y
Basic Information | |
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Species | Arabidopsis lyrata |
Cazyme ID | 917159 |
Family | AA7 |
Protein Properties | Length: 478 Molecular Weight: 54065.7 Isoelectric Point: 6.8569 |
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 | 38 | 140 | 2.2e-34 |
PKPVSIITPVKASDVQTVIRCARLHGIHVRTRSAGHCYEGLSYIAYNKPFVVIDIRNLQSISLDVDNRTGWVQTGATAGELYYEIGKTPKTLAFPAGIHP TVA | |||
AA7 | 140 | 470 | 5.49996e-41 |
AADNIIDALVVDASGRILDRQAMGEEYYFWAICGGGGSSFGIILSWKIKLVDVPSTITVFKVKRTSKKEAVRIINKWQYVADKVPDDLFIRTTLERSNKN AVHALFTGLYLGPANNLLALMEEKFPELGLEKDGCTEMSWVESVLWFADFHKGESLDDVLTNRERTSLSYKGKDDFVQEPIPEAAIQELWRRLDAPEARL AKIILTPFGGKMSEIAEHETLFPHREGNLYEIQYVAYWREEEDKNMTGTNKYLKWVDSVYELMTPYVSKSPRGAYVNFVDMDLGMYLGKKKTKYEEGKSW GVKYFKNNFERLVRVKTSVDPTDFFCDEQSI |
Full Sequence |
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Protein Sequence Length: 478 Download |
MNHNTVESKV IHTSKDSSFF SILDSSIQNP RFSVSETPKP VSIITPVKAS DVQTVIRCAR 60 LHGIHVRTRS AGHCYEGLSY IAYNKPFVVI DIRNLQSISL DVDNRTGWVQ TGATAGELYY 120 EIGKTPKTLA FPAGIHPTVA ADNIIDALVV DASGRILDRQ AMGEEYYFWA ICGGGGSSFG 180 IILSWKIKLV DVPSTITVFK VKRTSKKEAV RIINKWQYVA DKVPDDLFIR TTLERSNKNA 240 VHALFTGLYL GPANNLLALM EEKFPELGLE KDGCTEMSWV ESVLWFADFH KGESLDDVLT 300 NRERTSLSYK GKDDFVQEPI PEAAIQELWR RLDAPEARLA KIILTPFGGK MSEIAEHETL 360 FPHREGNLYE IQYVAYWREE EDKNMTGTNK YLKWVDSVYE LMTPYVSKSP RGAYVNFVDM 420 DLGMYLGKKK TKYEEGKSWG VKYFKNNFER LVRVKTSVDP TDFFCDEQSI PLLNKVT* 480 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG0277 | GlcD | 5.0e-8 | 40 | 334 | 328 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 7.0e-14 | 40 | 158 | 140 | + 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. | ||
pfam08031 | BBE | 6.0e-15 | 413 | 471 | 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. |
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 | AAO29955.1 | 0 | 1 | 477 | 1 | 495 | berberine bridge enzyme-like protein [Arabidopsis thaliana] |
DDBJ | BAE99575.1 | 0 | 4 | 477 | 24 | 511 | berberine bridge enzyme-like protein [Arabidopsis thaliana] |
RefSeq | NP_193814.1 | 0 | 1 | 471 | 45 | 524 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
RefSeq | NP_199254.1 | 0 | 4 | 477 | 46 | 533 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
RefSeq | NP_199257.1 | 0 | 1 | 477 | 39 | 533 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
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 | 3 | 473 | 17 | 513 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 4dns_B | 0 | 6 | 473 | 21 | 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 | 6 | 473 | 21 | 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 | 6 | 475 | 19 | 498 | 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 | 6 | 475 | 19 | 498 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO777438 | 496 | 8 | 474 | 0 |
EV546313 | 245 | 234 | 476 | 0 |
EG510444 | 196 | 281 | 476 | 0 |
EG510445 | 144 | 204 | 347 | 0 |
EG510445 | 157 | 72 | 208 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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