2-nitropropane dioxygenase [Bacteroidetes bacterium RIFOXYC2_FULL_40_12]
Protein Classification
NAD(P)H-dependent flavin oxidoreductase( domain architecture ID 11449685)
NAD(P)H-dependent flavin oxidoreductase similar to nitronate monooxygenase, an FMN-dependent enzyme that uses molecular oxygen to oxidize (anionic) alkyl nitronates and nitroalkanes to the corresponding carbonyl compounds and nitrite
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| YrpB | COG2070 | NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
12-311 | 5.58e-121 | |||||
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only]; : Pssm-ID: 441673 [Multi-domain] Cd Length: 302 Bit Score: 349.41 E-value: 5.58e-121
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| Name | Accession | Description | Interval | E-value | ||||||
| YrpB | COG2070 | NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
12-311 | 5.58e-121 | ||||||
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only]; Pssm-ID: 441673 [Multi-domain] Cd Length: 302 Bit Score: 349.41 E-value: 5.58e-121
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| enACPred_II | TIGR03151 | putative enoyl-[acyl-carrier-protein] reductase II; This oxidoreductase of the 2-nitropropane ... |
5-313 | 1.13e-97 | ||||||
putative enoyl-[acyl-carrier-protein] reductase II; This oxidoreductase of the 2-nitropropane dioxygenase family (pfam03060) is commonly found in apparent operons with genes involved in fatty acid biosynthesis. Furthermore, this genomic context generally includes the fabG 3-oxoacyl-[ACP] reductase and lacks the fabI enoyl-[ACP] reductase. Pssm-ID: 132195 Cd Length: 307 Bit Score: 290.50 E-value: 1.13e-97
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| NPD_like | cd04730 | 2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
14-223 | 6.18e-88 | ||||||
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: 263.19 E-value: 6.18e-88
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| NMO | pfam03060 | Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ... |
7-305 | 2.26e-59 | ||||||
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane dioxygenase (NPD) (EC:1.13.11.32), is an FMN-dependent enzyme that uses molecular oxygen to oxidize (anionic) alkyl nitronates and, in the case of the enzyme from Neurospora crassa, (neutral) nitroalkanes to the corresponding carbonyl compounds and nitrite. Previously classified as 2-nitropropane dioxygenase, but it is now recognized that this was the result of the slow ionization of nitroalkanes to their nitronate (anionic) forms. The enzymes from the fungus Neurospora crassa and the yeast Williopsis saturnus var. mrakii (formerly classified as Hansenula mrakii) contain non-covalently bound FMN as the cofactor. Active towards linear alkyl nitronates of lengths between 2 and 6 carbon atoms and, with lower activity, towards propyl-2-nitronate. The enzyme from N. crassa can also utilize neutral nitroalkanes, but with lower activity. One atom of oxygen is incorporated into the carbonyl group of the aldehyde product. The reaction appears to involve the formation of an enzyme-bound nitronate radical and an a-peroxynitroethane species, which then decomposes, either in the active site of the enzyme or after release, to acetaldehyde and nitrite. Pssm-ID: 367316 [Multi-domain] Cd Length: 331 Bit Score: 193.11 E-value: 2.26e-59
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| lldD | PRK11197 | L-lactate dehydrogenase; Provisional |
135-200 | 5.98e-04 | ||||||
L-lactate dehydrogenase; Provisional Pssm-ID: 183033 Cd Length: 381 Bit Score: 41.16 E-value: 5.98e-04
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| Name | Accession | Description | Interval | E-value | ||||||
| YrpB | COG2070 | NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
12-311 | 5.58e-121 | ||||||
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only]; Pssm-ID: 441673 [Multi-domain] Cd Length: 302 Bit Score: 349.41 E-value: 5.58e-121
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| enACPred_II | TIGR03151 | putative enoyl-[acyl-carrier-protein] reductase II; This oxidoreductase of the 2-nitropropane ... |
5-313 | 1.13e-97 | ||||||
putative enoyl-[acyl-carrier-protein] reductase II; This oxidoreductase of the 2-nitropropane dioxygenase family (pfam03060) is commonly found in apparent operons with genes involved in fatty acid biosynthesis. Furthermore, this genomic context generally includes the fabG 3-oxoacyl-[ACP] reductase and lacks the fabI enoyl-[ACP] reductase. Pssm-ID: 132195 Cd Length: 307 Bit Score: 290.50 E-value: 1.13e-97
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| NPD_like | cd04730 | 2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
14-223 | 6.18e-88 | ||||||
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: 263.19 E-value: 6.18e-88
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| NMO | pfam03060 | Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ... |
7-305 | 2.26e-59 | ||||||
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane dioxygenase (NPD) (EC:1.13.11.32), is an FMN-dependent enzyme that uses molecular oxygen to oxidize (anionic) alkyl nitronates and, in the case of the enzyme from Neurospora crassa, (neutral) nitroalkanes to the corresponding carbonyl compounds and nitrite. Previously classified as 2-nitropropane dioxygenase, but it is now recognized that this was the result of the slow ionization of nitroalkanes to their nitronate (anionic) forms. The enzymes from the fungus Neurospora crassa and the yeast Williopsis saturnus var. mrakii (formerly classified as Hansenula mrakii) contain non-covalently bound FMN as the cofactor. Active towards linear alkyl nitronates of lengths between 2 and 6 carbon atoms and, with lower activity, towards propyl-2-nitronate. The enzyme from N. crassa can also utilize neutral nitroalkanes, but with lower activity. One atom of oxygen is incorporated into the carbonyl group of the aldehyde product. The reaction appears to involve the formation of an enzyme-bound nitronate radical and an a-peroxynitroethane species, which then decomposes, either in the active site of the enzyme or after release, to acetaldehyde and nitrite. Pssm-ID: 367316 [Multi-domain] Cd Length: 331 Bit Score: 193.11 E-value: 2.26e-59
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| NPD_PKS | cd04743 | 2-Nitropropane dioxygenase (NPD)-like domain, associated with polyketide synthases (PKS). NPD ... |
