alpha-hydroxy-acid oxidizing protein [Clostridioides difficile]
Protein Classification
alpha-hydroxy-acid oxidizing protein( domain architecture ID 10120247)
FMN-dependent alpha-hydroxyacid oxidizing protein such as bacterial lactate dehydrogenase and eukaryotic 2-hydroxy-acid oxidase
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| alpha_hydroxyacid_oxid_FMN | cd02809 | Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
45-333 | 2.19e-94 | |||||
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: 282.41 E-value: 2.19e-94
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| Name | Accession | Description | Interval | E-value | ||||||
| alpha_hydroxyacid_oxid_FMN | cd02809 | Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
45-333 | 2.19e-94 | ||||||
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: 282.41 E-value: 2.19e-94
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| FMN_dh | pfam01070 | FMN-dependent dehydrogenase; |
47-337 | 4.51e-81 | ||||||
FMN-dependent dehydrogenase; Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 250.53 E-value: 4.51e-81
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| LldD | COG1304 | FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
47-337 | 1.92e-69 | ||||||
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: 220.77 E-value: 1.92e-69
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| lldD | PRK11197 | L-lactate dehydrogenase; Provisional |
48-333 | 6.23e-47 | ||||||
L-lactate dehydrogenase; Provisional Pssm-ID: 183033 Cd Length: 381 Bit Score: 162.89 E-value: 6.23e-47
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| Name | Accession | Description | Interval | E-value | ||||||
| alpha_hydroxyacid_oxid_FMN | cd02809 | Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
45-333 | 2.19e-94 | ||||||
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: 282.41 E-value: 2.19e-94
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| FMN_dh | pfam01070 | FMN-dependent dehydrogenase; |
47-337 | 4.51e-81 | ||||||
FMN-dependent dehydrogenase; Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 250.53 E-value: 4.51e-81
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| LldD | COG1304 | FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
47-337 | 1.92e-69 | ||||||
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: 220.77 E-value: 1.92e-69
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| FCB2_FMN | cd02922 | Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ... |
47-332 | 9.42e-54 | ||||||
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: 179.72 E-value: 9.42e-54
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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 ... |
47-333 | 3.14e-50 | ||||||
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: 170.70 E-value: 3.14e-50
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| LMO_FMN | cd03332 | L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ... |
45-332 | 4.39e-50 | ||||||
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: 171.31 E-value: 4.39e-50
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| lldD | PRK11197 | L-lactate dehydrogenase; Provisional |
48-333 | 6.23e-47 | ||||||
L-lactate dehydrogenase; Provisional Pssm-ID: 183033 Cd Length: 381 Bit Score: 162.89 E-value: 6.23e-47
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| PLN02535 | PLN02535 | glycolate oxidase |
189-331 | 5.36e-42 | ||||||
glycolate oxidase Pssm-ID: 215294 Cd Length: 364 Bit Score: 149.60 E-value: 5.36e-42
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| PLN02493 | PLN02493 | probable peroxisomal (S)-2-hydroxy-acid oxidase |
47-331 | 1.97e-39 | ||||||
probable peroxisomal (S)-2-hydroxy-acid oxidase Pssm-ID: 166134 [Multi-domain] Cd Length: 367 Bit Score: 142.95 E-value: 1.97e-39
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| PLN02979 | PLN02979 | glycolate oxidase |
60-331 | 7.71e-36 | ||||||
glycolate oxidase Pssm-ID: 166620 Cd Length: 366 Bit Score: 133.31 E-value: 7.71e-36
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| MDH_FMN | cd04736 | Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ... |
48-332 | 3.71e-25 | ||||||
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of homologous FMN-dependent a-hydroxy acid oxidizing enzymes that oxidizes (S)-mandelate to phenylglyoxalate. MDH is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate. 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: 240087 Cd Length: 361 Bit Score: 104.14 E-value: 3.71e-25
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| IDI-2_FMN | cd02811 | Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ... |
60-330 | 2.42e-18 | ||||||
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. Two types of IDIs have been characterized at present. The long known IDI-1 is only dependent on divalent metals for activity, whereas IDI-2 requires a metal, FMN and NADPH. IDI-2 catalyzes the interconversion of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) in the mevalonate pathway. Pssm-ID: 239205 [Multi-domain] Cd Length: 326 Bit Score: 84.09 E-value: 2.42e-18
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| TIM_phosphate_binding | cd04722 | TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
190-291 | 5.01e-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: 58.37 E-value: 5.01e-10
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| NPD_like | cd04730 | 2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
216-296 | 3.12e-09 | ||||||
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: 56.72 E-value: 3.12e-09
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| YrpB | COG2070 | NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
216-296 | 1.29e-08 | ||||||
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only]; Pssm-ID: 441673 [Multi-domain] Cd Length: 302 Bit Score: 55.50 E-value: 1.29e-08
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| GltS_FMN | cd02808 | Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
258-293 | 1.60e-06 | ||||||
