tRNA dihydrouridine synthase DusB [Flavonifractor sp. An82]
Protein Classification
tRNA dihydrouridine synthase( domain architecture ID 11414563)
tRNA dihydrouridine synthase catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| DusA | COG0042 | tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
4-314 | 1.92e-159 | |||||
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: 447.62 E-value: 1.92e-159
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| Name | Accession | Description | Interval | E-value | |||||
| DusA | COG0042 | tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
4-314 | 1.92e-159 | |||||
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: 447.62 E-value: 1.92e-159
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| nifR3_yhdG | TIGR00737 | putative TIM-barrel protein, nifR3 family; This model represents one branch of COG0042 ... |
3-314 | 3.25e-135 | |||||
putative TIM-barrel protein, nifR3 family; This model represents one branch of COG0042 (Predicted TIM-barrel enzymes, possibly dehydrogenases, nifR3 family). This branch includes NifR3 itself, from Rhodobacter capsulatus. It excludes a broadly distributed but more sparsely populated subfamily that contains sll0926 from Synechocystis PCC6803, HI0634 from Haemophilus influenzae, and BB0225 from Borrelia burgdorferi. It also excludes a shorter and more distant archaeal subfamily.The function of nifR3, a member of this family, is unknown, but it is found in an operon with nitrogen-sensing two component regulators in Rhodobacter capsulatus.Members of this family show a distant relationship to alpha/beta (TIM) barrel enzymes such as dihydroorotate dehydrogenase and glycolate oxidase. [Unknown function, General] Pssm-ID: 129820 Cd Length: 319 Bit Score: 386.72 E-value: 3.25e-135
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| Dus | pfam01207 | Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
14-310 | 1.12e-114 | |||||
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: 334.29 E-value: 1.12e-114
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| DUS_like_FMN | cd02801 | Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
12-243 | 4.84e-114 | |||||
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: 329.46 E-value: 4.84e-114
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| PRK10415 | PRK10415 | tRNA-dihydrouridine synthase B; Provisional |
1-290 | 1.58e-82 | |||||
tRNA-dihydrouridine synthase B; Provisional Pssm-ID: 182440 Cd Length: 321 Bit Score: 252.97 E-value: 1.58e-82
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| Name | Accession | Description | Interval | E-value | |||||
| DusA | COG0042 | tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
4-314 | 1.92e-159 | |||||
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: 447.62 E-value: 1.92e-159
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| nifR3_yhdG | TIGR00737 | putative TIM-barrel protein, nifR3 family; This model represents one branch of COG0042 ... |
3-314 | 3.25e-135 | |||||
putative TIM-barrel protein, nifR3 family; This model represents one branch of COG0042 (Predicted TIM-barrel enzymes, possibly dehydrogenases, nifR3 family). This branch includes NifR3 itself, from Rhodobacter capsulatus. It excludes a broadly distributed but more sparsely populated subfamily that contains sll0926 from Synechocystis PCC6803, HI0634 from Haemophilus influenzae, and BB0225 from Borrelia burgdorferi. It also excludes a shorter and more distant archaeal subfamily.The function of nifR3, a member of this family, is unknown, but it is found in an operon with nitrogen-sensing two component regulators in Rhodobacter capsulatus.Members of this family show a distant relationship to alpha/beta (TIM) barrel enzymes such as dihydroorotate dehydrogenase and glycolate oxidase. [Unknown function, General] Pssm-ID: 129820 Cd Length: 319 Bit Score: 386.72 E-value: 3.25e-135
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| Dus | pfam01207 | Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
14-310 | 1.12e-114 | |||||
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: 334.29 E-value: 1.12e-114
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| DUS_like_FMN | cd02801 | Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
12-243 | 4.84e-114 | |||||
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: 329.46 E-value: 4.84e-114
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| PRK10415 | PRK10415 | tRNA-dihydrouridine synthase B; Provisional |
1-290 | 1.58e-82 | |||||
tRNA-dihydrouridine synthase B; Provisional Pssm-ID: 182440 Cd Length: 321 Bit Score: 252.97 E-value: 1.58e-82
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| PRK10550 | PRK10550 | tRNA dihydrouridine(16) synthase DusC; |
70-235 | 9.14e-35 | |||||
tRNA dihydrouridine(16) synthase DusC; Pssm-ID: 236713 Cd Length: 312 Bit Score: 128.77 E-value: 9.14e-35
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| PRK11815 | PRK11815 | tRNA dihydrouridine(20/20a) synthase DusA; |
1-251 | 2.00e-26 | |||||
tRNA dihydrouridine(20/20a) synthase DusA; Pssm-ID: 236991 [Multi-domain] Cd Length: 333 Bit Score: 106.76 E-value: 2.00e-26
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| FadH | COG1902 | 2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ... |
121-250 | 4.67e-13 | |||||
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: 69.04 E-value: 4.67e-13
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| arch_FMN | cd02911 | Archeal FMN-binding domain. This family of archaeal proteins are part of the NAD(P)H-dependent ... |
12-238 | 6.85e-12 | |||||
Archeal FMN-binding domain. This family of archaeal proteins are part of the NAD(P)H-dependent flavin oxidoreductase (oxidored) FMN-binding 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. The specific function of this group is unknown. Pssm-ID: 239237 [Multi-domain] Cd Length: 233 Bit Score: 64.27 E-value: 6.85e-12
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| OYE_like_FMN_family | cd02803 | Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
153-241 | 1.06e-11 | |||||
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: 64.90 E-value: 1.06e-11
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| TIM_phosphate_binding | cd04722 | TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
13-227 | 1.77e-10 | |||||
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: 59.52 E-value: 1.77e-10
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| DHOD_1B_like | cd04740 | Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
55-238 | 2.15e-09 | |||||
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively. Pssm-ID: 240091 [Multi-domain] Cd Length: 296 Bit Score: 57.56 E-value: 2.15e-09
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| OYE_YqiM_FMN | cd02932 | Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress ... |
121-241 | 6.06e-08 | |||||
Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress response of Bacillus subtilis. Like the other OYE members, each monomer of YqjM contains FMN as a non-covalently bound cofactor and uses NADPH as a reducing agent. The YqjM enzyme exists as a homotetramer that is assembled as a dimer of catalytically dependent dimers, while other OYE members exist only as monomers or dimers. Moreover, the protein displays a shared active site architecture where an arginine finger at the COOH terminus of one monomer extends into the active site of the adjacent monomer and is directly involved in substrate recognition. Another remarkable difference in the binding of the ligand in YqjM is represented by the contribution of the NH2-terminal tyrosine instead of a COOH-terminal tyrosine in OYE and its homologs. Pssm-ID: 239242 [Multi-domain] Cd Length: 336 Bit Score: 53.27 E-value: 6.06e-08
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| PyrD | COG0167 | Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
57-244 | 8.57e-08 | |||||
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate dehydrogenase is part of the Pathway/BioSystem: Pyrimidine biosynthesis Pssm-ID: 439937 [Multi-domain] Cd Length: 296 Bit Score: 52.77 E-value: 8.57e-08
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| DHOD_DHPD_FMN | cd02810 | Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
86-241 | 6.37e-07 | |||||
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively. DHPD catalyzes the first step in pyrimidine degradation: the NADPH-dependent reduction of uracil and thymine to the corresponding 5,6-dihydropyrimidines. DHPD contains two FAD, two FMN and eight [4Fe-4S] clusters, arranged in two electron transfer chains that pass its homodimeric interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue. Pssm-ID: 239204 [Multi-domain] Cd Length: 289 Bit Score: 50.05 E-value: 6.37e-07
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| HisA | cd04732 | HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
112-227 | 1.20e-06 | |||||
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: 48.63 E-value: 1.20e-06
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| PRK07259 | PRK07259 | dihydroorotate dehydrogenase; |
57-233 | 5.95e-06 | |||||
dihydroorotate dehydrogenase; Pssm-ID: 235982 Cd Length: 301 Bit Score: 47.07 E-value: 5.95e-06
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| PRK07565 | PRK07565 | dihydroorotate dehydrogenase-like protein; |
149-201 | 8.76e-06 | |||||
dihydroorotate dehydrogenase-like protein; Pssm-ID: 236051 Cd Length: 334 Bit Score: 46.78 E-value: 8.76e-06
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| PRK00748 | PRK00748 | 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
