Basic Information | |
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Species | Prunus persica |
Cazyme ID | ppa025579m |
Family | AA7 |
Protein Properties | Length: 614 Molecular Weight: 68169.4 Isoelectric Point: 6.7936 |
Chromosome | Chromosome/Scaffold: 4 Start: 4632708 End: 4635159 |
Description | FAD-binding Berberine family protein |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA7 | 71 | 290 | 0 |
TSISKPEAIIYPFHDSHVQAAVICSKTNGILIRIRSGGHDYEGQSYVSRAPFVIIDLSNLRSIDVDIENESAWVESGATFGELYYRIAEKSKAYGFPAGS CPTMGVGGHISGGGFGTLFRKYGLAADNVLDAKIVDVNGRVLDRKSMGEELFWAIRGGGGSSFGVIVAWKLRLVPVPPSVTVFSISKTTEQGATKLFSKW QNIADKFHEDLFLHTVIGVE |
Full Sequence |
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Protein Sequence Length: 614 Download |
MEIFKLLPIL FIFINPVWSI TSNSATESFL QCFTSHIQNL KSSSKIILIK NSSAYASVVQ 60 SSIQNLRFLN TSISKPEAII YPFHDSHVQA AVICSKTNGI LIRIRSGGHD YEGQSYVSRA 120 PFVIIDLSNL RSIDVDIENE SAWVESGATF GELYYRIAEK SKAYGFPAGS CPTMGVGGHI 180 SGGGFGTLFR KYGLAADNVL DAKIVDVNGR VLDRKSMGEE LFWAIRGGGG SSFGVIVAWK 240 LRLVPVPPSV TVFSISKTTE QGATKLFSKW QNIADKFHED LFLHTVIGVE DKAGTNGGKT 300 IVIEFSSLFL GPVEKLLLLM QDNFPELSVA RSDCTEMSWI ESVLYFASIS INESEALLNR 360 TQQSKSFFKA KSDYVNEPIS EAGLEGLWQN LIEVGAYLIL TPYGGKMSEI SNSEIPFPHR 420 SGNLFKIQYM VTWDNEKETE KHIGMMRKLY AYMAPYVSKS PRAAYLNYKD LDLGRNKDAN 480 TSYAQASIWA LDLFNWVGGG YYGSIDWVVT VEGGYGGGYG IEQFDSSQGS DCGQGWPWSR 540 SGLSPEKARS YGGWYRSYGS SPEKARKLAL VGNKRERRGD TEGNERERGL RTRLFYIEWV 600 LFCEPLFSLA ILE* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02805 | PLN02805 | 5.0e-6 | 72 | 247 | 185 | + D-lactate dehydrogenase [cytochrome] | ||
COG0277 | GlcD | 8.0e-21 | 76 | 459 | 398 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 5.0e-23 | 76 | 213 | 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. |
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 | 4 | 494 | 6 | 498 | hypothetical protein [Vitis vinifera] |
RefSeq | XP_002268361.1 | 0 | 4 | 494 | 6 | 498 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002299029.1 | 0 | 22 | 494 | 1 | 474 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002317088.1 | 0 | 3 | 494 | 5 | 498 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002523160.1 | 0 | 1 | 494 | 1 | 498 | 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 | 27 | 494 | 5 | 484 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 4dns_B | 0 | 22 | 495 | 6 | 468 | 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 | 495 | 6 | 468 | 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 | 494 | 6 | 467 | 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 | 494 | 6 | 467 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |