thiazole biosynthesis protein ThiH; Members this protein family are the ThiH protein of ...
3-369
0e+00
thiazole biosynthesis protein ThiH; Members this protein family are the ThiH protein of thiamine biosynthesis, a homolog of the BioB protein of biotin biosynthesis. Genes for the this protein generally are found in operons with other thiamin biosynthesis genes. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
The actual alignment was detected with superfamily member TIGR02351:
Pssm-ID: 131404 [Multi-domain] Cd Length: 366 Bit Score: 573.15 E-value: 0e+00
thiazole biosynthesis protein ThiH; Members this protein family are the ThiH protein of ...
3-369
0e+00
thiazole biosynthesis protein ThiH; Members this protein family are the ThiH protein of thiamine biosynthesis, a homolog of the BioB protein of biotin biosynthesis. Genes for the this protein generally are found in operons with other thiamin biosynthesis genes. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
Pssm-ID: 131404 [Multi-domain] Cd Length: 366 Bit Score: 573.15 E-value: 0e+00
2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE [Coenzyme ...
26-365
5.22e-97
2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE [Coenzyme transport and metabolism]; 2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 440680 [Multi-domain] Cd Length: 351 Bit Score: 292.42 E-value: 5.22e-97
Biotin and Thiamin Synthesis associated domain; Biotin synthase (BioB), , catalyses the last ...
258-361
3.30e-24
Biotin and Thiamin Synthesis associated domain; Biotin synthase (BioB), , catalyses the last step of the biotin biosynthetic pathway. The reaction consists in the introduction of a sulphur atom into dethiobiotin. BioB functions as a homodimer. Thiamin synthesis if a complex process involving at least six gene products (ThiFSGH, ThiI and ThiJ). Two of the proteins required for the biosynthesis of the thiazole moiety of thiamine (vitamin B(1)) are ThiG and ThiH (this entry) and form a heterodimer. Both of these reactions are thought of involve the binding of co-factors, and both function as dimers.. This domain therefore may be involved in co-factor binding or dimerisation.
Pssm-ID: 214877 [Multi-domain] Cd Length: 94 Bit Score: 95.24 E-value: 3.30e-24
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
79-286
1.29e-12
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity. They are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster. Mechanistically, they share the transfer of a single electron from the iron-sulfur cluster to SAM, which leads to its reductive cleavage to methionine and a 5'-deoxyadenosyl radical, which, in turn, abstracts a hydrogen from the appropriately positioned carbon atom. Depending on the enzyme, SAM is consumed during this process or it is restored and reused. Radical SAM enzymes catalyze steps in metabolism, DNA repair, the biosynthesis of vitamins and coenzymes, and the biosynthesis of many antibiotics. Examples are biotin synthase (BioB), lipoyl synthase (LipA), pyruvate formate-lyase (PFL), coproporphyrinogen oxidase (HemN), lysine 2,3-aminomutase (LAM), anaerobic ribonucleotide reductase (ARR), and MoaA, an enzyme of the biosynthesis of molybdopterin.
Pssm-ID: 100105 [Multi-domain] Cd Length: 204 Bit Score: 66.20 E-value: 1.29e-12
Biotin and Thiamin Synthesis associated domain; Biotin synthase (BioB), EC:2.8.1.6, catalyzes the last step of the biotin biosynthetic pathway. The reaction consists in the introduction of a sulphur atom into dethiobiotin. BioB functions as a homodimer. Thiamin synthesis if a complex process involving at least six gene products (ThiFSGH, ThiI and ThiJ). Two of the proteins required for the biosynthesis of the thiazole moiety of thiamine (vitamin B(1)) are ThiG and ThiH (this family) and form a heterodimer. Both of these reactions are thought of involve the binding of co-factors, and both function as dimers. This domain therefore may be involved in co-factor binding or dimerization (Finn, RD personal observation).
Pssm-ID: 462054 [Multi-domain] Cd Length: 85 Bit Score: 60.55 E-value: 8.10e-12
thiazole biosynthesis protein ThiH; Members this protein family are the ThiH protein of ...
3-369
0e+00
thiazole biosynthesis protein ThiH; Members this protein family are the ThiH protein of thiamine biosynthesis, a homolog of the BioB protein of biotin biosynthesis. Genes for the this protein generally are found in operons with other thiamin biosynthesis genes. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
Pssm-ID: 131404 [Multi-domain] Cd Length: 366 Bit Score: 573.15 E-value: 0e+00
2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE [Coenzyme ...
26-365
5.22e-97
2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE [Coenzyme transport and metabolism]; 2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 440680 [Multi-domain] Cd Length: 351 Bit Score: 292.42 E-value: 5.22e-97
[FeFe] hydrogenase H-cluster radical SAM maturase HydG; This model describes the radical SAM ...
