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Conserved domains on  [gi|6324429|ref|NP_014498|]
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lumazine synthase RIB4 [Saccharomyces cerevisiae S288C]

Protein Classification

6,7-dimethyl-8-ribityllumazine synthase( domain architecture ID 10794454)

6,7-dimethyl-8-ribityllumazine synthase catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione with 3,4-dihydroxy-2-butanone in riboflavin biosynthesis pathway

CATH:  3.40.50.960
EC:  2.5.1.78
Gene Ontology:  GO:0000906|GO:0009231|GO:0009349
PubMed:  11153262|16010344
SCOP:  4003586

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
lumazine-synth TIGR00114
6,7-dimethyl-8-ribityllumazine synthase; This enzyme catalyzes the cyclo-ligation of 3, ...
 18-164 7.07e-63

6,7-dimethyl-8-ribityllumazine synthase; This enzyme catalyzes the cyclo-ligation of 3,4-dihydroxy-2-butanone-4-P and 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione to form 6,7-dimethyl-8-ribityllumazine, the immediate precursor of riboflavin. Sometimes referred to as riboflavin synthase, beta subunit, this should not be confused with the alpha subunit which carries out the subsequent reaction. Archaeal members of this family are considered putative, although included in the seed and scoring above the trusted cutoff. [Biosynthesis of cofactors, prosthetic groups, and carriers, Riboflavin, FMN, and FAD]


:

Pssm-ID: 211550  Cd Length: 138  Bit Score: 189.88  E-value: 7.07e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324429     18 IRVGIIHARWNRVIIDALVKGAIERMASLGVEENNIIIETVPGSYELPWGTKRFVDRQAklgkpLDVVIPIGVLIKGSTM 97
Cdd:TIGR00114   1 VRVGIVIARFNRFITDMLLKGAIDALKRLGAEVDNIDVIWVPGAFELPLAVKKLAESGK-----YDAVIALGTVIRGGTP 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6324429     98 HFEYISDSTTHALMNLQEKVDMPVIFGLLTCMTEEQALARAGIDEAhsmhNHGEDWGAAAVEMAVKF 164
Cdd:TIGR00114  76 HFEYVADEAAKGIADLALDYGKPVIFGILTTETIEQAIERAGTKAG----NKGVEAAVKALEMANLL 138
 
Name Accession Description Interval E-value
lumazine-synth TIGR00114
6,7-dimethyl-8-ribityllumazine synthase; This enzyme catalyzes the cyclo-ligation of 3, ...
 18-164 7.07e-63

6,7-dimethyl-8-ribityllumazine synthase; This enzyme catalyzes the cyclo-ligation of 3,4-dihydroxy-2-butanone-4-P and 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione to form 6,7-dimethyl-8-ribityllumazine, the immediate precursor of riboflavin. Sometimes referred to as riboflavin synthase, beta subunit, this should not be confused with the alpha subunit which carries out the subsequent reaction. Archaeal members of this family are considered putative, although included in the seed and scoring above the trusted cutoff. [Biosynthesis of cofactors, prosthetic groups, and carriers, Riboflavin, FMN, and FAD]


Pssm-ID: 211550  Cd Length: 138  Bit Score: 189.88  E-value: 7.07e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324429     18 IRVGIIHARWNRVIIDALVKGAIERMASLGVEENNIIIETVPGSYELPWGTKRFVDRQAklgkpLDVVIPIGVLIKGSTM 97
Cdd:TIGR00114   1 VRVGIVIARFNRFITDMLLKGAIDALKRLGAEVDNIDVIWVPGAFELPLAVKKLAESGK-----YDAVIALGTVIRGGTP 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6324429     98 HFEYISDSTTHALMNLQEKVDMPVIFGLLTCMTEEQALARAGIDEAhsmhNHGEDWGAAAVEMAVKF 164
Cdd:TIGR00114  76 HFEYVADEAAKGIADLALDYGKPVIFGILTTETIEQAIERAGTKAG----NKGVEAAVKALEMANLL 138
Lumazine_synthase-I cd09209
lumazine synthase (6,7-dimethyl-8-ribityllumazine synthase, LS), catalyzes the penultimate ...
 20-161 5.55e-61

lumazine synthase (6,7-dimethyl-8-ribityllumazine synthase, LS), catalyzes the penultimate step in the biosynthesis of riboflavin (vitamin B2); type-I; Type-I LS, also known as RibH1, catalyzes the penultimate step in the biosynthesis of riboflavin in plants and microorganisms. LS catalyse the formation of 6,7-dimethyl-8-ribityllumazine by the condensation of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione with 3,4-dihydroxy- 2-butanone-4-phosphate. Subsequently, the lumazine intermediate dismutates to yield riboflavin and 5-amino-6-ribitylamino- 2,4(1H,3H)-pyrimidinedione, in a reaction catalyzed by riboflavin synthase synthase (RS); RS belongs to a different family of the Lumazine-synthase-like superfamily. Riboflavin is the precursor of flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) which are essential cofactors for the catalysis of a wide range of redox reactions. These cofactors are also involved in many other processes involving DNA repair, circadian time-keeping, light sensing, and bioluminescence. Riboflavin is biosynthesized in plants, fungi and certain microorganisms; as animals lack the necessary enzymes to produce this vitamin, they acquire it from dietary sources. Type II LSs are distinct from type-I LS not only in protein sequence, but in that they exhibit different quaternary assemblies; type-I LSs form pentamers. The pathogen Brucella spp. encode both a Type-I LS and a Type-II LS called RibH1 and RibH2, respectively. RibH1/type-I LS appears to be the functional LS in Brucella spp., whereas RibH2/type-II LS has much lower catalytic activity as LS. The pathogen Brucella spp. have both a type-I LS and a type-II LS called RibH1 and RibH2, respectively. RibH1/type-I LS appears to be a functional LS in Brucella spp., whereas RibH2/type-II LS has much lower catalytic activity as LS.


Pssm-ID: 187742  Cd Length: 133  Bit Score: 184.96  E-value: 5.55e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324429   20 VGIIHARWNRVIIDALVKGAIERMASLGVEENNIIIETVPGSYELPWGTKRFVDRqaklgKPLDVVIPIGVLIKGSTMHF 99
Cdd:cd09209   1 IAIVVSRFNEEITDALLEGALDALKRHGVKEENIDVVRVPGAFEIPLAAKRLARS-----GKYDAIIALGCVIRGETPHF 75

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6324429  100 EYISDSTTHALMNLQEKVDMPVIFGLLTCMTEEQALARAGIDeahsMHNHGEDWGAAAVEMA 161
Cdd:cd09209  76 DYVCNEVTRGLMRLSLETGVPVIFGVLTTDNEEQALERAGGK----AGNKGAEAALAALEMA 133
DMRL_synthase pfam00885
6,7-dimethyl-8-ribityllumazine synthase; This family includes the beta chain of 6, ...
 17-160 4.36e-56

6,7-dimethyl-8-ribityllumazine synthase; This family includes the beta chain of 6,7-dimethyl-8- ribityllumazine synthase EC:2.5.1.9, an enzyme involved in riboflavin biosynthesis. The family also includes a subfamily of distant archaebacterial proteins that may also have the same function for example Swiss:O28856. The family contains a number of different subsets including a family of proteins comprising archaeal lumazine and riboflavin synthases, type I lumazine synthases, and the eubacterial type II lumazine synthases. It has been established that lumazine synthase catalyzes the penultimate step in the biosynthesis of riboflavin in plants and microorganizms. The type I lumazine synthases area active in pentameric or icosahedral quaternary assemblies, whereas the type II are decameric. Brucella, a bacterial genus that causes brucellosis, and other Rhizobiales have an atypical riboflavin metabolic pathway. Brucella spp code for both a type-I and a type-II lumazine synthase, and it has been shown that at least one of these two has to be present in order for Brucella to be viable, showing that in the case of Brucella flavin metabolism is implicated in bacterial virulence.


Pssm-ID: 459980  Cd Length: 134  Bit Score: 172.59  E-value: 4.36e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324429     17 KIRVGIIHARWNRVIIDALVKGAIERMASLGVEENnIIIETVPGSYELPWGTKRFvdrqAKLGKpLDVVIPIGVLIKGST 96
Cdd:pfam00885   1 GLRIGIVVARFNEDITDRLLEGALDALKRHGVAEN-IDVVRVPGAFELPLAAKKL----AESGK-YDAVIALGAVIRGET 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6324429     97 MHFEYISDSTTHALMNLQEKVDMPVIFGLLTCMTEEQALARAGIDeahsMHNHGEDWGAAAVEM 160
Cdd:pfam00885  75 PHFDYVANEVAKGLMDVSLDTGVPVIFGVLTTDTEEQALERAGGK----AGNKGREAAEAALEM 134
RibE COG0054
6,7-dimethyl-8-ribityllumazine synthase (Riboflavin synthase beta chain) [Coenzyme transport ...
 14-161 1.82e-48

6,7-dimethyl-8-ribityllumazine synthase (Riboflavin synthase beta chain) [Coenzyme transport and metabolism]; 6,7-dimethyl-8-ribityllumazine synthase (Riboflavin synthase beta chain) is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis


Pssm-ID: 439824  Cd Length: 152  Bit Score: 153.70  E-value: 1.82e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324429   14 DGSKIRVGIIHARWNRVIIDALVKGAIERMASLGVEENNIIIETVPGSYELPWGTKRFvdrqAKLGKPlDVVIPIGVLIK 93
Cdd:COG0054   7 PASGLRIAIVVARFNEDITDKLLEGALDALKRHGVSEENIDVVRVPGAFEIPLAAKKL----AESGRY-DAVIALGCVIR 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6324429   94 GSTMHFEYISDSTTHALMNLQEKVDMPVIFGLLTCMTEEQALARAGIdeahSMHNHGEDWGAAAVEMA 161
Cdd:COG0054  82 GETPHFDYVANEVTKGLMQVSLDTGVPVGFGVLTTDTIEQAIERAGG----KAGNKGAEAALAALEMA 145
PLN02404 PLN02404
6,7-dimethyl-8-ribityllumazine synthase
 12-160 7.14e-43

6,7-dimethyl-8-ribityllumazine synthase


Pssm-ID: 178026  Cd Length: 141  Bit Score: 139.49  E-value: 7.14e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324429    12 VYDGSKIRVGIIHARWNRVIIDALVKGAIERMASLGVEENNIIIETVPGSYELPWGTKRFvdrqAKLGKpLDVVIPIGVL 91
Cdd:PLN02404   2 LLDGEGLRFGVVVARFNEIITKNLLEGALETFKRYSVKEENIDVVWVPGSFEIPVVAQRL----AKSGK-YDAILCIGAV 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6324429    92 IKGSTMHFEYISDSTTHALMNLQEKVDMPVIFGLLTCMTEEQALARAGIDEAhsmhNHGEDWGAAAVEM 160
Cdd:PLN02404  77 IRGDTTHYDAVANSAASGVLSAGLNSGVPCIFGVLTCDDMEQALNRAGGKAG----NKGAEAALTAVEM 141
 
Name Accession Description Interval E-value
lumazine-synth TIGR00114
6,7-dimethyl-8-ribityllumazine synthase; This enzyme catalyzes the cyclo-ligation of 3, ...
 18-164 7.07e-63

6,7-dimethyl-8-ribityllumazine synthase; This enzyme catalyzes the cyclo-ligation of 3,4-dihydroxy-2-butanone-4-P and 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione to form 6,7-dimethyl-8-ribityllumazine, the immediate precursor of riboflavin. Sometimes referred to as riboflavin synthase, beta subunit, this should not be confused with the alpha subunit which carries out the subsequent reaction. Archaeal members of this family are considered putative, although included in the seed and scoring above the trusted cutoff. [Biosynthesis of cofactors, prosthetic groups, and carriers, Riboflavin, FMN, and FAD]


Pssm-ID: 211550  Cd Length: 138  Bit Score: 189.88  E-value: 7.07e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324429     18 IRVGIIHARWNRVIIDALVKGAIERMASLGVEENNIIIETVPGSYELPWGTKRFVDRQAklgkpLDVVIPIGVLIKGSTM 97
Cdd:TIGR00114   1 VRVGIVIARFNRFITDMLLKGAIDALKRLGAEVDNIDVIWVPGAFELPLAVKKLAESGK-----YDAVIALGTVIRGGTP 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6324429     98 HFEYISDSTTHALMNLQEKVDMPVIFGLLTCMTEEQALARAGIDEAhsmhNHGEDWGAAAVEMAVKF 164
Cdd:TIGR00114  76 HFEYVADEAAKGIADLALDYGKPVIFGILTTETIEQAIERAGTKAG----NKGVEAAVKALEMANLL 138
Lumazine_synthase-I cd09209
lumazine synthase (6,7-dimethyl-8-ribityllumazine synthase, LS), catalyzes the penultimate ...
 20-161 5.55e-61

lumazine synthase (6,7-dimethyl-8-ribityllumazine synthase, LS), catalyzes the penultimate step in the biosynthesis of riboflavin (vitamin B2); type-I; Type-I LS, also known as RibH1, catalyzes the penultimate step in the biosynthesis of riboflavin in plants and microorganisms. LS catalyse the formation of 6,7-dimethyl-8-ribityllumazine by the condensation of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione with 3,4-dihydroxy- 2-butanone-4-phosphate. Subsequently, the lumazine intermediate dismutates to yield riboflavin and 5-amino-6-ribitylamino- 2,4(1H,3H)-pyrimidinedione, in a reaction catalyzed by riboflavin synthase synthase (RS); RS belongs to a different family of the Lumazine-synthase-like superfamily. Riboflavin is the precursor of flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) which are essential cofactors for the catalysis of a wide range of redox reactions. These cofactors are also involved in many other processes involving DNA repair, circadian time-keeping, light sensing, and bioluminescence. Riboflavin is biosynthesized in plants, fungi and certain microorganisms; as animals lack the necessary enzymes to produce this vitamin, they acquire it from dietary sources. Type II LSs are distinct from type-I LS not only in protein sequence, but in that they exhibit different quaternary assemblies; type-I LSs form pentamers. The pathogen Brucella spp. encode both a Type-I LS and a Type-II LS called RibH1 and RibH2, respectively. RibH1/type-I LS appears to be the functional LS in Brucella spp., whereas RibH2/type-II LS has much lower catalytic activity as LS. The pathogen Brucella spp. have both a type-I LS and a type-II LS called RibH1 and RibH2, respectively. RibH1/type-I LS appears to be a functional LS in Brucella spp., whereas RibH2/type-II LS has much lower catalytic activity as LS.


Pssm-ID: 187742  Cd Length: 133  Bit Score: 184.96  E-value: 5.55e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324429   20 VGIIHARWNRVIIDALVKGAIERMASLGVEENNIIIETVPGSYELPWGTKRFVDRqaklgKPLDVVIPIGVLIKGSTMHF 99
Cdd:cd09209   1 IAIVVSRFNEEITDALLEGALDALKRHGVKEENIDVVRVPGAFEIPLAAKRLARS-----GKYDAIIALGCVIRGETPHF 75

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6324429  100 EYISDSTTHALMNLQEKVDMPVIFGLLTCMTEEQALARAGIDeahsMHNHGEDWGAAAVEMA 161
Cdd:cd09209  76 DYVCNEVTRGLMRLSLETGVPVIFGVLTTDNEEQALERAGGK----AGNKGAEAALAALEMA 133
DMRL_synthase pfam00885
6,7-dimethyl-8-ribityllumazine synthase; This family includes the beta chain of 6, ...
 17-160 4.36e-56

6,7-dimethyl-8-ribityllumazine synthase; This family includes the beta chain of 6,7-dimethyl-8- ribityllumazine synthase EC:2.5.1.9, an enzyme involved in riboflavin biosynthesis. The family also includes a subfamily of distant archaebacterial proteins that may also have the same function for example Swiss:O28856. The family contains a number of different subsets including a family of proteins comprising archaeal lumazine and riboflavin synthases, type I lumazine synthases, and the eubacterial type II lumazine synthases. It has been established that lumazine synthase catalyzes the penultimate step in the biosynthesis of riboflavin in plants and microorganizms. The type I lumazine synthases area active in pentameric or icosahedral quaternary assemblies, whereas the type II are decameric. Brucella, a bacterial genus that causes brucellosis, and other Rhizobiales have an atypical riboflavin metabolic pathway. Brucella spp code for both a type-I and a type-II lumazine synthase, and it has been shown that at least one of these two has to be present in order for Brucella to be viable, showing that in the case of Brucella flavin metabolism is implicated in bacterial virulence.


Pssm-ID: 459980  Cd Length: 134  Bit Score: 172.59  E-value: 4.36e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324429     17 KIRVGIIHARWNRVIIDALVKGAIERMASLGVEENnIIIETVPGSYELPWGTKRFvdrqAKLGKpLDVVIPIGVLIKGST 96
Cdd:pfam00885   1 GLRIGIVVARFNEDITDRLLEGALDALKRHGVAEN-IDVVRVPGAFELPLAAKKL----AESGK-YDAVIALGAVIRGET 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6324429     97 MHFEYISDSTTHALMNLQEKVDMPVIFGLLTCMTEEQALARAGIDeahsMHNHGEDWGAAAVEM 160
Cdd:pfam00885  75 PHFDYVANEVAKGLMDVSLDTGVPVIFGVLTTDTEEQALERAGGK----AGNKGREAAEAALEM 134
Lumazine_synthase-like cd08371
lumazine synthase and riboflavin synthase; involved in the riboflavin (vitamin B2) ...
 20-159 1.53e-51

lumazine synthase and riboflavin synthase; involved in the riboflavin (vitamin B2) biosynthetic pathway; This superfamily contains lumazine synthase (6,7-dimethyl-8-ribityllumazine synthase, LS) and riboflavin synthase (RS). Both enzymes play important roles in the riboflavin biosynthetic pathway. Riboflavin is the precursor of flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) which are essential cofactors for the catalysis of a wide range of redox reactions. These cofactors are also involved in many other processes involving DNA repair, circadian time-keeping, light sensing, and bioluminescence. Riboflavin is biosynthesized in plants, fungi and certain microorganisms; as animals lack the necessary enzymes to produce this vitamin, they acquire it from dietary sources. In the final steps of the riboflavin biosynthetic pathway, LS catalyzes the condensation of the 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione with 3,4-dihydroxy- 2-butanone-4-phosphate to release water, inorganic phosphate and 6,7-dimethyl-8-ribityllumazine (DMRL), and RS catalyzes a dismutation of DMRL which yields riboflavin and 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione. In the latter reaction, a four-carbon moiety is transferred between two DMRL molecules serving as donor and acceptor, respectively. Both the LS and RS catalyzed reactions are thermodynamically irreversible and can proceed in the absence of a catalyst. In bacteria and eukaryotes, there are two types of LS: type-I LS forms homo-pentamers or icosahedrally arranged dodecamers of pentamers, type-II LS forms decamers (dimers of pentamers). In archaea LSs and RSs appear to have diverged early in the evolution of archaea from a common ancestor.