15-270 | 1.12e-07 | ||||||
2-Nitropropane dioxygenase (NPD)-like domain, associated with polyketide synthases (PKS). NPD is part of the nitroalkaneoxidizing enzyme family, that catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDPs are members 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: 240094 Cd Length: 320 Bit Score: 52.51 E-value: 1.12e-07
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| TIM_phosphate_binding | cd04722 | TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
112-197 | 3.24e-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: 49.89 E-value: 3.24e-07
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| NPD_FabD | cd04742 | 2-Nitropropane dioxygenase (NPD)-like domain, associated with the (acyl-carrier-protein) ... |
135-219 | 1.94e-06 | ||||||
2-Nitropropane dioxygenase (NPD)-like domain, associated with the (acyl-carrier-protein) S-malonyltransferase FabD. NPD is part of the nitroalkaneoxidizing enzyme family, that catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDPs are members 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: 240093 Cd Length: 418 Bit Score: 48.79 E-value: 1.94e-06
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| LldD | COG1304 | FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
126-196 | 5.09e-06 | ||||||
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: 47.43 E-value: 5.09e-06
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| PyrD | COG0167 | Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
49-197 | 1.17e-04 | ||||||
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: 43.14 E-value: 1.17e-04
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| FadH | COG1902 | 2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ... |
107-190 | 1.93e-04 | ||||||
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: 42.46 E-value: 1.93e-04
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| NanE | cd04729 | N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
151-197 | 2.40e-04 | ||||||
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: 41.79 E-value: 2.40e-04
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| DHOD_1B_like | cd04740 | Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
159-197 | 2.62e-04 | ||||||
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: 42.15 E-value: 2.62e-04
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| lldD | PRK11197 | L-lactate dehydrogenase; Provisional |
135-200 | 5.98e-04 | ||||||
L-lactate dehydrogenase; Provisional Pssm-ID: 183033 Cd Length: 381 Bit Score: 41.16 E-value: 5.98e-04
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| His_biosynth | pfam00977 | Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
158-199 | 7.27e-04 | ||||||
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: 40.15 E-value: 7.27e-04
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| OYE_like_FMN_family | cd02803 | Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
107-196 | 7.50e-04 | ||||||
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: 40.63 E-value: 7.50e-04
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| alpha_hydroxyacid_oxid_FMN | cd02809 | Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
126-196 | 1.26e-03 | ||||||
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. 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). In green plants, glycolate oxidase is one of the key enzymes in photorespiration where it oxidizes glycolate to glyoxylate. LMO catalyzes the oxidation of L-lactate to acetate and carbon dioxide. MDH oxidizes (S)-mandelate to phenylglyoxalate. It is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate. Pssm-ID: 239203 [Multi-domain] Cd Length: 299 Bit Score: 39.74 E-value: 1.26e-03
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| PLN02274 | PLN02274 | inosine-5'-monophosphate dehydrogenase |
149-205 | 2.01e-03 | ||||||
inosine-5'-monophosphate dehydrogenase Pssm-ID: 215154 [Multi-domain] Cd Length: 505 Bit Score: 39.65 E-value: 2.01e-03
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| PRK07259 | PRK07259 | dihydroorotate dehydrogenase; |
159-197 | 2.10e-03 | ||||||
dihydroorotate dehydrogenase; Pssm-ID: 235982 Cd Length: 301 Bit Score: 39.36 E-value: 2.10e-03
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| GuaB | COG0516 | IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ... |
112-232 | 3.49e-03 | ||||||
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP reductase is part of the Pathway/BioSystem: Purine biosynthesis Pssm-ID: 440282 [Multi-domain] Cd Length: 326 Bit Score: 38.65 E-value: 3.49e-03
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| His_biosynth | pfam00977 | Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
145-218 | 5.94e-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: 37.46 E-value: 5.94e-03
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| DHOD_DHPD_FMN | cd02810 | Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
51-197 | 6.60e-03 | ||||||
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: 37.72 E-value: 6.60e-03
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| IMPDH | cd00381 | IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
149-205 | 6.61e-03 | ||||||
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the NAD-dependent oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5' monophosphate (XMP). It is a rate-limiting step in the de novo synthesis of the guanine nucleotides. There is often a CBS domain inserted in the middle of this domain, which is proposed to play a regulatory role. IMPDH is a key enzyme in the regulation of cell proliferation and differentiation. It has been identified as an attractive target for developing chemotherapeutic agents. Pssm-ID: 238223 [Multi-domain] Cd Length: 325 Bit Score: 37.88 E-value: 6.61e-03
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| HisF | cd04731 | The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ... |
158-199 | 7.84e-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: 37.06 E-value: 7.84e-03
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| PRK05286 | PRK05286 | quinone-dependent dihydroorotate dehydrogenase; |
130-195 | 8.01e-03 | ||||||
quinone-dependent dihydroorotate dehydrogenase; Pssm-ID: 235388 Cd Length: 344 Bit Score: 37.45 E-value: 8.01e-03
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