length: 241  Bit Score: 433.62  E-value: 5.00e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474   5 APALELLPAVDVQDGQAVRLVQGEAGSATSYGDPVTAALDWQRAGAEWIHLVDLDAAFGRGDNREVMRRVVEEIGVKIEL 84
Cdd:PRK14024   1 TMSLTLLPAVDVVDGQAVRLVQGEAGSETSYGSPLDAALAWQRDGAEWIHLVDLDAAFGRGSNRELLAEVVGKLDVKVEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474  85 SGGIRDDASLENALEMGAARVNLGTAALEDPEWTARVIERFGDRVAVGLDVRGTTLAARGWTKEGGDLWEVLDRLEDAGC 164
Cdd:PRK14024  81 SGGIRDDESLEAALATGCARVNIGTAALENPEWCARVIAEHGDRVAVGLDVRGHTLAARGWTRDGGDLWEVLERLDSAGC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474 165 ARYVVTDVTKDGTLKGPNTELLAQVCAKTAKPVVASGGISSLEDVAALAAMTGQGVEGAIMGKALYAGRFSLEQALAVAG 244
Cdd:PRK14024 161 SRYVVTDVTKDGTLTGPNLELLREVCARTDAPVVASGGVSSLDDLRALAELVPLGVEGAIVGKALYAGAFTLPEALAVVR 240


                 .
gi 896138474 245 G 245
Cdd:PRK14024 241 R 241
 
Name Accession Description Interval E-value
PRK14024 PRK14024
phosphoribosyl isomerase A; Provisional
 5-245 5.00e-156

phosphoribosyl isomerase A; Provisional


Pssm-ID: 237589  Cd Length: 241  Bit Score: 433.62  E-value: 5.00e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474   5 APALELLPAVDVQDGQAVRLVQGEAGSATSYGDPVTAALDWQRAGAEWIHLVDLDAAFGRGDNREVMRRVVEEIGVKIEL 84
Cdd:PRK14024   1 TMSLTLLPAVDVVDGQAVRLVQGEAGSETSYGSPLDAALAWQRDGAEWIHLVDLDAAFGRGSNRELLAEVVGKLDVKVEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474  85 SGGIRDDASLENALEMGAARVNLGTAALEDPEWTARVIERFGDRVAVGLDVRGTTLAARGWTKEGGDLWEVLDRLEDAGC 164
Cdd:PRK14024  81 SGGIRDDESLEAALATGCARVNIGTAALENPEWCARVIAEHGDRVAVGLDVRGHTLAARGWTRDGGDLWEVLERLDSAGC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474 165 ARYVVTDVTKDGTLKGPNTELLAQVCAKTAKPVVASGGISSLEDVAALAAMTGQGVEGAIMGKALYAGRFSLEQALAVAG 244
Cdd:PRK14024 161 SRYVVTDVTKDGTLTGPNLELLREVCARTDAPVVASGGVSSLDDLRALAELVPLGVEGAIVGKALYAGAFTLPEALAVVR 240


                 .
gi 896138474 245 G 245
Cdd:PRK14024 241 R 241
HisA COG0106
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ...
 9-244 6.83e-114

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: 326.61  E-value: 6.83e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474   9 ELLPAVDVQDGQAVRLVQGEAGSATSYG-DPVTAALDWQRAGAEWIHLVDLDAAF-GRGDNREVMRRVVEEIGVKIELSG 86
Cdd:COG0106    1 IIIPAIDLKDGKCVRLVQGDYDQETVYSdDPVEVAKRWEDAGAEWLHLVDLDGAFaGKPVNLELIEEIAKATGLPVQVGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474  87 GIRDDASLENALEMGAARVNLGTAALEDPEWTARVIERFGDRVAVGLDVRGTTLAARGWTKEGG-DLWEVLDRLEDAGCA 165
Cdd:COG0106   81 GIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFPERIVVGLDARDGKVATDGWQETSGvDLEELAKRFEDAGVA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896138474 166 RYVVTDVTKDGTLKGPNTELLAQVCAKTAKPVVASGGISSLEDVAALAAMtgqGVEGAIMGKALYAGRFSLEQALAVAG 244
Cdd:COG0106  161 AILYTDISRDGTLQGPNLELYRELAAATGIPVIASGGVSSLDDLRALKEL---GVEGAIVGKALYEGKIDLEEALALAR 236
HisA cd04732
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ...
 9-241 4.52e-102

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: 296.70  E-value: 4.52e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474   9 ELLPAVDVQDGQAVRLVQGEAGSATSY-GDPVTAALDWQRAGAEWIHLVDLDAAF-GRGDNREVMRRVVEEIGVKIELSG 86
Cdd:cd04732    1 IIIPAIDLKDGKCVRLYQGDYDKKTVYsDDPVEVAKKWEEAGAKWLHVVDLDGAKgGEPVNLELIEEIVKAVGIPVQVGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474  87 GIRDDASLENALEMGAARVNLGTAALEDPEWTARVIERFG-DRVAVGLDVRGTTLAARGWTKE-GGDLWEVLDRLEDAGC 164
Cdd:cd04732   81 GIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGgERIVVGLDAKDGKVATKGWLETsEVSLEELAKRFEELGV 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896138474 165 ARYVVTDVTKDGTLKGPNTELLAQVCAKTAKPVVASGGISSLEDVAALAAMtgqGVEGAIMGKALYAGRFSLEQALA 241
Cdd:cd04732  161 KAIIYTDISRDGTLSGPNFELYKELAAATGIPVIASGGVSSLDDIKALKEL---GVAGVIVGKALYEGKITLEEALA 234
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 9-235 2.81e-83

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: 248.55  E-value: 2.81e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474    9 ELLPAVDVQDGQAVRLVQGEAGSATSY-GDPVTAALDWQRAGAEWIHLVDLDAAF-GRGDNREVMRRVVEEIGVKIELSG 86
Cdd:pfam00977   1 RIIPAIDLKDGRVVRLVKGDYFQNTVYaGDPVELAKRYEEEGADELHFVDLDAAKeGRPVNLDVVEEIAEEVFIPVQVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474   87 GIRDDASLENALEMGAARVNLGTAALEDPEWTARVIERFG-DRVAVGLDVRGTTLAARGWTKEGG-DLWEVLDRLEDAGC 164
Cdd:pfam00977  81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGsQCIVVAIDARRGKVAINGWREDTGiDAVEWAKELEELGA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896138474  165 ARYVVTDVTKDGTLKGPNTELLAQVCAKTAKPVVASGGISSLEDVAALAAMtgqGVEGAIMGKALYAGRFS 235
Cdd:pfam00977 161 GEILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELFTE---GVDGVIAGSALYEGEIT 228
hisA-trpF TIGR01919
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 8-243 4.14e-78

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: 236.01  E-value: 4.14e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474    8 LELLPAVDVQDGQAVRLVQGEAGSATSYGDPVTAALDWQRAGAEWIHLVDLDAAFGRGDNREVMRRVVEEIGVKIELSGG 87
Cdd:TIGR01919   3 LILLPAVDVNGGAAVRLQQGAGGSKTYYGSLESAARWWEQGGAEWIHLVDLDAAFGGGNNEEMLEEVVGLLDVVEELSGG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474   88 IRDDASLENALEMGAARVNLGTAALEDPEWTARVIERFGDRVAVGLDVR----GTTLAARGWTKEGGDLWEVLDRLEDAG 163
Cdd:TIGR01919  83 RRDDSSLRAALTGGCARVNGGTAALENPWWAARVIREGGDIVAVGLDVLeigeWHTLGNRGWSDGGGDLEVLERLLDSGG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474  164 CARYVVTDVTKDGTLKGPNTELLAQVCAKTAKPVVASGGISSLEDVAALAAMTGQGVEGAIMGKALYAGRFSLEQALAVA 243
Cdd:TIGR01919 163 CSRVVVTDSKKDGLLGGPNLLLLAVVAARTDAIVAASGGSSLLDDLRAIKYLDEGGVSVAIGGKLLYARFFTLEAALAVE 242
 
Name Accession Description Interval E-value
PRK14024 PRK14024
phosphoribosyl isomerase A; Provisional
 5-245 5.00e-156

phosphoribosyl isomerase A; Provisional


Pssm-ID: 237589  Cd Length: 241  Bit Score: 433.62  E-value: 5.00e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474   5 APALELLPAVDVQDGQAVRLVQGEAGSATSYGDPVTAALDWQRAGAEWIHLVDLDAAFGRGDNREVMRRVVEEIGVKIEL 84
Cdd:PRK14024   1 TMSLTLLPAVDVVDGQAVRLVQGEAGSETSYGSPLDAALAWQRDGAEWIHLVDLDAAFGRGSNRELLAEVVGKLDVKVEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474  85 SGGIRDDASLENALEMGAARVNLGTAALEDPEWTARVIERFGDRVAVGLDVRGTTLAARGWTKEGGDLWEVLDRLEDAGC 164
Cdd:PRK14024  81 SGGIRDDESLEAALATGCARVNIGTAALENPEWCARVIAEHGDRVAVGLDVRGHTLAARGWTRDGGDLWEVLERLDSAGC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474 165 ARYVVTDVTKDGTLKGPNTELLAQVCAKTAKPVVASGGISSLEDVAALAAMTGQGVEGAIMGKALYAGRFSLEQALAVAG 244
Cdd:PRK14024 161 SRYVVTDVTKDGTLTGPNLELLREVCARTDAPVVASGGVSSLDDLRALAELVPLGVEGAIVGKALYAGAFTLPEALAVVR 240


                 .
gi 896138474 245 G 245
Cdd:PRK14024 241 R 241
HisA COG0106
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ...
 9-244 6.83e-114

