Basic Information | |
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Species | Phaseolus vulgaris |
Cazyme ID | Phvul.002G200100.1 |
Family | AA7 |
Protein Properties | Length: 522 Molecular Weight: 59198 Isoelectric Point: 6.8427 |
Chromosome | Chromosome/Scaffold: 02 Start: 35927192 End: 35928903 |
Description | FAD-binding Berberine family protein |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA7 | 74 | 280 | 0 |
SSKPLVIVTPLDVSQIQATIICSQRHGLQIRTRSGGHDYEGLSYVAQVPFVLLDLLNLREITVDEESRTAWVQSGATLGELYYSISQKSKTLGFPAGSCA SVGIGGHFSGGGYGFMMRKYGLAADNVIDAHIIDVNGNLLDRQAMGEDLFWAIRGGVPSTVTVFNVSRTLEENATEIIQKWQLVAHKLDERIMIRVDIAR VNSSQHG |
Full Sequence |
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Protein Sequence Length: 522 Download |
MKYLSSYFTF ATAIALFFSF QPSSADSHEN FVRCLYNYPH ITNTISNVVY TQTNSSYSSL 60 LDHTIEIRRF SNSSSKPLVI VTPLDVSQIQ ATIICSQRHG LQIRTRSGGH DYEGLSYVAQ 120 VPFVLLDLLN LREITVDEES RTAWVQSGAT LGELYYSISQ KSKTLGFPAG SCASVGIGGH 180 FSGGGYGFMM RKYGLAADNV IDAHIIDVNG NLLDRQAMGE DLFWAIRGGV PSTVTVFNVS 240 RTLEENATEI IQKWQLVAHK LDERIMIRVD IARVNSSQHG KLTIQASFVS LFLGGVEELI 300 PLMQNNLPEL GLDRNDCKET SWIGSAIFTN AVLIGSSGNE SPESMLNQTQ IRSGYFKAKS 360 DYVKQPIPIE GLRGLWRLLC DVKVEYAQLQ LAPYGGRMYE ISESEIPFSH RSRYIFHIHY 420 NTKWQEEGDE IAQRHMDWIR RLYKYMEPYV SNSPRAAYMN YRDLDIGVNN NGYTSYTQAK 480 IWDLKYFNNN FKRLARVKTK VDPDNFFRNE QSIPILSMEE Y* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK11230 | PRK11230 | 0.006 | 77 | 236 | 186 | + glycolate oxidase subunit GlcD; Provisional | ||
COG0277 | GlcD | 1.0e-14 | 77 | 516 | 466 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam08031 | BBE | 1.0e-16 | 457 | 514 | 58 | + 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 | 4.0e-22 | 77 | 214 | 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 |
DDBJ | BAB33033.1 | 0 | 1 | 519 | 1 | 535 | CPRD2 [Vigna unguiculata] |
RefSeq | XP_002299045.1 | 0 | 5 | 517 | 6 | 531 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002330609.1 | 0 | 23 | 517 | 23 | 532 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002333020.1 | 0 | 14 | 517 | 13 | 531 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002333338.1 | 0 | 14 | 517 | 13 | 531 | 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 | 25 | 516 | 1 | 513 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 4dns_B | 0 | 22 | 516 | 4 | 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 | 22 | 516 | 4 | 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 | 20 | 516 | 2 | 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 | 20 | 516 | 2 | 496 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |