y
Basic Information | |
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Species | Glycine max |
Cazyme ID | Glyma08g08550.1 |
Family | AA7 |
Protein Properties | Length: 524 Molecular Weight: 58388.4 Isoelectric Point: 10.0561 |
Chromosome | Chromosome/Scaffold: 08 Start: 6111721 End: 6116168 |
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 | 299 | 0 |
PKPKFIFTPTRDSHVQAAVICSKKLGIHLRVLSGGHDFEGVSYVSEIESPFIVVDLIKLRDINVDIKSNTAWVQAGATNGELYYRIYEKSSLHGFPAGTC TSLGIGGHITGGAYGSMVRKYGLGADNVLDAKIVDANGRILDRKAMGEDLFWAIRGGGGGSFGILLWWKVKLVPVPPTVTVFTVKKTLEQGATKLLHRWQ EVAPFLDENLFIRVRIQRAQSTVTTS |
Full Sequence |
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Protein Sequence Length: 524 Download |
MASLVSHLRL SVLLLSVSLG NSASLQENFV QCLNLNSDRT FPFNPLIYTP KSPSFTSVLD 60 SSGKNQRLLV PSTPKPKFIF TPTRDSHVQA AVICSKKLGI HLRVLSGGHD FEGVSYVSEI 120 ESPFIVVDLI KLRDINVDIK SNTAWVQAGA TNGELYYRIY EKSSLHGFPA GTCTSLGIGG 180 HITGGAYGSM VRKYGLGADN VLDAKIVDAN GRILDRKAMG EDLFWAIRGG GGGSFGILLW 240 WKVKLVPVPP TVTVFTVKKT LEQGATKLLH RWQEVAPFLD ENLFIRVRIQ RAQSTVTTSY 300 EGLFLGGARK LLKIMKTSFP ELGVTRKDCM ETSWIKSVLY IAGFPSGTPP EVLLKGKPIA 360 KFFFKGKSDF VRKPIPETGL EGLRQRLLVE DSPLILWSPY GGRMNQFSES DTPFPYRNGT 420 LFISLYISLW QEGEKNVAKH IDWIGNLHNY MGAYVPSFPR GQYVNYRDLD LGINTKNNTG 480 NIQESAWGYR YFKNNFDRLV KIKTKVDPQN VFRHEQSIPP LPK* 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG0277 | GlcD | 1.0e-10 | 76 | 237 | 172 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam08031 | BBE | 5.0e-18 | 463 | 519 | 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. | ||
pfam01565 | FAD_binding_4 | 2.0e-20 | 76 | 215 | 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 | CAN81654.1 | 0 | 10 | 523 | 11 | 529 | hypothetical protein [Vitis vinifera] |
RefSeq | XP_002268361.1 | 0 | 10 | 523 | 11 | 529 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002330564.1 | 0 | 22 | 523 | 23 | 530 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002330565.1 | 0 | 22 | 521 | 23 | 528 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002523164.1 | 0 | 27 | 522 | 31 | 532 | Reticuline oxidase precursor, 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 | 3vte_A | 0 | 23 | 522 | 1 | 514 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 4dns_B | 0 | 22 | 521 | 6 | 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 | 22 | 521 | 6 | 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 | 3tsj_B | 0 | 24 | 523 | 6 | 498 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
PDB | 3tsj_A | 0 | 24 | 523 | 6 | 498 | 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 |