Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.011G159100.1 |
Family | AA7 |
Protein Properties | Length: 533 Molecular Weight: 59310.2 Isoelectric Point: 8.5814 |
Chromosome | Chromosome/Scaffold: 11 Start: 17620871 End: 17622571 |
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 | 74 | 524 | 0 |
SVPKPEFIFTPFNESDIQAAVACCKQLGIHFRVRSGGHDYEAVSYVSAIESPFIIIDLAKLRSVDVDIEDNSAWVQAGATNGELYYRIAEKSKTHGFPAG LCTSLGMGGLITGGAYGAMMRKYGLGADNVIDARIVDAQGRILDRKAMGEELFWAIRGGGGGSFGIITAWKVKLVPVPETVTVFTVTKTLEQGATKLLYR WQQVADKLDEDLFIRVSIQTAGTTGNRTITTSYNAVFLGDAKRLLRVMESSFPELGLTQKDCIETTWLESVLYTGSYPSNTPPEALLQANNVLKSYFKAK SDFVQEPIPESALKGIWKRLFKEEGGFMIWNPFGGMMSKISEFETPFPHRKGDLFMIQYVTGWQDASGDVGKHVKWIRELYKYMAPYVSKNPREAYVNYR DLDLGINRNTNTSFIKASVWGAKYFKGNFYRLALVKSKVDPDNIFRHEQSI |
Full Sequence |
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Protein Sequence Length: 533 Download |
MVLPSASILS ILVVLLLSPF VFSYPIQDTF LQCLSSTSES SFPFSTALYT PINNSSFTTV 60 LLSTAQNLRY ILPSVPKPEF IFTPFNESDI QAAVACCKQL GIHFRVRSGG HDYEAVSYVS 120 AIESPFIIID LAKLRSVDVD IEDNSAWVQA GATNGELYYR IAEKSKTHGF PAGLCTSLGM 180 GGLITGGAYG AMMRKYGLGA DNVIDARIVD AQGRILDRKA MGEELFWAIR GGGGGSFGII 240 TAWKVKLVPV PETVTVFTVT KTLEQGATKL LYRWQQVADK LDEDLFIRVS IQTAGTTGNR 300 TITTSYNAVF LGDAKRLLRV MESSFPELGL TQKDCIETTW LESVLYTGSY PSNTPPEALL 360 QANNVLKSYF KAKSDFVQEP IPESALKGIW KRLFKEEGGF MIWNPFGGMM SKISEFETPF 420 PHRKGDLFMI QYVTGWQDAS GDVGKHVKWI RELYKYMAPY VSKNPREAYV NYRDLDLGIN 480 RNTNTSFIKA SVWGAKYFKG NFYRLALVKS KVDPDNIFRH EQSIPPLPLH MR* 540 |
Functional Domains Download unfiltered results here | ||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
PRK13905 | murB | 0.0005 | 79 | 222 | 163 | + UDP-N-acetylenolpyruvoylglucosamine reductase; Provisional |
TIGR00387 | glcD | 0.0003 | 84 | 216 | 134 | + 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 | 3.0e-17 | 468 | 525 | 58 | + 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 | 4.0e-22 | 78 | 247 | 178 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] |
pfam01565 | FAD_binding_4 | 5.0e-30 | 78 | 217 | 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 |
RefSeq | XP_002299036.1 | 0 | 28 | 532 | 28 | 532 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002317092.1 | 0 | 27 | 532 | 27 | 532 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002330564.1 | 0 | 20 | 531 | 20 | 532 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002330620.1 | 0 | 27 | 532 | 27 | 532 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002332870.1 | 0 | 27 | 532 | 27 | 532 | predicted protein [Populus trichocarpa] |
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 | 4dns_B | 0 | 18 | 527 | 1 | 496 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
PDB | 4dns_A | 0 | 18 | 527 | 1 | 496 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
PDB | 3vte_A | 0 | 27 | 530 | 4 | 516 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3tsj_B | 0 | 27 | 527 | 8 | 496 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3tsj_A | 0 | 27 | 527 | 8 | 496 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
cannabinoid biosynthesis | RXN-7854 | EC-1.21.3 | tetrahydrocannabinolic acid synthase |