Pssm-ID: 187740  Cd Length: 129  Bit Score: 161.04  E-value: 1.53e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324429   20 VGIIHARWNRVIIDALVKGAIERMASLGVEeNNIIIETVPGSYELPWGTKRFVDRQaklgkPLDVVIPIGVLIKGSTMHF 99
Cdd:cd08371   1 VGIVDARFNRDIVDALVKGAIAELAELGGN-IKIIVVTVPGAYEIPLAAKKLLEKE-----DYDAVVAIGVVIKGETYHF 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6324429  100 EYISDSTTHALMNLQEKVDMPVIFGLLTCMT-EEQALARAGIdeahsmHNHGEDWGAAAVE 159
Cdd:cd08371  75 EIVAHEVSRGLMNLQLETDKPVIFGVLTPDNaEEQADERAKR------GNKGEEAARAAVE 129
RibE COG0054
6,7-dimethyl-8-ribityllumazine synthase (Riboflavin synthase beta chain) [Coenzyme transport ...
 14-161 1.82e-48

6,7-dimethyl-8-ribityllumazine synthase (Riboflavin synthase beta chain) [Coenzyme transport and metabolism]; 6,7-dimethyl-8-ribityllumazine synthase (Riboflavin synthase beta chain) is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis


Pssm-ID: 439824  Cd Length: 152  Bit Score: 153.70  E-value: 1.82e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324429   14 DGSKIRVGIIHARWNRVIIDALVKGAIERMASLGVEENNIIIETVPGSYELPWGTKRFvdrqAKLGKPlDVVIPIGVLIK 93
Cdd:COG0054   7 PASGLRIAIVVARFNEDITDKLLEGALDALKRHGVSEENIDVVRVPGAFEIPLAAKKL----AESGRY-DAVIALGCVIR 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6324429   94 GSTMHFEYISDSTTHALMNLQEKVDMPVIFGLLTCMTEEQALARAGIdeahSMHNHGEDWGAAAVEMA 161
Cdd:COG0054  82 GETPHFDYVANEVTKGLMQVSLDTGVPVGFGVLTTDTIEQAIERAGG----KAGNKGAEAALAALEMA 145
PLN02404 PLN02404
6,7-dimethyl-8-ribityllumazine synthase
 12-160 7.14e-43

6,7-dimethyl-8-ribityllumazine synthase


Pssm-ID: 178026  Cd Length: 141  Bit Score: 139.49  E-value: 7.14e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324429    12 VYDGSKIRVGIIHARWNRVIIDALVKGAIERMASLGVEENNIIIETVPGSYELPWGTKRFvdrqAKLGKpLDVVIPIGVL 91
Cdd:PLN02404   2 LLDGEGLRFGVVVARFNEIITKNLLEGALETFKRYSVKEENIDVVWVPGSFEIPVVAQRL----AKSGK-YDAILCIGAV 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6324429    92 IKGSTMHFEYISDSTTHALMNLQEKVDMPVIFGLLTCMTEEQALARAGIDEAhsmhNHGEDWGAAAVEM 160
Cdd:PLN02404  77 IRGDTTHYDAVANSAASGVLSAGLNSGVPCIFGVLTCDDMEQALNRAGGKAG----NKGAEAALTAVEM 141
ribH PRK00061
6,7-dimethyl-8-ribityllumazine synthase; Provisional
 14-161 7.41e-42

6,7-dimethyl-8-ribityllumazine synthase; Provisional


Pssm-ID: 234606  Cd Length: 154  Bit Score: 137.18  E-value: 7.41e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324429    14 DGSKIRVGIIHARWNRVIIDALVKGAIERMASLGVEENNIIIETVPGSYELPWGTKRFVDRqaklgKPLDVVIPIGVLIK 93
Cdd:PRK00061   9 VAKGLRIGIVVARFNDFITDALLEGALDALKRHGVSEENIDVVRVPGAFEIPLAAKKLAES-----GKYDAVIALGAVIR 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6324429    94 GSTMHFEYISDSTTHALMNLQEKVDMPVIFGLLTCMTEEQALARAGideaHSMHNHGEDWGAAAVEMA 161
Cdd:PRK00061  84 GETPHFDYVANEVAKGLADVSLETGVPVGFGVLTTDTIEQAIERAG----TKAGNKGAEAALAALEMA 147
Lumazine_synthase-II cd09208
lumazine synthase (6,7-dimethyl-8-ribityllumazine synthase, LS), catalyzes the penultimate ...
 19-127 3.86e-12

