MULTISPECIES: thiazole synthase [Mycobacteriaceae]
Protein Classification
thiazole synthase( domain architecture ID 18578739)
thiazole synthase (ThiG) catalyzes the formation of thiazole from 1-deoxy-D-xylulose 5-phosphate (DXP) and dehydroglycine
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| ThiG | COG2022 | Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) [Coenzyme transport and ... |
1-250 | 7.30e-147 | |||||
Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) [Coenzyme transport and metabolism]; Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) is part of the Pathway/BioSystem: Thiamine biosynthesis : Pssm-ID: 441625 Cd Length: 259 Bit Score: 410.58 E-value: 7.30e-147
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| Name | Accession | Description | Interval | E-value | |||||
| ThiG | COG2022 | Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) [Coenzyme transport and ... |
1-250 | 7.30e-147 | |||||
Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) [Coenzyme transport and metabolism]; Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) is part of the Pathway/BioSystem: Thiamine biosynthesis Pssm-ID: 441625 Cd Length: 259 Bit Score: 410.58 E-value: 7.30e-147
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| thiG | PRK00208 | thiazole synthase; Reviewed |
5-250 | 3.52e-144 | |||||
thiazole synthase; Reviewed Pssm-ID: 234687 Cd Length: 250 Bit Score: 403.29 E-value: 3.52e-144
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| ThiG | pfam05690 | Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole ... |
8-250 | 7.43e-129 | |||||
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole biosynthesis protein G sequences. ThiG, together with ThiF and ThiH, is proposed to be involved in the synthesis of 4-methyl-5-(b-hydroxyethyl)thiazole (THZ) which is an intermediate in the thiazole production pathway. This family also includes triosephosphate isomerase and pyridoxal 5'-phosphate synthase subunit PdxS. Pssm-ID: 428589 Cd Length: 247 Bit Score: 364.65 E-value: 7.43e-129
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| ThiG | cd04728 | Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the ... |
6-250 | 4.81e-128 | |||||
Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the thiazole moiety of thiamin pyrophosphate, an essential ubiquitous cofactor that plays an important role in carbohydrate and amino acid metabolism. ThiG catalyzes the formation of thiazole from 1-deoxy-D-xylulose 5-phosphate (DXP) and dehydroglycine, with the help of the sulfur carrier protein ThiS that carries the sulfur needed for thiazole assembly on its carboxy terminus (ThiS-COSH). Pssm-ID: 240079 Cd Length: 248 Bit Score: 362.58 E-value: 4.81e-128
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| Name | Accession | Description | Interval | E-value | |||||
| ThiG | COG2022 | Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) [Coenzyme transport and ... |
1-250 | 7.30e-147 | |||||
Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) [Coenzyme transport and metabolism]; Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) is part of the Pathway/BioSystem: Thiamine biosynthesis Pssm-ID: 441625 Cd Length: 259 Bit Score: 410.58 E-value: 7.30e-147
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| thiG | PRK00208 | thiazole synthase; Reviewed |
5-250 | 3.52e-144 | |||||
thiazole synthase; Reviewed Pssm-ID: 234687 Cd Length: 250 Bit Score: 403.29 E-value: 3.52e-144
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| ThiG | pfam05690 | Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole ... |
8-250 | 7.43e-129 | |||||
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole biosynthesis protein G sequences. ThiG, together with ThiF and ThiH, is proposed to be involved in the synthesis of 4-methyl-5-(b-hydroxyethyl)thiazole (THZ) which is an intermediate in the thiazole production pathway. This family also includes triosephosphate isomerase and pyridoxal 5'-phosphate synthase subunit PdxS. Pssm-ID: 428589 Cd Length: 247 Bit Score: 364.65 E-value: 7.43e-129
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| ThiG | cd04728 | Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the ... |
6-250 | 4.81e-128 | |||||
Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the thiazole moiety of thiamin pyrophosphate, an essential ubiquitous cofactor that plays an important role in carbohydrate and amino acid metabolism. ThiG catalyzes the formation of thiazole from 1-deoxy-D-xylulose 5-phosphate (DXP) and dehydroglycine, with the help of the sulfur carrier protein ThiS that carries the sulfur needed for thiazole assembly on its carboxy terminus (ThiS-COSH). Pssm-ID: 240079 Cd Length: 248 Bit Score: 362.58 E-value: 4.81e-128
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| PRK11840 | PRK11840 | bifunctional sulfur carrier protein/thiazole synthase protein; Provisional |
1-250 | 4.05e-97 | |||||
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional Pssm-ID: 236998 [Multi-domain] Cd Length: 326 Bit Score: 287.03 E-value: 4.05e-97
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| thiG | CHL00162 | thiamin biosynthesis protein G; Validated |
5-250 | 2.44e-92 | |||||
thiamin biosynthesis protein G; Validated Pssm-ID: 214380 Cd Length: 267 Bit Score: 272.74 E-value: 2.44e-92
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| PRK04302 | PRK04302 | triosephosphate isomerase; Provisional |
158-216 | 8.05e-09 | |||||
triosephosphate isomerase; Provisional Pssm-ID: 235274 Cd Length: 223 Bit Score: 54.10 E-value: 8.05e-09
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| TIM_phosphate_binding | cd04722 | TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
73-208 | 3.65e-07 | |||||
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: 49.12 E-value: 3.65e-07
