Basic Information | |
---|---|
Species | Cucumis sativus |
Cazyme ID | Cucsa.167270.1 |
Family | AA7 |
Protein Properties | Length: 477 Molecular Weight: 53052.3 Isoelectric Point: 8.0011 |
Chromosome | Chromosome/Scaffold: 01154 Start: 636634 End: 638780 |
Description | FAD-binding Berberine family protein |
View CDS |
External Links |
---|
NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
AA7 | 48 | 468 | 0 |
NLRFSTPNTPKPLLIITPSNISHIQASVICFKSHHLQIRIRSGGHDYERSIAVDVETSTAWVQSGATLGELYYRIAEKSRTLAFPAGTSPTVGVGGHFSG GGYGTLLRKYGLAADNVIDAYLVDANGEFLDRDSMGEDLFWAIRGGGGGSFGIVVAWKVKLVSVPTTVTICTTTRNMEEGAINLIHQWQYVANKFDEDLF LGIILTGGKISAEGGKINPIALFFTLFLGKADELMAILSKTFPELGLTKEECKETSWIESTIFVASGFQMGDQASDVLLNRTTLANGNIKKSNLTTLKSE DIEVVNLGFTPYGGRMSQISESEIPFSHRTGNLYKIGYLIRWEEQGVDIYSYMTPFVSKSPRAAYVNYRDLDIGSNNKYEKTSYKRVRVWGLKYFGNNFN RLVQIKKKVDPYNFFSHEQSI |
Full Sequence |
---|
Protein Sequence Length: 477 Download |
APNSSFIEHE DFLQCLLHHS PDANSITKLV YTPFNTSYSS ILNFSIRNLR FSTPNTPKPL 60 LIITPSNISH IQASVICFKS HHLQIRIRSG GHDYERSIAV DVETSTAWVQ SGATLGELYY 120 RIAEKSRTLA FPAGTSPTVG VGGHFSGGGY GTLLRKYGLA ADNVIDAYLV DANGEFLDRD 180 SMGEDLFWAI RGGGGGSFGI VVAWKVKLVS VPTTVTICTT TRNMEEGAIN LIHQWQYVAN 240 KFDEDLFLGI ILTGGKISAE GGKINPIALF FTLFLGKADE LMAILSKTFP ELGLTKEECK 300 ETSWIESTIF VASGFQMGDQ ASDVLLNRTT LANGNIKKSN LTTLKSEDIE VVNLGFTPYG 360 GRMSQISESE IPFSHRTGNL YKIGYLIRWE EQGVDIYSYM TPFVSKSPRA AYVNYRDLDI 420 GSNNKYEKTS YKRVRVWGLK YFGNNFNRLV QIKKKVDPYN FFSHEQSIPT LPYHRI* 480 |
Functional Domains Download unfiltered results here | ||||||
---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
COG0277 | GlcD | 2.0e-12 | 59 | 209 | 174 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] |
pfam08031 | BBE | 3.0e-17 | 411 | 469 | 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. |
pfam01565 | FAD_binding_4 | 2.0e-18 | 59 | 178 | 137 | + 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 | |
---|---|
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 | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
RefSeq | XP_002299022.1 | 0 | 8 | 471 | 20 | 523 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002300557.1 | 0 | 8 | 471 | 27 | 528 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002330608.1 | 0 | 9 | 471 | 30 | 533 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002332196.1 | 0 | 9 | 471 | 21 | 524 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002334045.1 | 0 | 9 | 471 | 28 | 528 | predicted protein [Populus trichocarpa] |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3vte_A | 0 | 10 | 475 | 5 | 517 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3tsj_B | 0 | 10 | 471 | 9 | 496 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3tsj_A | 0 | 10 | 471 | 9 | 496 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3tsh_A | 0 | 10 | 471 | 9 | 496 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
PDB | 4dns_B | 0 | 9 | 471 | 10 | 496 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
EST Download unfiltered results here | ||||
---|---|---|---|---|
Hit | Length | Start | End | EValue |
HO777438 | 510 | 9 | 471 | 0 |
JG480065 | 252 | 7 | 240 | 0 |
HO798639 | 317 | 35 | 331 | 0 |
DY801911 | 259 | 8 | 247 | 0 |
JG555271 | 240 | 8 | 229 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
---|
![]() |