| Basic Information | |
|---|---|
| Species | Arabidopsis lyrata |
| Cazyme ID | 917168 |
| Family | AA7 |
| Protein Properties | Length: 542 Molecular Weight: 60857.7 Isoelectric Point: 9.8624 |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA7 | 86 | 537 | 0 |
| KPGFIFRPIHESQVQASIICSKKLGIHFRVRSGGHDFEALSYVSRIEKPFILIDLSKLRQVDVDIETNSAWVQPGATLGELYYRIAEKSKVHGFPAGLCT SVGIGGYMTGGGYGSLMRKFGLAGDNVLDVKMVDANGKLLDRTAMGEDLFWALRGGGGASFGIVLAWKIKLVPVPETVTIFTVTKTLKQDARLKIISKWQ QIASKLVEELHIRLVLRAVGNNGNKTITMSYLGQFLGEKGTLMKVMEKDFPELGLTQKDCTEMSWIESTLFHGGFPTGSPIEILLQRKSPLGKDYFKATS DFVKEPIPVLGLKGIFKRLIEGKIEFLNWTPYGGMMSKISESAIPFPHRNGTLFKILYYANWLENDKTSMSRKINSIKEIYSYMAPYVSSNPREAYVNYR DLDFGQNENNSKFNFIEAKIWGPKYFKDNFNRLVKIKTKVDPNNFFRHEQSI | |||
| Full Sequence |
|---|
| Protein Sequence Length: 542 Download |
| MGISKPHPTI SCILFLVLYF SFYCITPTSS SASLQDQFIN CVKRNTHVSF PLETTLFTPA 60 KNVSMFSQVL ESTAQNLQFL AKSLPKPGFI FRPIHESQVQ ASIICSKKLG IHFRVRSGGH 120 DFEALSYVSR IEKPFILIDL SKLRQVDVDI ETNSAWVQPG ATLGELYYRI AEKSKVHGFP 180 AGLCTSVGIG GYMTGGGYGS LMRKFGLAGD NVLDVKMVDA NGKLLDRTAM GEDLFWALRG 240 GGGASFGIVL AWKIKLVPVP ETVTIFTVTK TLKQDARLKI ISKWQQIASK LVEELHIRLV 300 LRAVGNNGNK TITMSYLGQF LGEKGTLMKV MEKDFPELGL TQKDCTEMSW IESTLFHGGF 360 PTGSPIEILL QRKSPLGKDY FKATSDFVKE PIPVLGLKGI FKRLIEGKIE FLNWTPYGGM 420 MSKISESAIP FPHRNGTLFK ILYYANWLEN DKTSMSRKIN SIKEIYSYMA PYVSSNPREA 480 YVNYRDLDFG QNENNSKFNF IEAKIWGPKY FKDNFNRLVK IKTKVDPNNF FRHEQSIPPM 540 P* 600 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| TIGR00387 | glcD | 0.008 | 136 | 263 | 137 | + 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 | 0.003 | 136 | 322 | 200 | + D-lactate dehydrogenase [cytochrome] | ||
| pfam08031 | BBE | 2.0e-19 | 480 | 538 | 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 | 5.0e-22 | 87 | 226 | 141 | + 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. | ||
| COG0277 | GlcD | 2.0e-22 | 87 | 539 | 473 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| Gene Ontology | |
|---|---|
| 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 | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAL24314.1 | 0 | 1 | 541 | 1 | 541 | berberine bridge enzyme-like protein [Arabidopsis thaliana] |
| RefSeq | NP_199251.1 | 0 | 1 | 541 | 1 | 540 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
| RefSeq | NP_199252.1 | 0 | 1 | 541 | 1 | 541 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
| RefSeq | NP_199253.1 | 0 | 1 | 540 | 1 | 536 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
| RefSeq | XP_002523164.1 | 0 | 36 | 541 | 31 | 532 | Reticuline oxidase precursor, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3vte_A | 0 | 32 | 541 | 1 | 514 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 4dns_B | 0 | 26 | 540 | 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 | 26 | 540 | 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 | 3tsj_B | 0 | 60 | 540 | 26 | 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 | 60 | 540 | 26 | 496 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
