y
Basic Information | |
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Species | Arabidopsis lyrata |
Cazyme ID | 890625 |
Family | AA7 |
Protein Properties | Length: 528 Molecular Weight: 59901.8 Isoelectric Point: 10.0067 |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA7 | 64 | 299 | 0 |
NLRFNISSTPKPFLIIAATHESHVQAAVTCGKRHNLQMKIRSGGHDYDGLSYVTYSRKPFFVLDMFNLRSVDVDVASKTAWVQTGAILGEVYYYIWEKSK TLAYPAGICPTVGVGGHISGGGYGNMMRKYGLTVDNTIDARMVDVNGKILDRKLMGEDLYWAINGGGGGSYGVVLAYKINLVEVPENVTVFRISRTLEQN ATEIVNRWQRVAPELPDELFIRTVIDVVNSTVSSQK |
Full Sequence |
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Protein Sequence Length: 528 Download |
MKYTLILFLF FVVFIWQSSS SSANSETFTQ CLTSNSDPKH PISPAIFFAG NRSYSSVLQA 60 NIRNLRFNIS STPKPFLIIA ATHESHVQAA VTCGKRHNLQ MKIRSGGHDY DGLSYVTYSR 120 KPFFVLDMFN LRSVDVDVAS KTAWVQTGAI LGEVYYYIWE KSKTLAYPAG ICPTVGVGGH 180 ISGGGYGNMM RKYGLTVDNT IDARMVDVNG KILDRKLMGE DLYWAINGGG GGSYGVVLAY 240 KINLVEVPEN VTVFRISRTL EQNATEIVNR WQRVAPELPD ELFIRTVIDV VNSTVSSQKT 300 VRATFIAMFL GDTTTLLSIL NRRFPELGLV RSDCTETSWI QSVLFWTNIQ VGSSEKLLLQ 360 RNQPVNYLKR KSDYVREPIS RIGLESIWKK MIELEIPTMA FNPYGGAMGR ISSTVTPFPY 420 RAGNLWKIQY AANWREDRLT DRYMELTRKL YQFMTPFVSK NPRQSFFNYR DVDLGINSHN 480 GKMSSYVEGK RYGKKYFAGN FERLVKIKTR VDRGNFFRNE QSIPVLP* 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG0277 | GlcD | 5.0e-9 | 75 | 273 | 211 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam08031 | BBE | 3.0e-14 | 465 | 524 | 60 | + 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-20 | 75 | 214 | 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. |
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 |
EMBL | CAN80091.1 | 0 | 16 | 527 | 22 | 530 | hypothetical protein [Vitis vinifera] |
RefSeq | NP_174357.1 | 0 | 1 | 527 | 1 | 527 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
RefSeq | XP_002269462.1 | 0 | 16 | 527 | 22 | 530 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002523151.1 | 0 | 18 | 527 | 27 | 537 | Reticuline oxidase precursor, putative [Ricinus communis] |
RefSeq | XP_002523152.1 | 0 | 23 | 527 | 7 | 509 | 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 | 28 | 526 | 13 | 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 | 28 | 526 | 13 | 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 | 23 | 526 | 6 | 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 | 23 | 526 | 6 | 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 | 3tsh_A | 0 | 23 | 526 | 6 | 496 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |