y
Basic Information | |
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Species | Cucumis sativus |
Cazyme ID | Cucsa.167260.1 |
Family | AA7 |
Protein Properties | Length: 544 Molecular Weight: 60419.4 Isoelectric Point: 9.0397 |
Chromosome | Chromosome/Scaffold: 01154 Start: 630827 End: 633238 |
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 | 76 | 303 | 0 |
IPNTPKPLFIITPTNISHVQAAVICSKSHGLQIRIRSGGHDFEGLSYVAYHPFIIVDLIDLSSVTIEVKQSTAWVQSGATLGELYYRIAEKSRTLAFPAG NSPTVGVGGHFSGGGFGTLLRKYGLAADNVIDAYLVDANGVFHDRKSMGEDLFWAIRGGGGGSFGIVVAWKVKLVPVPATVTICTISRTLEEEAIKLVDQ WQYVANKLDEDLFLGINLLGGKISAQGD |
Full Sequence |
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Protein Sequence Length: 544 Download |
MKFSLLLPLS LAFIAVCSSS SVWPSASSHV NHEEFLQCLL HHSPHSKSIA KLAYTPINTS 60 YSSVLNFSIR NLRFSIPNTP KPLFIITPTN ISHVQAAVIC SKSHGLQIRI RSGGHDFEGL 120 SYVAYHPFII VDLIDLSSVT IEVKQSTAWV QSGATLGELY YRIAEKSRTL AFPAGNSPTV 180 GVGGHFSGGG FGTLLRKYGL AADNVIDAYL VDANGVFHDR KSMGEDLFWA IRGGGGGSFG 240 IVVAWKVKLV PVPATVTICT ISRTLEEEAI KLVDQWQYVA NKLDEDLFLG INLLGGKISA 300 QGDKINPIAL FFSLFLGKAD ELMAILNKTF PQLGLTKEEC KETSWIESVV YTGNGLQIED 360 QPLEVLLNRT PLATGNIKMK SDYVKEPIPK ATIEEIWQRL ESQDIEGANL VFVPYGGRMS 420 QISDSEIPFS HRAGNLYKIG YLTGWFEPGV NAEKTHLNWI RDIYGYMTPF VSKSPRAAYV 480 NYRDLDIGSN SKYGKTSYKR ARVWGLKYFG NNFNRMVYVK NKVDPYNFFR HEQSIPVLLK 540 HKI* 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam08031 | BBE | 5.0e-16 | 478 | 536 | 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. | ||
COG0277 | GlcD | 1.0e-16 | 82 | 538 | 477 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 9.0e-19 | 82 | 215 | 135 | + 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 | 27 | 538 | 16 | 523 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002299045.1 | 0 | 32 | 538 | 28 | 530 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002330608.1 | 0 | 25 | 538 | 24 | 533 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002332196.1 | 0 | 26 | 538 | 16 | 524 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002334045.1 | 0 | 23 | 538 | 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 | 33 | 541 | 5 | 516 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3tsj_B | 0 | 33 | 540 | 9 | 498 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3tsj_A | 0 | 33 | 540 | 9 | 498 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3tsh_A | 0 | 33 | 540 | 9 | 498 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
PDB | 4dns_B | 0 | 32 | 539 | 10 | 497 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |