y
Basic Information | |
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Species | Brassica rapa |
Cazyme ID | Bra013472 |
Family | AA7 |
Protein Properties | Length: 528 Molecular Weight: 58758 Isoelectric Point: 9.6337 |
Chromosome | Chromosome/Scaffold: 01 Start: 5857739 End: 5859322 |
Description | FAD-binding Berberine family protein |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA7 | 77 | 521 | 0 |
AIIAAKHESHVQATVVCAKSNGVQIRTRSGGHDLDGLSYVSSIPFVVLDMHNLRSITVDVRSKKAWVQAGAIMGELYTKIAEKSKKLAFPAGICPTVGAG GHISGGGYGNLIRKHGLSVDHVVDAQLVDVNGKILNRSSMGEDLFWAIRGGGGASFGVILSYTINLVEIPKTITVFKVNKTLEQGATDVLYKWQLVSSKL PRELFLRAMPDLKIGAKPGDKTIAVKFYAQFLGSSEKLMKIINKNLPELGLKREDCYEMSWLNTTMFWMNYPVGAPTSILLDRPSAPPGQFYKGKSDYVK KPIPKEGMEKIWRTMLKFNNVWMQWNPYGGVMDKIPANATAFPHRKGNLFKIQYFALWTDANATDANLGLMRELYGVAEPYVSSNPREAFLNYRDVDVGS NPSGETNVEEAMIYGSKYFVGNLKRLMDVKAKCDPDNFFRYEQSI |
Full Sequence |
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Protein Sequence Length: 528 Download |
MKEVLCVLFF VLVSVSYAKV TKPNTDNFLR CLRSRTSPEY PITEAIYTPD NSIFLTSYLS 60 YAKNKRCSDP NNTNLIAIIA AKHESHVQAT VVCAKSNGVQ IRTRSGGHDL DGLSYVSSIP 120 FVVLDMHNLR SITVDVRSKK AWVQAGAIMG ELYTKIAEKS KKLAFPAGIC PTVGAGGHIS 180 GGGYGNLIRK HGLSVDHVVD AQLVDVNGKI LNRSSMGEDL FWAIRGGGGA SFGVILSYTI 240 NLVEIPKTIT VFKVNKTLEQ GATDVLYKWQ LVSSKLPREL FLRAMPDLKI GAKPGDKTIA 300 VKFYAQFLGS SEKLMKIINK NLPELGLKRE DCYEMSWLNT TMFWMNYPVG APTSILLDRP 360 SAPPGQFYKG KSDYVKKPIP KEGMEKIWRT MLKFNNVWMQ WNPYGGVMDK IPANATAFPH 420 RKGNLFKIQY FALWTDANAT DANLGLMREL YGVAEPYVSS NPREAFLNYR DVDVGSNPSG 480 ETNVEEAMIY GSKYFVGNLK RLMDVKAKCD PDNFFRYEQS IHPLLAM* 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR01678 | FAD_lactone_ox | 0.006 | 82 | 243 | 163 | + sugar 1,4-lactone oxidases. This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1. | ||
TIGR00387 | glcD | 0.004 | 70 | 251 | 196 | + glycolate oxidase, subunit GlcD. This protein, the glycolate oxidase GlcD subunit, is similar in sequence to that of several D-lactate dehydrogenases, including that of E. coli. The glycolate oxidase has been found to have some D-lactate dehydrogenase activity [Energy metabolism, Other]. | ||
pfam08031 | BBE | 4.0e-12 | 465 | 521 | 57 | + Berberine and berberine like. This domain is found in the berberine bridge and berberine bridge- like enzymes which are involved in the biosynthesis of numerous isoquinoline alkaloids. They catalyze the transformation of the N-methyl group of (S)-reticuline into the C-8 berberine bridge carbon of (S)-scoulerine. | ||
COG0277 | GlcD | 1.0e-16 | 77 | 251 | 182 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 3.0e-21 | 77 | 214 | 139 | + 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. |
Gene Ontology | |
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GO Term | Description |
GO:0008762 | UDP-N-acetylmuramate dehydrogenase activity |
GO:0016491 | oxidoreductase activity |
GO:0050660 | flavin adenine dinucleotide binding |
GO:0055114 | oxidation-reduction process |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
RefSeq | NP_173964.1 | 0 | 1 | 527 | 1 | 527 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
RefSeq | NP_173966.1 | 0 | 1 | 524 | 1 | 525 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
RefSeq | NP_193812.1 | 0 | 18 | 527 | 19 | 528 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
RefSeq | NP_564244.1 | 0 | 1 | 526 | 1 | 527 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
RefSeq | NP_564245.1 | 0 | 18 | 527 | 19 | 530 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3vte_A | 0 | 26 | 524 | 5 | 513 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3tsj_B | 0 | 26 | 525 | 9 | 497 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3tsj_A | 0 | 26 | 525 | 9 | 497 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3tsh_A | 0 | 26 | 525 | 9 | 497 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
PDB | 4dns_B | 0 | 27 | 525 | 12 | 497 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
cannabinoid biosynthesis | RXN-7854 | EC-1.21.3 | tetrahydrocannabinolic acid synthase |