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: 326.61  E-value: 6.83e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474   9 ELLPAVDVQDGQAVRLVQGEAGSATSYG-DPVTAALDWQRAGAEWIHLVDLDAAF-GRGDNREVMRRVVEEIGVKIELSG 86
Cdd:COG0106    1 IIIPAIDLKDGKCVRLVQGDYDQETVYSdDPVEVAKRWEDAGAEWLHLVDLDGAFaGKPVNLELIEEIAKATGLPVQVGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474  87 GIRDDASLENALEMGAARVNLGTAALEDPEWTARVIERFGDRVAVGLDVRGTTLAARGWTKEGG-DLWEVLDRLEDAGCA 165
Cdd:COG0106   81 GIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFPERIVVGLDARDGKVATDGWQETSGvDLEELAKRFEDAGVA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896138474 166 RYVVTDVTKDGTLKGPNTELLAQVCAKTAKPVVASGGISSLEDVAALAAMtgqGVEGAIMGKALYAGRFSLEQALAVAG 244
Cdd:COG0106  161 AILYTDISRDGTLQGPNLELYRELAAATGIPVIASGGVSSLDDLRALKEL---GVEGAIVGKALYEGKIDLEEALALAR 236
HisA cd04732
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ...
 9-241 4.52e-102

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: 296.70  E-value: 4.52e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474   9 ELLPAVDVQDGQAVRLVQGEAGSATSY-GDPVTAALDWQRAGAEWIHLVDLDAAF-GRGDNREVMRRVVEEIGVKIELSG 86
Cdd:cd04732    1 IIIPAIDLKDGKCVRLYQGDYDKKTVYsDDPVEVAKKWEEAGAKWLHVVDLDGAKgGEPVNLELIEEIVKAVGIPVQVGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474  87 GIRDDASLENALEMGAARVNLGTAALEDPEWTARVIERFG-DRVAVGLDVRGTTLAARGWTKE-GGDLWEVLDRLEDAGC 164
Cdd:cd04732   81 GIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGgERIVVGLDAKDGKVATKGWLETsEVSLEELAKRFEELGV 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896138474 165 ARYVVTDVTKDGTLKGPNTELLAQVCAKTAKPVVASGGISSLEDVAALAAMtgqGVEGAIMGKALYAGRFSLEQALA 241
Cdd:cd04732  161 KAIIYTDISRDGTLSGPNFELYKELAAATGIPVIASGGVSSLDDIKALKEL---GVAGVIVGKALYEGKITLEEALA 234
PRK00748 PRK00748
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 9-239 1.97e-95

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated


Pssm-ID: 179108  Cd Length: 233  Bit Score: 279.64  E-value: 1.97e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474   9 ELLPAVDVQDGQAVRLVQGEAGSATSYG-DPVTAALDWQRAGAEWIHLVDLDAAF-GRGDNREVMRRVVEEIGVKIELSG 86
Cdd:PRK00748   2 IIIPAIDLKDGKCVRLYQGDYDQATVYSdDPVAQAKAWEDQGAKWLHLVDLDGAKaGKPVNLELIEAIVKAVDIPVQVGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474  87 GIRDDASLENALEMGAARVNLGTAALEDPEWTARVIERFGDRVAVGLDVRGTTLAARGWTKEGG-DLWEVLDRLEDAGCA 165
Cdd:PRK00748  82 GIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFPGKIVVGLDARDGKVATDGWLETSGvTAEDLAKRFEDAGVK 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896138474 166 RYVVTDVTKDGTLKGPNTELLAQVCAKTAKPVVASGGISSLEDVAALAAMtgQGVEGAIMGKALYAGRFSLEQA 239
Cdd:PRK00748 162 AIIYTDISRDGTLSGPNVEATRELAAAVPIPVIASGGVSSLDDIKALKGL--GAVEGVIVGRALYEGKFDLAEA 233
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 9-235 2.81e-83

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: 248.55  E-value: 2.81e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474    9 ELLPAVDVQDGQAVRLVQGEAGSATSY-GDPVTAALDWQRAGAEWIHLVDLDAAF-GRGDNREVMRRVVEEIGVKIELSG 86
Cdd:pfam00977   1 RIIPAIDLKDGRVVRLVKGDYFQNTVYaGDPVELAKRYEEEGADELHFVDLDAAKeGRPVNLDVVEEIAEEVFIPVQVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474   87 GIRDDASLENALEMGAARVNLGTAALEDPEWTARVIERFG-DRVAVGLDVRGTTLAARGWTKEGG-DLWEVLDRLEDAGC 164
Cdd:pfam00977  81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGsQCIVVAIDARRGKVAINGWREDTGiDAVEWAKELEELGA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896138474  165 ARYVVTDVTKDGTLKGPNTELLAQVCAKTAKPVVASGGISSLEDVAALAAMtgqGVEGAIMGKALYAGRFS 235
Cdd:pfam00977 161 GEILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELFTE---GVDGVIAGSALYEGEIT 228
hisA-trpF TIGR01919
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 8-243 4.14e-78

