y
Basic Information | |
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Species | Glycine max |
Cazyme ID | Glyma10g32070.1 |
Family | AA7 |
Protein Properties | Length: 551 Molecular Weight: 61390 Isoelectric Point: 6.0296 |
Chromosome | Chromosome/Scaffold: 10 Start: 40517954 End: 40520086 |
Description | FAD-binding Berberine family protein |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA7 | 69 | 535 | 0 |
NLRFAEPVIPKPIAIVLPESLEQLQKSVACCREGFMEIRVRCGGHSYEGTSYVADDGTPFVIIDMMNLNHVWVDMETETAWVEGGATLGETYYAISQASN EHGFSGGSCPTVGVGGHIGGGGFGILSRKYGLAADNVVDALLVNADGKLFDRETMGEDVFWAIRGGGGGLWGIIYAWKIKVLKLPQVVTSFTVSRTGTKR HVANLVHKWQNVAPNLEDDFYLSCFVGAGLPQAKTKGLSTTFNGFYLGPRAGAISILDHAFPELGIVEEECIEMSWIQSTVFFSGLSDGASVSDLNNRYL QEKQYFKAKSDYVKKHVPLVGIETALDILEKEPKGYVILDPYGGKMHNISSESIAFPHRRGNLFTIQYLIYWKEADNDKNSDYVDWIRGFYAAMTPFVSW GPRAAYVNYMDFDLGVMERISNGANMKDVVEHARVWGEKYFLSNYDRLVRAKTLIDPNNVFTNDQGI |
Full Sequence |
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Protein Sequence Length: 551 Download |
MFYFLKRLCL LCFLLLSFDV SLCSCASLRD LASCLDNHDI KNFTTLPYKE HDHSSAYNYY 60 KILNFSIQNL RFAEPVIPKP IAIVLPESLE QLQKSVACCR EGFMEIRVRC GGHSYEGTSY 120 VADDGTPFVI IDMMNLNHVW VDMETETAWV EGGATLGETY YAISQASNEH GFSGGSCPTV 180 GVGGHIGGGG FGILSRKYGL AADNVVDALL VNADGKLFDR ETMGEDVFWA IRGGGGGLWG 240 IIYAWKIKVL KLPQVVTSFT VSRTGTKRHV ANLVHKWQNV APNLEDDFYL SCFVGAGLPQ 300 AKTKGLSTTF NGFYLGPRAG AISILDHAFP ELGIVEEECI EMSWIQSTVF FSGLSDGASV 360 SDLNNRYLQE KQYFKAKSDY VKKHVPLVGI ETALDILEKE PKGYVILDPY GGKMHNISSE 420 SIAFPHRRGN LFTIQYLIYW KEADNDKNSD YVDWIRGFYA AMTPFVSWGP RAAYVNYMDF 480 DLGVMERISN GANMKDVVEH ARVWGEKYFL SNYDRLVRAK TLIDPNNVFT NDQGIPPISL 540 TISDVKPQSK * 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR01678 | FAD_lactone_ox | 0.0007 | 79 | 280 | 207 | + 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. | ||
PRK11230 | PRK11230 | 0.0004 | 80 | 274 | 212 | + glycolate oxidase subunit GlcD; Provisional | ||
pfam08031 | BBE | 9.0e-15 | 473 | 536 | 64 | + 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-21 | 80 | 538 | 474 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 2.0e-23 | 80 | 219 | 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 |
EMBL | CBI16966.1 | 0 | 10 | 538 | 287 | 767 | unnamed protein product [Vitis vinifera] |
EMBL | CBI16966.1 | 0 | 376 | 516 | 85 | 224 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002264336.1 | 0 | 10 | 538 | 11 | 534 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002329230.1 | 0 | 25 | 537 | 11 | 525 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002533924.1 | 0 | 1 | 540 | 1 | 537 | d-lactate dehydrogenase, putative [Ricinus communis] |
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 | 3d2j_A | 0 | 12 | 539 | 7 | 520 | A Chain A, Polygalacturonase From Erwinia Carotovora Ssp. Carotovora |
PDB | 3d2h_A | 0 | 12 | 539 | 7 | 520 | A Chain A, Polygalacturonase From Erwinia Carotovora Ssp. Carotovora |
PDB | 3d2d_A | 0 | 12 | 539 | 7 | 520 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Reticuline |
PDB | 3fw9_A | 0 | 30 | 539 | 1 | 495 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Scoulerine |
PDB | 4ec3_A | 0 | 30 | 539 | 7 | 501 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |
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 |