112-205 | 2.18e-05 | |||||
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated Pssm-ID: 179108 Cd Length: 233 Bit Score: 45.06 E-value: 2.18e-05
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| DHOD_like | cd04739 | Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ... |
149-201 | 2.41e-05 | |||||
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively. This subgroup has the conserved FMN binding site, but lacks some catalytic residues and may therefore be inactive. Pssm-ID: 240090 Cd Length: 325 Bit Score: 45.30 E-value: 2.41e-05
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| DCR_FMN | cd02930 | 2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur ... |
121-248 | 9.33e-05 | |||||
2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur flavoenzyme which contains FMN, FAD, and a 4Fe-4S cluster. It is also a monomer, unlike that of its eukaryotic counterparts which form homotetramers and lack the flavin and iron-sulfur cofactors. Metabolism of unsaturated fatty acids requires auxiliary enzymes in addition to those used in b-oxidation. After a given number of cycles through the b-oxidation pathway, those unsaturated fatty acyl-CoAs with double bonds at even-numbered carbon positions contain 2-trans, 4-cis double bonds that can not be modified by enoyl-CoA hydratase. DCR utilizes NADPH to remove the C4-C5 double bond. DCR can catalyze the reduction of both natural fatty acids with cis double bonds, as well as substrates containing trans double bonds. The reaction is initiated by hybrid transfer from NADPH to FAD, which in turn transfers electrons, one at a time, to FMN via the 4Fe-4S cluster. The fully reduced FMN provides a hydrid ion to the C5 atom of substrate, and Tyr and His are proposed to form a catalytic dyad that protonates the C4 atom of the substrate and completes the reaction. Pssm-ID: 239240 [Multi-domain] Cd Length: 353 Bit Score: 43.81 E-value: 9.33e-05
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| OYE_like_4_FMN | cd04735 | Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ... |
167-233 | 6.92e-04 | |||||
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: 41.04 E-value: 6.92e-04
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| PRK08318 | PRK08318 | NAD-dependent dihydropyrimidine dehydrogenase subunit PreA; |
87-169 | 1.37e-03 | |||||
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA; Pssm-ID: 236237 [Multi-domain] Cd Length: 420 Bit Score: 40.31 E-value: 1.37e-03
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| HisF | cd04731 | The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ... |
90-226 | 2.65e-03 | |||||
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: 38.60 E-value: 2.65e-03
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| IGPS | pfam00218 | Indole-3-glycerol phosphate synthase; |
148-200 | 3.41e-03 | |||||
Indole-3-glycerol phosphate synthase; Pssm-ID: 395163 Cd Length: 252 Bit Score: 38.43 E-value: 3.41e-03
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| YrpB | COG2070 | NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
149-226 | 3.63e-03 | |||||
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only]; Pssm-ID: 441673 [Multi-domain] Cd Length: 302 Bit Score: 38.55 E-value: 3.63e-03
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| NPD_like | cd04730 | 2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
154-226 | 3.81e-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: 38.23 E-value: 3.81e-03
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| DHPD_FMN | cd02940 | Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
87-221 | 3.82e-03 | |||||
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in pyrimidine degradation: the NADPH-dependent reduction of uracil and thymine to the corresponding 5,6-dihydropyrimidines. DHPD contains two FAD, two FMN, and eight [4Fe-4S] clusters, arranged in two electron transfer chains that pass the dimer interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue. Pssm-ID: 239244 Cd Length: 299 Bit Score: 38.42 E-value: 3.82e-03
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| HisF | COG0107 | Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ... |
188-221 | 6.50e-03 | |||||
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: 37.70 E-value: 6.50e-03
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| LOX_like_FMN | cd04737 | L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ... |
87-227 | 9.56e-03 | |||||
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing alpha-hydroxyacid oxidases and catalyzes the oxidation of l-lactate using molecular oxygen to generate pyruvate and H2O2. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO). Pssm-ID: 240088 [Multi-domain] Cd Length: 351 Bit Score: 37.42 E-value: 9.56e-03
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