Basic Information | |
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Species | Panicum virgatum |
Cazyme ID | Pavirv00001496m |
Family | AA7 |
Protein Properties | Length: 475 Molecular Weight: 51024.6 Isoelectric Point: 6.9632 |
Chromosome | Chromosome/Scaffold: 010245 Start: 11118 End: 12610 |
Description | FAD-binding Berberine family protein |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA7 | 33 | 467 | 0 |
VGKPAAVILPASKRDLRRAVLCARSSSLAIRVRSGGHSYEGLSYTTENHVPFVVIDLARLNHVRVDPAAATVWAESGATLGEVYRVVGLSSRNLALSAGS CATLGMGGHVAGGGFGLLSRKHGLAADNVLDAILIDPSGDTLTRDTMDDDVFWAIRGGGGGSWGVVYAWKLRLVPVPDNITVFSVGRTGPAELIAGLMHR WQYVAPSLPDEFYLSTFVPTGSSNGNLSMSFTGQVLGPKHLAMSVLDQTFPELGLAESELSEVSWVESAANFAGVSSVADLTNRQPSVGEYAKRKSDYVQ GSIQLDPYGGAMARMGSAATPFPHRAGYLYSIQYAVSWNASDLDRAEEYIGWLRSFYGFMSSYVSKSPRAAYVNYLDLDLGTNDWANATGGTSGSKSVAR AASWGERYFFTNFDRLVRAKSKVDPENVFNNAQSI |
Full Sequence |
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Protein Sequence Length: 475 Download |
MAVSQLLPPV VPRAYTPLLD SSIRNLRFEL PGVGKPAAVI LPASKRDLRR AVLCARSSSL 60 AIRVRSGGHS YEGLSYTTEN HVPFVVIDLA RLNHVRVDPA AATVWAESGA TLGEVYRVVG 120 LSSRNLALSA GSCATLGMGG HVAGGGFGLL SRKHGLAADN VLDAILIDPS GDTLTRDTMD 180 DDVFWAIRGG GGGSWGVVYA WKLRLVPVPD NITVFSVGRT GPAELIAGLM HRWQYVAPSL 240 PDEFYLSTFV PTGSSNGNLS MSFTGQVLGP KHLAMSVLDQ TFPELGLAES ELSEVSWVES 300 AANFAGVSSV ADLTNRQPSV GEYAKRKSDY VQGSIQLDPY GGAMARMGSA ATPFPHRAGY 360 LYSIQYAVSW NASDLDRAEE YIGWLRSFYG FMSSYVSKSP RAAYVNYLDL DLGTNDWANA 420 TGGTSGSKSV ARAASWGERY FFTNFDRLVR AKSKVDPENV FNNAQSIPPL RYDD* 480 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR01678 | FAD_lactone_ox | 0.0001 | 35 | 207 | 179 | + 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. | ||
TIGR01677 | pln_FAD_oxido | 1.0e-5 | 37 | 115 | 81 | + plant-specific FAD-dependent oxidoreductase. This model represents an uncharacterized plant-specific family of FAD-dependent oxidoreductases. At least seven distinct members are found in Arabidopsis thaliana. The family shows considerable sequence similarity to three different enzymes of ascorbic acid biosynthesis: L-galactono-1,4-lactone dehydrogenase (EC 1.3.2.3) from higher plants, D-arabinono-1,4-lactone oxidase (EC 1.1.3.37 from Saccharomyces cerevisiae, and L-gulonolactone oxidase (EC 1.1.3.8) from mouse, as well as to a bacterial sorbitol oxidase. The class of compound acted on by members of this family is unknown. | ||
pfam08031 | BBE | 2.0e-15 | 403 | 468 | 66 | + 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-19 | 34 | 470 | 459 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 5.0e-24 | 36 | 175 | 141 | + 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 |
GenBank | EAZ05659.1 | 0 | 3 | 470 | 42 | 528 | hypothetical protein OsI_27886 [Oryza sativa Indica Group] |
RefSeq | NP_001061035.1 | 0 | 3 | 470 | 42 | 528 | Os08g0158200 [Oryza sativa (japonica cultivar-group)] |
RefSeq | XP_002445086.1 | 0 | 14 | 470 | 58 | 559 | hypothetical protein SORBIDRAFT_07g003920 [Sorghum bicolor] |
RefSeq | XP_002445087.1 | 0 | 14 | 469 | 63 | 556 | hypothetical protein SORBIDRAFT_07g003930 [Sorghum bicolor] |
RefSeq | XP_002445088.1 | 0 | 14 | 445 | 63 | 519 | hypothetical protein SORBIDRAFT_07g003940 [Sorghum bicolor] |
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 | 3fw9_A | 0 | 15 | 470 | 25 | 494 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Scoulerine |
PDB | 4ec3_A | 0 | 15 | 470 | 31 | 500 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |
PDB | 3gsy_A | 0 | 15 | 470 | 31 | 500 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
PDB | 3d2j_A | 0 | 15 | 470 | 50 | 519 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
PDB | 3d2h_A | 0 | 15 | 470 | 50 | 519 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
berberine biosynthesis | RETICULINE-OXIDASE-RXN | EC-1.21.3.3 | reticuline oxidase |
dehydroscoulerine biosynthesis | RETICULINE-OXIDASE-RXN | EC-1.21.3.3 | reticuline oxidase |
sanguinarine and macarpine biosynthesis | RETICULINE-OXIDASE-RXN | EC-1.21.3.3 | reticuline oxidase |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO777438 | 507 | 2 | 474 | 0 |
FL865087 | 144 | 332 | 475 | 0 |
FL865088 | 144 | 332 | 475 | 0 |
EC892424 | 224 | 13 | 236 | 0 |
EG376970 | 215 | 3 | 217 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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