Basic Information | |
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Species | Cucumis sativus |
Cazyme ID | Cucsa.207580.1 |
Family | AA7 |
Protein Properties | Length: 497 Molecular Weight: 55646 Isoelectric Point: 6.4529 |
Chromosome | Chromosome/Scaffold: 01443 Start: 379911 End: 382700 |
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 | 43 | 261 | 0 |
RFSEPETPKPVAIITPSHASQVQATVICCKSHGLQIRTRSGGHDFEGRSYVANVPFVLIDLIKLNSITIDVEDESAWVQSGATVGELYFRIGEKSRTLGF PAGFAATIGLGGFLSGGGFGMMVRKYGLGADNVVDAYVVDGNGRVVNRYSMGEDLFWAIRGGGGGSFGIVLAWKLRLVQVPSIVTSFALHKIWDQNAANL IYRWQYIAPWVDQDLFISA |
Full Sequence |
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Protein Sequence Length: 497 Download |
MKDFVNCIYV HSSNNNDSNS TLIHTPSSSS YSYVLNFSIR NLRFSEPETP KPVAIITPSH 60 ASQVQATVIC CKSHGLQIRT RSGGHDFEGR SYVANVPFVL IDLIKLNSIT IDVEDESAWV 120 QSGATVGELY FRIGEKSRTL GFPAGFAATI GLGGFLSGGG FGMMVRKYGL GADNVVDAYV 180 VDGNGRVVNR YSMGEDLFWA IRGGGGGSFG IVLAWKLRLV QVPSIVTSFA LHKIWDQNAA 240 NLIYRWQYIA PWVDQDLFIS AWASFFSLFL RNATELLSLM EKTFPELGLK KEDCLETSWV 300 ESMAFSASGF VSAKSLELLL DRTPLHNGRY KTKSDYATEP ISETALEGMW ERFKDEELET 360 VQLILIPFGG KMNEISESET PSPHRAGYPI HIGYYLTWQR PDVDSKHLKW ARELHNYMTP 420 FVSKSPRAAY VNYRDLDMGT NNDDGAPTRC EEASIWGHRY FGNNFERLME VKRKVDPFNF 480 FRHEQSIPPA PPSVGI* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR00387 | glcD | 0.005 | 55 | 189 | 141 | + glycolate oxidase, subunit GlcD. This protein, the glycolate oxidase GlcD subunit, is similar in sequence to that of several D-lactate dehydrogenases, including that of E. coli. The glycolate oxidase has been found to have some D-lactate dehydrogenase activity [Energy metabolism, Other]. | ||
PLN02805 | PLN02805 | 0.0008 | 52 | 224 | 182 | + D-lactate dehydrogenase [cytochrome] | ||
pfam08031 | BBE | 7.0e-19 | 429 | 488 | 60 | + 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 | 3.0e-22 | 52 | 490 | 473 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 4.0e-24 | 52 | 189 | 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 |
RefSeq | XP_002299045.1 | 0 | 2 | 488 | 29 | 528 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002330609.1 | 0 | 2 | 489 | 29 | 530 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002330611.1 | 0 | 4 | 489 | 1 | 499 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002332196.1 | 0 | 2 | 489 | 22 | 523 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002333020.1 | 0 | 2 | 489 | 29 | 529 | 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 | 2 | 492 | 5 | 515 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 4dns_B | 0 | 2 | 489 | 11 | 495 | 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 | 2 | 489 | 11 | 495 | 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 | 2 | 489 | 9 | 495 | 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 | 2 | 489 | 9 | 495 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |