Basic Information | |
---|---|
Species | Prunus persica |
Cazyme ID | ppa016588m |
Family | AA7 |
Protein Properties | Length: 510 Molecular Weight: 57139.8 Isoelectric Point: 9.8018 |
Chromosome | Chromosome/Scaffold: 4 Start: 5025890 End: 5027419 |
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 | 54 | 501 | 0 |
PTTPKPLLIVAAKHESHVPATVICAKSLGLEIRIRSGGHDYEGVSYVSRNTKDFIVLDMFNLRSINIDMADESAWVQSGAILGEIFYAISMKSKNHAFPA GVCPSIGAGGHFTGGGYGNMMRKYGLSTDNIVDAKIVNVNGKILDRKAMGEDLFWAIRGGGGSSFGVILAWKIKFVRVPATVTVFEVKRTLALGATEILV KWQQVADKLDHDLFIRAIIKPANGTIEVSFMSLFLGNSERLLKLMSQSFPQLGLQKTDCHEMSWIQSVLYWTNYQNGTTSPEVLLNRVPKGQVFLKRKSD YVKQPISKTDLEALWKVMIEIGEVTMLWNPYGGKMSEIPETATPFPHRAGNLFKIQYSVNWKEEGFESTKRYLSLMKKLYVAMTPYVSKNPRMAFYNYRD LDIGTNSKGGYDEAKVYGTKYFKGNFERLVRIKTEVDPENFFRNEQSI |
Full Sequence |
---|
Protein Sequence Length: 510 Download |
SCTNSSSVEF NFLQCLSKHS QRSNPISEAI YTSKSASFSS VLQSYVRNLR FISPTTPKPL 60 LIVAAKHESH VPATVICAKS LGLEIRIRSG GHDYEGVSYV SRNTKDFIVL DMFNLRSINI 120 DMADESAWVQ SGAILGEIFY AISMKSKNHA FPAGVCPSIG AGGHFTGGGY GNMMRKYGLS 180 TDNIVDAKIV NVNGKILDRK AMGEDLFWAI RGGGGSSFGV ILAWKIKFVR VPATVTVFEV 240 KRTLALGATE ILVKWQQVAD KLDHDLFIRA IIKPANGTIE VSFMSLFLGN SERLLKLMSQ 300 SFPQLGLQKT DCHEMSWIQS VLYWTNYQNG TTSPEVLLNR VPKGQVFLKR KSDYVKQPIS 360 KTDLEALWKV MIEIGEVTML WNPYGGKMSE IPETATPFPH RAGNLFKIQY SVNWKEEGFE 420 STKRYLSLMK KLYVAMTPYV SKNPRMAFYN YRDLDIGTNS KGGYDEAKVY GTKYFKGNFE 480 RLVRIKTEVD PENFFRNEQS IPTLPSKQL* |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG0277 | GlcD | 1.0e-13 | 59 | 504 | 473 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 5.0e-17 | 59 | 198 | 143 | + 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 | 3.0e-18 | 447 | 502 | 56 | + 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. |
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 |
EMBL | CAN60572.1 | 0 | 5 | 505 | 25 | 530 | hypothetical protein [Vitis vinifera] |
EMBL | CAN80091.1 | 0 | 5 | 505 | 25 | 530 | hypothetical protein [Vitis vinifera] |
RefSeq | XP_002270585.1 | 0 | 5 | 505 | 25 | 530 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002317086.1 | 0 | 1 | 506 | 16 | 528 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002523155.1 | 0 | 11 | 503 | 28 | 523 | Reticuline oxidase precursor, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3vte_A | 0 | 11 | 505 | 6 | 514 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 4dns_B | 0 | 5 | 504 | 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 | 5 | 504 | 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 | 11 | 504 | 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 |
PDB | 3tsj_A | 0 | 11 | 504 | 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 | 509 | 11 | 504 | 0 |
DY290183 | 354 | 91 | 439 | 0 |
DY262774 | 380 | 128 | 496 | 0 |
CF514388 | 280 | 173 | 448 | 0 |
HO781153 | 349 | 172 | 506 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
---|