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: 236.01  E-value: 4.14e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474    8 LELLPAVDVQDGQAVRLVQGEAGSATSYGDPVTAALDWQRAGAEWIHLVDLDAAFGRGDNREVMRRVVEEIGVKIELSGG 87
Cdd:TIGR01919   3 LILLPAVDVNGGAAVRLQQGAGGSKTYYGSLESAARWWEQGGAEWIHLVDLDAAFGGGNNEEMLEEVVGLLDVVEELSGG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474   88 IRDDASLENALEMGAARVNLGTAALEDPEWTARVIERFGDRVAVGLDVR----GTTLAARGWTKEGGDLWEVLDRLEDAG 163
Cdd:TIGR01919  83 RRDDSSLRAALTGGCARVNGGTAALENPWWAARVIREGGDIVAVGLDVLeigeWHTLGNRGWSDGGGDLEVLERLLDSGG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474  164 CARYVVTDVTKDGTLKGPNTELLAQVCAKTAKPVVASGGISSLEDVAALAAMTGQGVEGAIMGKALYAGRFSLEQALAVA 243
Cdd:TIGR01919 163 CSRVVVTDSKKDGLLGGPNLLLLAVVAARTDAIVAASGGSSLLDDLRAIKYLDEGGVSVAIGGKLLYARFFTLEAALAVE 242
TIGR00007 TIGR00007
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ...
 10-237 5.94e-78

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: 235.17  E-value: 5.94e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474   10 LLPAVDVQDGQAVRLVQGEAGSATSYGD-PVTAALDWQRAGAEWIHLVDLDAAF-GRGDNREVMRRVVEEIGVKIELSGG 87
Cdd:TIGR00007   1 IIPAIDIKDGKCVRLYQGDYDKETVYGDdPVEAAKKWEEEGAERIHVVDLDGAKeGGPVNLPVIKKIVRETGVPVQVGGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474   88 IRDDASLENALEMGAARVNLGTAALEDPEWTARVIERFG-DRVAVGLDVRGTTLAARGWT-KEGGDLWEVLDRLEDAGCA 165
Cdd:TIGR00007  81 IRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYGpERIVVSLDARGGEVAVKGWLeKSEVSLEELAKRLEELGLE 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896138474  166 RYVVTDVTKDGTLKGPNTELLAQVCAKTAKPVVASGGISSLEDVAALAAMtgqGVEGAIMGKALYAGRFSLE 237
Cdd:TIGR00007 161 GIIYTDISRDGTLSGPNFELTKELVKAVNVPVIASGGVSSIDDLIALKKL---GVYGVIVGKALYEGKITLE 229
PRK13585 PRK13585
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ...
 6-245 3.91e-64

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase;


Pssm-ID: 184165  Cd Length: 241  Bit Score: 200.52  E-value: 3.91e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474   6 PALELLPAVDVQDGQAVRLVQGEAGSAT-SYGDPVTAALDWQRAGAEWIHLVDLDAAF-GRGDNREVMRRVVEEIGVKIE 83
Cdd:PRK13585   1 MSFEVIPAVDMKGGKCVQLVQGEPGTETvSYGDPVEVAKRWVDAGAETLHLVDLDGAFeGERKNAEAIEKIIEAVGVPVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474  84 LSGGIRDDASLENALEMGAARVNLGTAALEDPEWTARVIERFG-DRVAVGLDVRGTTLAARGWTKE-GGDLWEVLDRLED 161
Cdd:PRK13585  81 LGGGIRSAEDAASLLDLGVDRVILGTAAVENPEIVRELSEEFGsERVMVSLDAKDGEVVIKGWTEKtGYTPVEAAKRFEE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474 162 AGCARYVVTDVTKDGTLKGPNTELLAQVCAKTAKPVVASGGISSLEDVAALAAMtgqGVEGAIMGKALYAGRFSLEQALA 241
Cdd:PRK13585 161 LGAGSILFTNVDVEGLLEGVNTEPVKELVDSVDIPVIASGGVTTLDDLRALKEA---GAAGVVVGSALYKGKFTLEEAIE 237


                 ....
gi 896138474 242 VAGG 245
Cdd:PRK13585 238 AVKG 241
HisA_HisF cd04723
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ...
 9-241 3.02e-52

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: 169.76  E-value: 3.02e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474   9 ELLPAVDVQDGQAVRLVQGEAGS-------ATSYGDPVTAALDWQRAGAEWIHLVDLDAAFGRGDNREVMRRVVEEIGVK 81
Cdd:cd04723    1 RIIPVIDLKDGVVVHGVGGDRDNyrpitsnLCSTSDPLDVARAYKELGFRGLYIADLDAIMGRGDNDEAIRELAAAWPLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474  82 IELSGGIRDDASLENALEMGAARVNLGTAALEDpEWTARVIERFG-DRVAVGLDVRGTTLaarGWTKEGGDLWEVLDRLE 160
Cdd:cd04723   81 LWVDGGIRSLENAQEWLKRGASRVIVGTETLPS-DDDEDRLAALGeQRLVLSLDFRGGQL---LKPTDFIGPEELLRRLA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474 161 DAgCARYVVTDVTKDGTLKGPNTELLAQVCAKTAKPVVASGGISSLEDVAALAAMtgqGVEGAIMGKALYAGRFSLEQAL 240
Cdd:cd04723  157 KW-PEELIVLDIDRVGSGQGPDLELLERLAARADIPVIAAGGVRSVEDLELLKKL---GASGALVASALHDGGLTLEDVV 232


                 .
gi 896138474 241 A 241
Cdd:cd04723  233 R 233
PRK04128 PRK04128
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ...
 8-243 1.32e-46

1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;


Pssm-ID: 167709  Cd Length: 228  Bit Score: 155.32  E-value: 1.32e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474   8 LELLPAVDVQDGQAVRLVQGEAGSATSYGDPVTAALDWQRAgAEWIHLVDLDAAF-GRGDNREVMRRVVEEIGVKIELSG 86
Cdd:PRK04128   2 MRIYPAIDLMNGKAVRLYKGRKEEVKVYGDPVEIALRFSEY-VDKIHVVDLDGAFeGKPKNLDVVKNIIRETGLKVQVGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474  87 GIRDDASLENALEMGAARVNLGTAALeDPEWTARVIERFGDrVAVGLDVRGTTLAARGWTKEGG----DLWEVLDRLEDa 162
Cdd:PRK04128  81 GLRTYESIKDAYEIGVENVIIGTKAF-DLEFLEKVTSEFEG-ITVSLDVKGGRIAVKGWLEESSikveDAYEMLKNYVN- 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474 163 gcaRYVVTDVTKDGTLKG-PNTELLAQvcaktAKPVVASGGISSLEDVAALAAMtgqGVEGAIMGKALYAGRFSLEQALA 241
Cdd:PRK04128 158 ---RFIYTSIERDGTLTGiEEIERFWG-----DEEFIYAGGVSSAEDVKKLAEI---GFSGVIIGKALYEGRISLEELLE 226


                 ..
gi 896138474 242 VA 243
Cdd:PRK04128 227 VQ 228
PRK13587 PRK13587
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 8-234 2.93e-34

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Provisional


Pssm-ID: 172156  Cd Length: 234  Bit Score: 123.40  E-value: 2.93e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474   8 LELLPAVDVQDGQAVRLVQGEAGSATSYGDPVTAALDW--QRAGAEWIHLVDLDAAFGR----GDNREVMRRVVEEigvK 81
Cdd:PRK13587   2 IELWPAIDLIGSTSVRLTEGKYDSEEKMSRSAEESIAYysQFECVNRIHIVDLIGAKAQhareFDYIKSLRRLTTK---D 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474  82 IELSGGIRDDASLENALEMGAARVNLGTAALEDPEWTARVIERFGDRVAVGLDVRGTTLAARGWTKEGG-DLWEVLDRLE 160
Cdd:PRK13587  79 IEVGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGRIYLSVDAYGEDIKVNGWEEDTElNLFSFVRQLS 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896138474 161 DAGCARYVVTDVTKDGTLKGPNTELLAQVCAKTAKPVVASGGISSLEDVAALAAMtgqGVEGAIMGKALYAGRF 234
Cdd:PRK13587 159 DIPLGGIIYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGGIRHQQDIQRLASL---NVHAAIIGKAAHQASF 229
PRK13586 PRK13586
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ...
 8-232 3.48e-30

1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;


Pssm-ID: 237439  Cd Length: 232  Bit Score: 112.53  E-value: 3.48e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474   8 LELLPAVDVQDGQAVRLVQGEAGSATSYGDPVTAALDWQRAGAEWIHLVDLDAAFGRGDNREVMRRVVeEIGVK-IELSG 86
Cdd:PRK13586   2 SKIIPSIDISLGKAVKRIRGVKGTGLILGNPIEIASKLYNEGYTRIHVVDLDAAEGVGNNEMYIKEIS-KIGFDwIQVGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474  87 GIRDDASLENALEMGAARVNLGTAALEDPEWTARVIERFG-DRVAVGLDVRGT-TLAARGWTKEGGDLWEVLDRLEDAGC 164
Cdd:PRK13586  81 GIRDIEKAKRLLSLDVNALVFSTIVFTNFNLFHDIVREIGsNRVLVSIDYDNTkRVLIRGWKEKSMEVIDGIKKVNELEL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896138474 165 ARYVVTDVTKDGTLKGPNTEllaqVC--AKTAKPVVA-SGGISSLEDVAALAAMtgqGVEGAIMGKALYAG 232
Cdd:PRK13586 161 LGIIFTYISNEGTTKGIDYN----VKdyARLIRGLKEyAGGVSSDADLEYLKNV---GFDYIIVGMAFYLG 224
PRK14114 PRK14114
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ...
 10-237 2.13e-26

1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;


Pssm-ID: 172604  Cd Length: 241  Bit Score: 103.17  E-value: 2.13e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474  10 LLPAVDVQDGQAVRLVQGEAGSATSY-GDPVTAALDWQRAGAEWIHLVDLDAAF-GRGDNREVMRRVvEEIGVKIELSGG 87
Cdd:PRK14114   3 VVPAIDLFRGKVARMVKGKKENTIFYeKDPAELVEKLIEEGFTLIHVVDLSKAIeNSVENLPVLEKL-SEFAEHIQIGGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474  88 IRDDASLENALEMGAARVNLGTAALEDPEWTARVIErFGDRVAVGLDVRGTTLAARGWTKEGG-DLWEVLDRLEDAGCAR 166
Cdd:PRK14114  82 IRSLDYAEKLRKLGYRRQIVSSKVLEDPSFLKFLKE-IDVEPVFSLDTRGGKVAFKGWLAEEEiDPVSLLKRLKEYGLEE 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896138474 167 YVVTDVTKDGTLKGPNTELLAQVCAKTAKPVVASGGIS---SLEDVAALAAMTGQGVEGAIMGKALYAGRFSLE 237
Cdd:PRK14114 161 IVHTEIEKDGTLQEHDFSLTRKIAIEAEVKVFAAGGISsenSLKTAQRVHRETNGLLKGVIVGRAFLEGILTVE 234
HisF cd04731
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ...
 10-214 9.14e-25

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: 98.69  E-value: 9.14e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474  10 LLPAVDVQDGqavRLVQG-EAGSATSYGDPVTAALDWQRAGAEWIHLVDLDAAF-GRGDNREVMRRVVEEIGVKIELSGG 87
Cdd:cd04731    3 IIPCLDVKDG---RVVKGvNFKNLRDAGDPVELAKRYNEQGADELVFLDITASSeGRETMLDVVERVAEEVFIPLTVGGG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474  88 IRDDASLENALEMGAARVNLGTAALEDPEWTARVIERFGD-RVAVGLDVRGTTLAARGWTKEGG------DLWEVLDRLE 160
Cdd:cd04731   80 IRSLEDARRLLRAGADKVSINSAAVENPELIREIAKRFGSqCVVVSIDAKRRGDGGYEVYTHGGrkptglDAVEWAKEVE 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896138474 161 DAGCARYVVTDVTKDGTLKGPNTELLAQVCAKTAKPVVASGGISSLEDV----------AALAA 214
Cdd:cd04731  160 ELGAGEILLTSMDRDGTKKGYDLELIRAVSSAVNIPVIASGGAGKPEHFveafeeggadAALAA 223
hisAF_rel TIGR00734
hisA/hisF family protein; This model models a family of proteins found so far in three ...
 8-232 3.61e-24

hisA/hisF family protein; This model models a family of proteins found so far in three archaeal species: Methanobacterium thermoautotrophicum, Methanococcus jannaschii, and Archaeoglobus fulgidus. This protein is homologous to phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase (HisA) and, with lower similarity, to the cyclase HisF, both of which are enzymes of histidine biosynthesis. Each species with this protein also encodes HisA. The function of this protein is unknown. [Unknown function, General]


Pssm-ID: 273240  Cd Length: 221  Bit Score: 96.53  E-value: 3.61e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474    8 LELLPAVDVQDGQAVrlvQGEAGSATSY----------GDPVTAALDWQRAGAEWIHLVDLDAAFGRGDNREVMRRvVEE 77
Cdd:TIGR00734   1 MKIIPVIDLKDGIAV---AGKSGERESYpplesvsrlsSSPDDAAKVIEEIGARFIYIADLDRIVGLGDNFSLLSK-LSK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474   78 IGVKIeLSGGIRDDASLENALEM--GAARVNLGTAALEDPEWTARVIerfgdrVAVGLDVRGTTLAARGwtKEGGdlWEV 155
Cdd:TIGR00734  77 RVELI-ADCGVRSPEDLETLPFTleFASRVVVATETLDITELLRECY------TVVSLDFKEKFLDASG--LFES--LEE 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896138474  156 LDRLEDAGCARYVVTDVTKDGTLKGPNTELLAQVCAKTAKPVVASGGISSLEDVAALAAMtgqGVEGAIMGKALYAG 232
Cdd:TIGR00734 146 VRDFLNSFDYGLIVLDIHSVGTMKGPNLELLTKTLELSEHPVMLGGGISGVEDLELLKEM---GVSAVLVATAVHKG 219
hisF TIGR00735
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ...
 7-238 1.40e-21

imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273241  Cd Length: 254  Bit Score: 90.50  E-value: 1.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474    7 ALELLPAVDVQDGQAVRLVQGEagSATSYGDPVTAALDWQRAGAEWIHLVDLDA-AFGRGDNREVMRRVVEEIGVKIELS 85
Cdd:TIGR00735   3 AKRIIPCLDVRDGRVVKGVQFL--NLRDAGDPVELAQRYDEEGADELVFLDITAsSEGRTTMIDVVERTAETVFIPLTVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474   86 GGIRDDASLENALEMGAARVNLGTAALEDPEWTARVIERFGDR-VAVGLDVRGTTLAARGW---TKEGG------DLWEV 155
Cdd:TIGR00735  81 GGIKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFGSQcIVVAIDAKRVYVNSYCWyevYIYGGrestglDAVEW 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474  156 LDRLEDAGCARYVVTDVTKDGTLKGPNTELLAQVCAKTAKPVVASGGISSLEDVaaLAAMTGQGVEGAIMGKALYAGRFS 235
Cdd:TIGR00735 161 AKEVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEAVKIPVIASGGAGKPEHF--YEAFTKGKADAALAASVFHYREIT 238


                  ...
gi 896138474  236 LEQ 238
Cdd:TIGR00735 239 IGE 241
HisF COG0107
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ...
 12-214 1.68e-19

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: 84.69  E-value: 1.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474  12 PAVDVQDGqavRLVQG-------EAGsatsygDPVTAALDWQRAGAEWIHLVDLDAAF-GRGDNREVMRRVVEEIGVKIE 83
Cdd:COG0107    7 PCLDVKDG---RVVKGvnfvnlrDAG------DPVELAKRYNEQGADELVFLDITASSeGRKTMLDVVRRVAEEVFIPLT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474  84 LSGGIRDDASLENALEMGAARVNLGTAALEDPEWTARVIERFGD-RVAVGLDVRgttlaargwtKEGGDLWEV------- 155
Cdd:COG0107   78 VGGGIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSqCIVVAIDAK----------RVPDGGWEVythggrk 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896138474 156 ---LD------RLEDAGCARYVVTDVTKDGTLKGPNTELLAQVCAKTAKPVVASGGISSLEDV----------AALAA 214
Cdd:COG0107  148 ptgLDavewakEAEELGAGEILLTSMDRDGTKDGYDLELTRAVSEAVSIPVIASGGAGTLEHFvevfteggadAALAA 225
OYE_like_4_FMN cd04735
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ...
 63-141 5.03e-05

Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.


Pssm-ID: 240086 [Multi-domain]  Cd Length: 353  Bit Score: 43.74  E-value: 5.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474  63 GRGDNREVMRRVVEEIGVKIEL--SGGIRDDASLENALEMGAARVNLGTAALEDPEWTARVIErfGDRVAVGLDVRGTTL 140
Cdd:cd04735  266 GRDDNQTIMELVKERIAGRLPLiaVGSINTPDDALEALETGADLVAIGRGLLVDPDWVEKIKE--GREDEINLEIDPDDL 343


                 .
gi 896138474 141 A 141
Cdd:cd04735  344 E 344
Dus pfam01207
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ...
 108-230 1.49e-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: 42.31  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474  108 GTAALEDPEWTARVIERFGDrvAVGLDVrgtTLAAR-GWTKEGGDLWEVLDRLEDAGCARYVVTDVTKDGTLKGP-NTEL 185
Cdd:pfam01207 100 GAALLRNPDLVAQIVKAVVK--AVGIPV---TVKIRiGWDDSHENAVEIAKIVEDAGAQALTVHGRTRAQNYEGTaDWDA 174

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 896138474  186 LAQVCAKTAKPVVASGGISSLEDvaALAAMTGQGVEGAIMGKALY 230
Cdd:pfam01207 175 IKQVKQAVSIPVIANGDITDPED--AQRCLAYTGADGVMIGRGAL 217
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 25-226 1.82e-04

TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.


Pssm-ID: 240073 [Multi-domain]  Cd Length: 200  Bit Score: 41.42  E-value: 1.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474  25 VQGEAGSATSYGDPVTAALDWQRAGAEWIHLVDLDAAF--GRGDNREVMRRVVEEIGVKIELSGGIRDDA-----SLENA 97
Cdd:cd04722    1 VILALLAGGPSGDPVELAKAAAEAGADAIIVGTRSSDPeeAETDDKEVLKEVAAETDLPLGVQLAINDAAaavdiAAAAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474  98 LEMGAARVNLGTAALEDPEWTARVI----ERFGDRVAVGLDVRGTTLAARGWTKEGGDLWevldrleDAGCARYVVTDVT 173
Cdd:cd04722   81 RAAGADGVEIHGAVGYLAREDLELIrelrEAVPDVKVVVKLSPTGELAAAAAEEAGVDEV-------GLGNGGGGGGGRD 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 896138474 174 KDGTLKgpntELLAQVCAKTAKPVVASGGISSLEDVAALAAMtgqGVEGAIMG 226
Cdd:cd04722  154 AVPIAD----LLLILAKRGSKVPVIAGGGINDPEDAAEALAL---GADGVIVG 199
DUS_like_FMN cd02801
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ...
 108-231 3.78e-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: 3.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474 108 GTAALEDPEWTARVIERFgdRVAVGLDVrgtTLAAR-GWTKEGgDLWEVLDRLEDAGCARYVVTDVTKDGTLKGP-NTEL 185
Cdd:cd02801  101 GAALLKDPELVAEIVRAV--REAVPIPV---TVKIRlGWDDEE-ETLELAKALEDAGASALTVHGRTREQRYSGPaDWDY 174

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 896138474 186 LAQVCAKTAKPVVASGGISSLEDVAALAAMTgqGVEGAIMGKALYA 231
Cdd:cd02801  175 IAEIKEAVSIPVIANGDIFSLEDALRCLEQT--GVDGVMIGRGALG 218
DusA COG0042
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ...
 97-217 4.88e-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: 40.85  E-value: 4.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474  97 ALEMGAARVNL--------------GTAALEDPEWTARVIERFgdRVAVGLDVrgtTLAAR-GWTKEGGDLWEVLDRLED 161
Cdd:COG0042   83 AEELGADEIDInmgcpvkkvtkggaGAALLRDPELVAEIVKAV--VEAVDVPV---TVKIRlGWDDDDENALEFARIAED 157

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474 162 AGCARYVV---TdvTKDGTlKGP-NTELLAQVCAKTAKPVVASGGISSLEDVAALAAMTG 217
Cdd:COG0042  158 AGAAALTVhgrT--REQRY-KGPaDWDAIARVKEAVSIPVIGNGDIFSPEDAKRMLEETG 214
YrpB COG2070
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ...
 185-226 2.00e-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: 38.94  E-value: 2.00e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 896138474 185 LLAQVCAKTAKPVVASGGISSLEDVAALAAMtgqGVEGAIMG 226
Cdd:COG2070  149 LVPEVRDAVDIPVIAAGGIADGRGIAAALAL---GADGVQMG 187
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 173-228 2.24e-03

Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate synthase is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440121 [Multi-domain]  Cd Length: 206  Bit Score: 38.24  E-value: 2.24e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 896138474 173 TKDGTLKGPNTELLAQVCAKTAKPVVASGGIsSLEDVAALAAMTGQG--VEGAIMGKA 228
Cdd:COG0352  134 TKPGAPPPLGLEGLAWWAELVEIPVVAIGGI-TPENAAEVLAAGADGvaVISAIWGAP 190
FadH COG1902
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ...
 89-214 3.85e-03

2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family [Energy production and conversion];


Pssm-ID: 441506 [Multi-domain]  Cd Length: 365  Bit Score: 38.23  E-value: 3.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474  89 RDDA---SLENalemgaaRVNLGTAALEdpewtaRVIERFGDRVAVGLDVRGTTLAARGWTKEggDLWEVLDRLEDAGCA 165
Cdd:COG1902  187 RTDEyggSLEN-------RARFLLEVVE------AVRAAVGPDFPVGVRLSPTDFVEGGLTLE--ESVELAKALEEAGVD 251

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 896138474 166 -------RYVVTDVTKDGTLKGPNTELLAQVCAKTAKPVVASGGISSLED-VAALAA 214
Cdd:COG1902  252 ylhvssgGYEPDAMIPTIVPEGYQLPFAARIRKAVGIPVIAVGGITTPEQaEAALAS 308
TMP-TENI pfam02581
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ...
 88-214 8.74e-03

Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl)thiazole phosphate to yield thiamine phosphate. This Pfam family also includes the regulatory protein TENI, a protein from Bacillus subtilis that regulates the production of several extracellular enzymes by reducing alkaline protease production. While TenI shows high sequence similarity with thiamin phosphate synthase, the purified protein has no thiamin phosphate synthase activity. Instead, it is a thiazole tautomerase.


Pssm-ID: 426849 [Multi-domain]  Cd Length: 180  Bit Score: 36.37  E-value: 8.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896138474   88 IRDDASLenALEMGAARVNLGtaalEDPEWTARVIERFGDRVAVGLDVRGTTLAARGwtkeggdlwevldrleDAGCARY 167
Cdd:pfam02581  61 INDRVDL--ALAVGADGVHLG----QDDLPVAEARELLGPDLIIGVSTHTLEEALEA----------------EALGADY 118

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 896138474  168 VV------TDVTKDGTLKGPntELLAQVCAKTAKPVVASGGIsSLEDVAALAA 214
Cdd:pfam02581 119 IGfgpifpTPTKPDAPPLGL--EGLKAIAEAVEIPVVAIGGI-TPENVPEVIE 168
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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