Protein : Qrob_P0428470.2 Q. robur
Protein Identifier  ? Qrob_P0428470.2 Organism . Name  Quercus robur
Score  56.0 Score Type  egn
Protein Description  (M=27) 1.3.3.8 - Tetrahydroberberine oxidase. Code Enzyme  EC:1.3.3.8
Gene Prediction Quality  validated Protein length 

Sequence

Length: 241  
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0 Synonyms

6 GO Terms

Identifier Name Description
GO:0016491 oxidoreductase activity Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
GO:0055114 oxidation-reduction process A metabolic process that results in the removal or addition of one or more electrons to or from a substance, with or without the concomitant removal or addition of a proton or protons.
GO:0003824 catalytic activity Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
GO:0050660 flavin adenine dinucleotide binding Interacting selectively and non-covalently with FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
GO:0008762 UDP-N-acetylmuramate dehydrogenase activity Catalysis of the reaction: UDP-N-acetylmuramate + NADP+ = UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + NADPH + H+.
GO:0016614 oxidoreductase activity, acting on CH-OH group of donors Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group act as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.

30 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|rcu:RCOM_1335960 27 211 + 185 Gaps:78 50.10 525 47.15 2e-63 Reticuline oxidase precursor putative (EC:1.21.3.3)
blastp_kegg lcl|pop:POPTR_0011s16440g 21 211 + 191 Gaps:77 51.64 519 47.01 7e-60 FAD-binding domain-containing family protein
blastp_kegg lcl|cic:CICLE_v10018216mg 27 209 + 183 Gaps:78 49.25 530 48.28 1e-59 hypothetical protein
blastp_kegg lcl|vvi:100264684 27 209 + 183 Gaps:36 43.89 499 47.95 1e-58 reticuline oxidase-like protein-like
blastp_kegg lcl|cit:102618094 27 209 + 183 Gaps:78 49.53 527 48.66 2e-57 tetrahydrocannabinolic acid synthase-like
blastp_kegg lcl|vvi:100266314 29 210 + 182 Gaps:78 33.33 780 45.77 2e-57 reticuline oxidase-like protein-like
blastp_kegg lcl|pvu:PHAVU_005G004600g 56 240 + 185 Gaps:60 47.67 514 45.31 3e-56 hypothetical protein
blastp_kegg lcl|tcc:TCM_027080 72 210 + 139 Gaps:19 28.06 563 63.92 5e-56 FAD-binding Berberine family protein putative
blastp_kegg lcl|cit:102618663 72 222 + 151 Gaps:23 31.03 535 56.63 1e-55 reticuline oxidase-like protein-like
blastp_kegg lcl|cic:CICLE_v10014829mg 72 213 + 142 Gaps:19 29.70 542 56.52 3e-55 hypothetical protein
blastp_pdb 3fw7_A 72 208 + 137 Gaps:20 31.53 498 50.32 2e-35 mol:protein length:498 Reticuline oxidase
blastp_pdb 3fw9_A 72 208 + 137 Gaps:20 31.72 495 50.32 2e-35 mol:protein length:495 Reticuline oxidase
blastp_pdb 3d2j_A 72 208 + 137 Gaps:20 29.18 538 50.32 2e-35 mol:protein length:538 berberine bridge-forming enzyme
blastp_pdb 3d2h_A 72 208 + 137 Gaps:20 29.18 538 50.32 2e-35 mol:protein length:538 berberine bridge-forming enzyme
blastp_pdb 3d2d_A 72 208 + 137 Gaps:20 29.18 538 50.32 2e-35 mol:protein length:538 berberine bridge-forming enzyme
blastp_pdb 3gsy_A 72 208 + 137 Gaps:20 30.25 519 50.32 3e-35 mol:protein length:519 Reticuline oxidase Berberine bridge-forming
blastp_pdb 3fw8_A 72 208 + 137 Gaps:20 31.72 495 49.68 3e-34 mol:protein length:495 Reticuline oxidase
blastp_pdb 3fwa_A 72 208 + 137 Gaps:20 31.59 497 49.68 4e-34 mol:protein length:497 Reticuline oxidase
blastp_pdb 2bvh_D 26 180 + 155 Gaps:37 35.73 459 31.71 3e-06 mol:protein length:459 6-HYDROXY-D-NICOTINE OXIDASE
blastp_pdb 2bvh_C 26 180 + 155 Gaps:37 35.73 459 31.71 3e-06 mol:protein length:459 6-HYDROXY-D-NICOTINE OXIDASE
blastp_uniprot_sprot sp|P30986|RETO_ESCCA 72 208 + 137 Gaps:20 29.18 538 50.32 1e-34 Reticuline oxidase OS Eschscholzia californica GN BBE1 PE 1 SV 1
blastp_uniprot_sprot sp|P93479|RETO_PAPSO 72 208 + 137 Gaps:20 29.35 535 48.41 2e-33 Reticuline oxidase OS Papaver somniferum GN BBE1 PE 3 SV 1
blastp_uniprot_sprot sp|Q33DQ2|THCAI_CANSA 74 213 + 140 Gaps:20 29.36 545 43.12 5e-33 Inactive tetrahydrocannabinolic acid synthase OS Cannabis sativa PE 3 SV 1
blastp_uniprot_sprot sp|Q8GTB6|THCAS_CANSA 74 213 + 140 Gaps:20 29.36 545 43.75 5e-33 Tetrahydrocannabinolic acid synthase OS Cannabis sativa PE 1 SV 1
blastp_uniprot_sprot sp|A6P6V9|CBDAS_CANSA 72 205 + 134 Gaps:19 28.12 544 41.83 9e-32 Cannabidiolic acid synthase OS Cannabis sativa GN CBDAS PE 1 SV 1
blastp_uniprot_sprot sp|A6P6W1|CASL2_CANSA 74 205 + 132 Gaps:20 27.89 545 43.42 3e-31 Cannabidiolic acid synthase-like 2 OS Cannabis sativa GN CBDAS3 PE 2 SV 1
blastp_uniprot_sprot sp|A6P6W0|CASL1_CANSA 74 205 + 132 Gaps:20 27.89 545 43.42 4e-31 Cannabidiolic acid synthase-like 1 OS Cannabis sativa GN CBDAS2 PE 2 SV 1
blastp_uniprot_sprot sp|Q9SVG4|RETOL_ARATH 72 210 + 139 Gaps:19 27.72 570 43.04 1e-27 Reticuline oxidase-like protein OS Arabidopsis thaliana GN At4g20830 PE 1 SV 2
rpsblast_cdd gnl|CDD|30625 71 189 + 119 Gaps:19 27.89 459 32.03 2e-09 COG0277 GlcD FAD/FMN-containing dehydrogenases [Energy production and conversion].
rpsblast_cdd gnl|CDD|201863 74 148 + 75 Gaps:4 56.83 139 35.44 4e-09 pfam01565 FAD_binding_4 FAD binding domain. This family consists of various enzymes that use FAD as a co-factor most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure the alignment includes the FAD binding site called the PP-loop between residues 99-110. The FAD molecule is covalently bound in the known structure however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor mitomycin radical oxidase this enzyme oxidises the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.

10 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
Gene3D 74 182 109 G3DSA:3.30.465.10 none none IPR016169
Phobius 1 2 2 SIGNAL_PEPTIDE_N_REGION none N-terminal region of a signal peptide. none
Pfam 74 149 76 PF01565 "KEGG:00520+1.3.1.98","KEGG:00550+1.3.1.98","MetaCyc:PWY-6386","MetaCyc:PWY-6387","UniPathway:UPA00219" FAD binding domain IPR006094
Phobius 3 13 11 SIGNAL_PEPTIDE_H_REGION none Hydrophobic region of a signal peptide. none
SUPERFAMILY 72 182 111 SSF56176 none none IPR016166
Phobius 19 240 222 NON_CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. none
ProSiteProfiles 74 183 110 PS51387 none PCMH-type FAD-binding domain profile. IPR016166
PANTHER 73 210 138 PTHR32448 none none none
Phobius 1 18 18 SIGNAL_PEPTIDE none Signal peptide region none
Phobius 14 18 5 SIGNAL_PEPTIDE_C_REGION none C-terminal region of a signal peptide. none

3 Localization

Analysis Start End Length
SignalP_GRAM_NEGATIVE 1 18 17
SignalP_GRAM_POSITIVE 1 20 19
SignalP_EUK 1 18 17

0 Qtllist

0 Targeting