lumazine synthase (6,7-dimethyl-8-ribityllumazine synthase, LS), catalyzes the penultimate step in the biosynthesis of riboflavin (vitamin B2); type-II; Type-II LS also known as RibH2, catalyzes the penultimate step in the biosynthesis of riboflavin in plants and microorganisms. LS catalyses the formation of 6,7-dimethyl-8-ribityllumazine by the condensation of 5-amino-6-ribitylamino- 2,4(1H,3H)-pyrimidinedione with 3,4-dihydroxy- 2-butanone-4-phosphate. Subsequently, the lumazine intermediate dismutates yielding riboflavin and 5-amino-6-ribitylamino- 2,4(1H,3H)-pyrimidinedione, in a reaction catalyzed by riboflavin synthase (RS); RS belongs to a different family of the Lumazine-synthase-like superfamily. Riboflavin is the precursor of flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) which are essential cofactors for the catalysis of a wide range of redox reactions. These cofactors are also involved in many other processes involving DNA repair, circadian time-keeping, light sensing, and bioluminescence. Riboflavin is biosynthesized in plants, fungi and certain microorganisms; as animals lack the necessary enzymes to produce this vitamin, they acquire it from dietary sources. Type II LSs are distinct from type-I LS not only in protein sequence, but in that they exhibit different quaternary assemblies; type-II LSs form decamers (dimers of pentamers). The pathogen Brucella spp. have both a type-I LS and a type-II LS called RibH1 and RibH2, respectively. RibH1/type-I LS appears to be a functional LS in Brucella spp., whereas RibH2/type-II LS has much lower catalytic activity as LS and may be regulated by a riboswitch that senses FMN, suggesting that the type-II LSs may have evolved into very poor catalysts or, that they may harbor a new, as-yet-unknown function.


Pssm-ID: 187741  Cd Length: 137  Bit Score: 60.12  E-value: 3.86e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324429   19 RVGIIHARWNRVIIDALVKGAIERMASLGVEENNIIIETVPGSYELPWGTKRFvdrqAKLGKpLDVVIPIGVLIKGSTMH 98
Cdd:cd09208   2 RIAFIQARWHADIVDQARKGFEAEMAAKGGASDEVDIFDVPGAFEIPLHAKRL----ARTGR-YAAIVGAALVVDGGIYR 76

                        90       100
                ....*....|....*....|....*....
gi 6324429   99 FEYISDSTTHALMNLQEKVDMPVIFGLLT 127
Cdd:cd09208  77 HEFVAQAVIDGLMRVQLETEVPVFSVVLT 105
PRK12419 PRK12419
6,7-dimethyl-8-ribityllumazine synthase;
19-127 3.62e-10

6,7-dimethyl-8-ribityllumazine synthase;


Pssm-ID: 237096  Cd Length: 158  Bit Score: 55.42  E-value: 3.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324429    19 RVGIIHARWNRVIIDALVKGAIERMASLGVEENNIIIETVPGSYELPWGTKRFvdrqAKLGKpLDVVIPIGVLIKGSTMH 98
Cdd:PRK12419  12 RIAFIQARWHADIVDQARKGFVAEIAARGGAASQVDIFDVPGAFEIPLHAQTL----AKTGR-YAAIVAAALVVDGGIYR 86

                         90       100
                 ....*....|....*....|....*....
gi 6324429    99 FEYISDSTTHALMNLQEKVDMPVIFGLLT 127
Cdd:PRK12419  87 HEFVAQAVIDGLMRVQLDTEVPVFSVVLT 115
 
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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