Basic Information | |
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Species | Capsella rubella |
Cazyme ID | Carubv10012287m |
Family | AA7 |
Protein Properties | Length: 532 Molecular Weight: 59450.9 Isoelectric Point: 9.8645 |
Chromosome | Chromosome/Scaffold: 1 Start: 10672917 End: 10674512 |
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 | 69 | 525 | 0 |
RNLRYFNNTTRKPVAIVAAADVSHIQATITCAKKLALQLRIRSGGHDYDGMSYVSTVDFVVLDMFNLRSIKIDHKLDTAWVESGAILGEIFYGVANKSND LRGFPAGICPGLGAGGHFSGGGYGNMMRKYGLSIDNIIDAKIVDVKGRVLDRSSMGEDLFWAIRGGGAASFCVVLAWKIKLVPVPAKVTVFNVETVGNRG SVNTTELVAKWQEIADKIDNDLFIRLTLSSSNKTVKASFMGMYLGNSLKLLKTMNAQFPELGLKKTECIEMKWIESVLFWLGIPPGTAPTSSMLNRIPQK QIYLKRKSDYVQKPISRTGLDAIFKVLLENENVTMAWNPYGGRMSEIPSTKTPFPHRAGNMFKIQYAANWFVPGEAVAKDCLSQTERVFEAMSPYVSKNP REAFFNYRDVDIGTSMNSTYKEGKVYGMKYFKNNFEKLVKVKSRVDPDNFFRYEQSI |
Full Sequence |
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Protein Sequence Length: 532 Download |
MKSLTIQTLV ITIFLFTIPT LFASPPTLED VFAQCLTDFK PSNPKSPIQN FIYTQQNPKF 60 LTILNNYVRN LRYFNNTTRK PVAIVAAADV SHIQATITCA KKLALQLRIR SGGHDYDGMS 120 YVSTVDFVVL DMFNLRSIKI DHKLDTAWVE SGAILGEIFY GVANKSNDLR GFPAGICPGL 180 GAGGHFSGGG YGNMMRKYGL SIDNIIDAKI VDVKGRVLDR SSMGEDLFWA IRGGGAASFC 240 VVLAWKIKLV PVPAKVTVFN VETVGNRGSV NTTELVAKWQ EIADKIDNDL FIRLTLSSSN 300 KTVKASFMGM YLGNSLKLLK TMNAQFPELG LKKTECIEMK WIESVLFWLG IPPGTAPTSS 360 MLNRIPQKQI YLKRKSDYVQ KPISRTGLDA IFKVLLENEN VTMAWNPYGG RMSEIPSTKT 420 PFPHRAGNMF KIQYAANWFV PGEAVAKDCL SQTERVFEAM SPYVSKNPRE AFFNYRDVDI 480 GTSMNSTYKE GKVYGMKYFK NNFEKLVKVK SRVDPDNFFR YEQSIPVLSS H* 540 |
Functional Domains Download unfiltered results here | ||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
COG0277 | GlcD | 8.0e-9 | 64 | 261 | 210 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] |
pfam08031 | BBE | 5.0e-16 | 471 | 526 | 56 | + 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 | 7.0e-17 | 81 | 221 | 142 | + 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 |
GenBank | AAF79255.1 | 0 | 1 | 531 | 1 | 527 | AC023279_4 F12K21.9 [Arabidopsis thaliana] |
RefSeq | NP_174358.1 | 0 | 1 | 531 | 1 | 531 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
RefSeq | NP_564449.1 | 0 | 1 | 531 | 1 | 527 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
RefSeq | XP_002317086.1 | 0 | 28 | 530 | 23 | 528 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002523155.1 | 0 | 32 | 526 | 29 | 522 | 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 | 4dns_B | 0 | 23 | 528 | 1 | 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 | 23 | 528 | 1 | 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 | 3vte_A | 0 | 32 | 531 | 7 | 516 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3tsj_B | 0 | 25 | 528 | 4 | 496 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3tsj_A | 0 | 25 | 528 | 4 | 496 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |