Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.011G158100.2 |
Family | AA7 |
Protein Properties | Length: 518 Molecular Weight: 58407.9 Isoelectric Point: 6.9656 |
Chromosome | Chromosome/Scaffold: 11 Start: 17533889 End: 17535838 |
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 | 49 | 511 | 0 |
RNLRFNTTATPKPLVIVTPVNVSQIQDVVICSKKHGLQIRVRSGGHDFEGLSYVSIVPFVLVDLINLRMINVDVENSNAWVEAGATLGEVYYRIAEKSKT LAFPAGVSPTVGVGGHFSGGGSGMILRKFGLAADHITDAVLVDVEGRIHDRKSMGEDLFWAIRGGGGNTFGIVVAWKLNLVPVPPIVTAFNVSRTLEQNA TKLVHRWQFVSNKLHEDIFTRIFLRKVESSQRGKTTIQAAFTTLFIGEVDRLLSLMQESFPELGLVKEDCIEMSWIESVLYFAGFPSNTSLDALLDRTPI SDVFFKIKSDYVKEPLPEIALEGIWERMDQLEVQISELQFTAYGGKMDEISESSLPFPHRAGIIYQIEYAVLWEEESSEASQRYISWIRRLLNYMTPYVS KNPRQVYVNYRDLDLGINKLDGNTSYKQASIWGRKYFKNNFDRLVRVKTAVDPANFFRHEQSI |
Full Sequence |
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Protein Sequence Length: 518 Download |
MNSLIPSILP FLSIFLLSFS WATSAHTHDD FLHCLYNKNS DSISKFSIRN LRFNTTATPK 60 PLVIVTPVNV SQIQDVVICS KKHGLQIRVR SGGHDFEGLS YVSIVPFVLV DLINLRMINV 120 DVENSNAWVE AGATLGEVYY RIAEKSKTLA FPAGVSPTVG VGGHFSGGGS GMILRKFGLA 180 ADHITDAVLV DVEGRIHDRK SMGEDLFWAI RGGGGNTFGI VVAWKLNLVP VPPIVTAFNV 240 SRTLEQNATK LVHRWQFVSN KLHEDIFTRI FLRKVESSQR GKTTIQAAFT TLFIGEVDRL 300 LSLMQESFPE LGLVKEDCIE MSWIESVLYF AGFPSNTSLD ALLDRTPISD VFFKIKSDYV 360 KEPLPEIALE GIWERMDQLE VQISELQFTA YGGKMDEISE SSLPFPHRAG IIYQIEYAVL 420 WEEESSEASQ RYISWIRRLL NYMTPYVSKN PRQVYVNYRD LDLGINKLDG NTSYKQASIW 480 GRKYFKNNFD RLVRVKTAVD PANFFRHEQS IPPLSSW* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR01679 | bact_FAD_ox | 0.002 | 58 | 230 | 177 | + FAD-linked oxidoreductase. This model represents a family of bacterial oxidoreductases with covalently linked FAD, closely related to two different eukaryotic oxidases, 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. | ||
pfam01565 | FAD_binding_4 | 9.0e-19 | 61 | 198 | 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. | ||
pfam08031 | BBE | 7.0e-19 | 454 | 512 | 59 | + 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-21 | 61 | 514 | 476 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] |
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_002299021.1 | 0 | 24 | 517 | 26 | 533 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002299022.1 | 0 | 21 | 517 | 14 | 526 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002300557.1 | 0 | 1 | 517 | 1 | 531 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002317084.1 | 0 | 1 | 517 | 1 | 517 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002334045.1 | 0 | 21 | 517 | 21 | 531 | 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 | 3vte_A | 0 | 42 | 514 | 35 | 513 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 4dns_B | 0 | 24 | 514 | 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 | 24 | 514 | 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 | 29 | 514 | 9 | 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_A | 0 | 29 | 514 | 9 | 496 | 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 |