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| NanE | cd04729 | N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
169-212 | 8.45e-05 | |||||
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to N-acetylglucosamine-6-phosphate. This reaction is part of the pathway that allows the usage of sialic acid as a carbohydrate source. Sialic acids are a family of related sugars that are found as a component of glycoproteins, gangliosides, and other sialoglycoconjugates. Pssm-ID: 240080 [Multi-domain] Cd Length: 219 Bit Score: 42.56 E-value: 8.45e-05
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| PRK01130 | PRK01130 | putative N-acetylmannosamine-6-phosphate 2-epimerase; |
170-212 | 2.42e-04 | |||||
putative N-acetylmannosamine-6-phosphate 2-epimerase; Pssm-ID: 234907 Cd Length: 221 Bit Score: 41.29 E-value: 2.42e-04
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| FCB2_FMN | cd02922 | Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ... |
112-206 | 4.79e-04 | |||||
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) is a respiratory enzyme located in the intermembrane space of fungal mitochondria which catalyzes the oxidation of L-lactate to pyruvate. FCB2 also participates in a short electron-transport chain involving cytochrome c and cytochrome oxidase which ultimately directs the reducing equivalents gained from L-lactate oxidation to oxygen, yielding one molecule of ATP for every L-lactate molecule consumed. FCB2 is composed of 2 domains: a C-terminal flavin-binding domain, which includes the active site for lacate oxidation, and an N-terminal b2-cytochrome domain, required for efficient cytochrome c reduction. FCB2 is a homotetramer and contains two noncovalently bound cofactors, FMN and heme per subunit. Pssm-ID: 239238 [Multi-domain] Cd Length: 344 Bit Score: 40.66 E-value: 4.79e-04
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| NPD_like | cd04730 | 2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
170-209 | 1.57e-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: 38.62 E-value: 1.57e-03
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| DHDPS-like | cd00408 | Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
127-208 | 1.59e-03 | |||||
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the class I aldolases, which use an active-site lysine which stabilizes a reaction intermediate via Schiff base formation, and have TIM beta/alpha barrel fold. The dihydrodipicolinate synthase family comprises several pyruvate-dependent class I aldolases that use the same catalytic step to catalyze different reactions in different pathways and includes such proteins as N-acetylneuraminate lyase, MosA protein, 5-keto-4-deoxy-glucarate dehydratase, trans-o-hydroxybenzylidenepyruvate hydratase-aldolase, trans-2'-carboxybenzalpyruvate hydratase-aldolase, and 2-keto-3-deoxy- gluconate aldolase. The family is also referred to as the N-acetylneuraminate lyase (NAL) family. Pssm-ID: 188630 [Multi-domain] Cd Length: 281 Bit Score: 39.07 E-value: 1.59e-03
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| HisA_HisF | cd04723 | Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ... |
18-210 | 2.49e-03 | |||||
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: 38.02 E-value: 2.49e-03
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| DUS_like_FMN | cd02801 | Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
139-214 | 2.69e-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: 37.86 E-value: 2.69e-03
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| YrpB | COG2070 | NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
170-209 | 2.73e-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: 38.17 E-value: 2.73e-03
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| His_biosynth | pfam00977 | Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
139-209 | 3.08e-03 | |||||
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: 37.84 E-value: 3.08e-03
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| LldD | COG1304 | FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
140-214 | 3.98e-03 | |||||
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase [Energy production and conversion, Lipid transport and metabolism, General function prediction only]; FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis Pssm-ID: 440915 [Multi-domain] Cd Length: 357 Bit Score: 37.80 E-value: 3.98e-03
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| OYE_like_FMN_family | cd02803 | Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
112-216 | 5.03e-03 | |||||
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. 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. Members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase. Pssm-ID: 239201 [Multi-domain] Cd Length: 327 Bit Score: 37.55 E-value: 5.03e-03
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| LMO_FMN | cd03332 | L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ... |
173-206 | 5.41e-03 | |||||
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that catalyzes the conversion of L-lactate and oxygen to acetate, carbon dioxide, and water. LMO is a member of the family of alpha-hydroxy acid oxidases. It is thought to be a homooctamer with two- and four- fold axes in the center of the octamer. Pssm-ID: 239448 [Multi-domain] Cd Length: 383 Bit Score: 37.65 E-value: 5.41e-03
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| PRK13585 | PRK13585 | 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ... |
170-212 | 8.88e-03 | |||||
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase; Pssm-ID: 184165 Cd Length: 241 Bit Score: 36.42 E-value: 8.88e-03
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| Blast search parameters | ||||
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