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that catalyzes the reductive synthesis of L-glutamate from 2-oxoglutarate and L-glutamine via intramolecular channelling of ammonia, a reaction in the plant, yeast and bacterial pathway for ammonia assimilation. It is a multifunctional enzyme that functions through three distinct active centers, carrying out L-glutamine hydrolysis, conversion of 2-oxoglutarate into L-glutamate, and electron uptake from an electron donor. Pssm-ID: 239202 [Multi-domain] Cd Length: 392 Bit Score: 49.46 E-value: 1.60e-06
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| IMPDH | cd00381 | IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
165-293 | 1.88e-06 | ||||||
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: 49.05 E-value: 1.88e-06
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| NMO | pfam03060 | Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ... |
190-297 | 3.68e-06 | ||||||
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: 47.89 E-value: 3.68e-06
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| Glu_synthase | pfam01645 | Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
220-292 | 1.11e-05 | ||||||
Conserved region in glutamate synthase; This family represents a region of the glutamate synthase protein. This region is expressed as a separate subunit in the glutamate synthase alpha subunit from archaebacteria, or part of a large multidomain enzyme in other organizms. The aligned region of these proteins contains a putative FMN binding site and Fe-S cluster. Pssm-ID: 396287 [Multi-domain] Cd Length: 367 Bit Score: 46.56 E-value: 1.11e-05
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| PyrD | COG0167 | Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
191-287 | 8.07e-05 | ||||||
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: 43.91 E-value: 8.07e-05
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| DusA | COG0042 | tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
192-291 | 8.48e-05 | ||||||
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: 43.54 E-value: 8.48e-05
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| GltB2 | COG0069 | Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ... |
258-293 | 1.58e-04 | ||||||
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 is part of the Pathway/BioSystem: Glutamine biosynthesis Pssm-ID: 439839 Cd Length: 728 Bit Score: 43.31 E-value: 1.58e-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 ... |
156-294 | 3.13e-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: 42.17 E-value: 3.13e-04
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| Aldolase_Class_I | cd00945 | Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ... |
158-290 | 4.66e-04 | ||||||
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which stabilizes a reaction intermediates via Schiff base formation, and have TIM beta/alpha barrel fold. The members of this family include 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-4-hydroxyglutarate (KHG) aldolases, transaldolase, dihydrodipicolinate synthase sub-family, Type I 3-dehydroquinate dehydratase, DeoC and DhnA proteins, and metal-independent fructose-1,6-bisphosphate aldolase. Although structurally similar, the class II aldolases use a different mechanism and are believed to have an independent evolutionary origin. Pssm-ID: 188634 [Multi-domain] Cd Length: 201 Bit Score: 40.77 E-value: 4.66e-04
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| DUS_like_FMN | cd02801 | Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
198-291 | 5.14e-04 | ||||||
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: 40.94 E-value: 5.14e-04
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| PRK06843 | PRK06843 | inosine 5-monophosphate dehydrogenase; Validated |
198-296 | 5.91e-04 | ||||||
inosine 5-monophosphate dehydrogenase; Validated Pssm-ID: 180725 [Multi-domain] Cd Length: 404 Bit Score: 41.56 E-value: 5.91e-04
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| PTZ00314 | PTZ00314 | inosine-5'-monophosphate dehydrogenase; Provisional |
261-291 | 4.64e-03 | ||||||
inosine-5'-monophosphate dehydrogenase; Provisional Pssm-ID: 240355 [Multi-domain] Cd Length: 495 Bit Score: 38.80 E-value: 4.64e-03
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| PRK04302 | PRK04302 | triosephosphate isomerase; Provisional |
253-297 | 5.42e-03 | ||||||
triosephosphate isomerase; Provisional Pssm-ID: 235274 Cd Length: 223 Bit Score: 37.54 E-value: 5.42e-03
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| gltB | PRK11750 | glutamate synthase subunit alpha; Provisional |
255-301 | 6.18e-03 | ||||||
glutamate synthase subunit alpha; Provisional Pssm-ID: 236968 [Multi-domain] Cd Length: 1485 Bit Score: 38.70 E-value: 6.18e-03
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| IGPS | cd00331 | Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ... |
216-296 | 7.03e-03 | ||||||
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, catalyzing the ring closure reaction of 1-(o-carboxyphenylamino)-1-deoxyribulose-5-phosphate (CdRP) to indole-3-glycerol phosphate (IGP), accompanied by the release of carbon dioxide and water. IGPS is active as a separate monomer in most organisms, but is also found fused to other enzymes as part of a bifunctional or multifunctional enzyme involved in tryptophan biosynthesis. Pssm-ID: 238203 Cd Length: 217 Bit Score: 37.44 E-value: 7.03e-03
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| IMPDH | pfam00478 | IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
262-291 | 7.18e-03 | ||||||
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family. Pssm-ID: 459826 [Multi-domain] Cd Length: 463 Bit Score: 38.14 E-value: 7.18e-03
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| DHOD_1B_like | cd04740 | Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
198-333 | 8.37e-03 | ||||||
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: 37.53 E-value: 8.37e-03
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