55-361
1.34e-51
[FeFe] hydrogenase H-cluster radical SAM maturase HydG; This model describes the radical SAM protein HydG. It is part of an enzyme metallocenter maturation system, working together with GTP-binding protein HydF and another radical SAM enzyme, HydE, in H-cluster maturation in [FeFe] hydrogenases. [Protein fate, Protein modification and repair]
Pssm-ID: 274879 [Multi-domain] Cd Length: 471 Bit Score: 178.38 E-value: 1.34e-51
Biotin and Thiamin Synthesis associated domain; Biotin synthase (BioB), , catalyses the last ...
258-361
3.30e-24
Biotin and Thiamin Synthesis associated domain; Biotin synthase (BioB), , catalyses the last step of the biotin biosynthetic pathway. The reaction consists in the introduction of a sulphur atom into dethiobiotin. BioB functions as a homodimer. Thiamin synthesis if a complex process involving at least six gene products (ThiFSGH, ThiI and ThiJ). Two of the proteins required for the biosynthesis of the thiazole moiety of thiamine (vitamin B(1)) are ThiG and ThiH (this entry) and form a heterodimer. Both of these reactions are thought of involve the binding of co-factors, and both function as dimers.. This domain therefore may be involved in co-factor binding or dimerisation.
Pssm-ID: 214877 [Multi-domain] Cd Length: 94 Bit Score: 95.24 E-value: 3.30e-24
Biotin synthase or related enzyme [Coenzyme transport and metabolism]; Biotin synthase or ...
36-303
5.38e-18
Biotin synthase or related enzyme [Coenzyme transport and metabolism]; Biotin synthase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 440268 [Multi-domain] Cd Length: 308 Bit Score: 83.56 E-value: 5.38e-18
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
79-286
1.29e-12
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity. They are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster. Mechanistically, they share the transfer of a single electron from the iron-sulfur cluster to SAM, which leads to its reductive cleavage to methionine and a 5'-deoxyadenosyl radical, which, in turn, abstracts a hydrogen from the appropriately positioned carbon atom. Depending on the enzyme, SAM is consumed during this process or it is restored and reused. Radical SAM enzymes catalyze steps in metabolism, DNA repair, the biosynthesis of vitamins and coenzymes, and the biosynthesis of many antibiotics. Examples are biotin synthase (BioB), lipoyl synthase (LipA), pyruvate formate-lyase (PFL), coproporphyrinogen oxidase (HemN), lysine 2,3-aminomutase (LAM), anaerobic ribonucleotide reductase (ARR), and MoaA, an enzyme of the biosynthesis of molybdopterin.
Pssm-ID: 100105 [Multi-domain] Cd Length: 204 Bit Score: 66.20 E-value: 1.29e-12
[FeFe] hydrogenase H-cluster radical SAM maturase HydE; This model describes the radical SAM ...
35-131
1.43e-12
[FeFe] hydrogenase H-cluster radical SAM maturase HydE; This model describes the radical SAM protein HydE, one of a pair of radical SAM proteins, along with GTP-binding protein HydF, for maturation of [Fe] hydrogenase in Chlamydomonas reinhardtii and numerous bacteria. [Protein fate, Protein modification and repair]
Pssm-ID: 274880 [Multi-domain] Cd Length: 340 Bit Score: 67.97 E-value: 1.43e-12
Biotin and Thiamin Synthesis associated domain; Biotin synthase (BioB), EC:2.8.1.6, catalyzes the last step of the biotin biosynthetic pathway. The reaction consists in the introduction of a sulphur atom into dethiobiotin. BioB functions as a homodimer. Thiamin synthesis if a complex process involving at least six gene products (ThiFSGH, ThiI and ThiJ). Two of the proteins required for the biosynthesis of the thiazole moiety of thiamine (vitamin B(1)) are ThiG and ThiH (this family) and form a heterodimer. Both of these reactions are thought of involve the binding of co-factors, and both function as dimers. This domain therefore may be involved in co-factor binding or dimerization (Finn, RD personal observation).
Pssm-ID: 462054 [Multi-domain] Cd Length: 85 Bit Score: 60.55 E-value: 8.10e-12
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
81-230
9.66e-07
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual methylations, isomerization, sulphur insertion, ring formation, anaerobic oxidation and protein radical formation.
Pssm-ID: 427681 [Multi-domain] Cd Length: 159 Bit Score: 48.29 E-value: 9.66e-07
radical SAM domain protein, CofH subfamily; This protein family includes the CofH protein of ...
82-166
7.13e-03
radical SAM domain protein, CofH subfamily; This protein family includes the CofH protein of coenzyme F(420) biosynthesis from Methanocaldococcus jannaschii, but appears to hit genomes more broadly than just the subset that make coenzyme F(420), so that narrower group is being built as a separate family. [Hypothetical proteins, Conserved]
Pssm-ID: 273071 [Multi-domain] Cd Length: 309 Bit Score: 38.14 E-value: 7.13e-03
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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