Basic Information | |
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Species | Cucumis sativus |
Cazyme ID | Cucsa.167230.1 |
Family | AA7 |
Protein Properties | Length: 538 Molecular Weight: 59846.8 Isoelectric Point: 9.513 |
Chromosome | Chromosome/Scaffold: 01154 Start: 592992 End: 599430 |
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 | 72 | 534 | 0 |
RFSKPETPKPLLIITPSHVSHIQAAVICSKSHGLQIRTRSGGHDYEGLSYVASHPFIILDLINLRSMKIDVESNTAWVESGTTLGELYYRIGEKSRTLAF PAGICPTVGVGGHFSGGGYGLMLRKFGLAADNVIDAYLVDANGKVHDRESMGEDLFWAIRGGGGGSFGIVVAWKIKLVSVPATVTMCNTYRNLKGDGIKL VHQWQYVANKLDENLFLGIILTGGNITTTQEGITNPIATFFSLFLGKVNELVATLSTTFPELGLIKQDCIETSWIESTLIASTGVQTVESLEPLLNRTPS NLENEKIKSDYIKEPISIATIEGIWQRLKAQDIETSQLIFIPYGGRMSQISESETPFSHRVGNLYKIGYILGWKEQSLKAKKKHISWIREIYEYMTPFVS KSPRSAYANYRDLDIGVNKKYGKTSVKQASIWGLKYFGNNFKRLVYVKTKVDPYDFFRHEQSI |
Full Sequence |
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Protein Sequence Length: 538 Download |
MKYSSPLIPF SLILIVVSSS SLWVSASPHK HHNFLQCLSE HSSKSYPISK VVHTPINSSY 60 SSVLNFSIRN LRFSKPETPK PLLIITPSHV SHIQAAVICS KSHGLQIRTR SGGHDYEGLS 120 YVASHPFIIL DLINLRSMKI DVESNTAWVE SGTTLGELYY RIGEKSRTLA FPAGICPTVG 180 VGGHFSGGGY GLMLRKFGLA ADNVIDAYLV DANGKVHDRE SMGEDLFWAI RGGGGGSFGI 240 VVAWKIKLVS VPATVTMCNT YRNLKGDGIK LVHQWQYVAN KLDENLFLGI ILTGGNITTT 300 QEGITNPIAT FFSLFLGKVN ELVATLSTTF PELGLIKQDC IETSWIESTL IASTGVQTVE 360 SLEPLLNRTP SNLENEKIKS DYIKEPISIA TIEGIWQRLK AQDIETSQLI FIPYGGRMSQ 420 ISESETPFSH RVGNLYKIGY ILGWKEQSLK AKKKHISWIR EIYEYMTPFV SKSPRSAYAN 480 YRDLDIGVNK KYGKTSVKQA SIWGLKYFGN NFKRLVYVKT KVDPYDFFRH EQSIPTL* 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG0277 | GlcD | 1.0e-13 | 81 | 264 | 195 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam08031 | BBE | 2.0e-16 | 477 | 535 | 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-21 | 81 | 218 | 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_002299022.1 | 0 | 23 | 537 | 14 | 523 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002299045.1 | 0 | 7 | 537 | 8 | 530 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002330608.1 | 0 | 25 | 537 | 24 | 533 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002332196.1 | 0 | 23 | 537 | 14 | 524 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002334045.1 | 0 | 23 | 537 | 21 | 528 | 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 | 26 | 537 | 1 | 513 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3tsj_B | 0 | 28 | 537 | 5 | 496 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3tsj_A | 0 | 28 | 537 | 5 | 496 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3tsh_A | 0 | 28 | 537 | 5 | 496 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
PDB | 4dns_B | 0 | 31 | 537 | 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 |