y
Basic Information | |
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Species | Arabidopsis thaliana |
Cazyme ID | AT1G30720.1 |
Family | AA7 |
Protein Properties | Length: 528 Molecular Weight: 58878.6 Isoelectric Point: 9.6373 |
Chromosome | Chromosome/Scaffold: 1 Start: 10898172 End: 10899912 |
Description | reticuline oxidase-like protein precursor, putative, expressed |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA7 | 68 | 523 | 0 |
RFDKPTTPKPISVVAAATWTHIQAAVGCARELSLQVRIRSGGHDFEGLSYTSTVPFFVLDMFGFKTVDVNLTERTAWVDSGATLGELYYRISEKSNVLGF PAGLSTTLGVGGHFSGGGYGNLMRKYGLSVDNVFGSGIVDSNGNIFTDRVSMGEDRFWAIRGGGAASYGVVLGYKIQLVPVPEKVTVFKVGKTVGEGAVD LIMKWQSFAHSTDRNLFVRLTLTLVNGTKPGENTVLATFIGMYLGRSDKLLTVMNRDFPELKLKKTDCTEMRWIDSVLFWDDYPVGTPTSVLLNPLVAKK LFMKRKSDYVKRLISRTDLGLILKKLVEVEKVKMNWNPYGGRMGEIPSSRTPFPHRAGNLFNIEYIIDWSEAGDNVEKKYLALANEFYRFMTPYVSSNPR EAFLNYRDLDIGSSVKSTYQEGKIYGAKYFKENFERLVDIKTTIDAENFWKNEQSI |
Full Sequence |
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Protein Sequence Length: 528 Download |
MEKLLVISLL LLISTSVTTS QSVTDPIAFL RCLDRQPTDP TSPNSAVAYI PTNSSFTTVL 60 RSRIPNLRFD KPTTPKPISV VAAATWTHIQ AAVGCARELS LQVRIRSGGH DFEGLSYTST 120 VPFFVLDMFG FKTVDVNLTE RTAWVDSGAT LGELYYRISE KSNVLGFPAG LSTTLGVGGH 180 FSGGGYGNLM RKYGLSVDNV FGSGIVDSNG NIFTDRVSMG EDRFWAIRGG GAASYGVVLG 240 YKIQLVPVPE KVTVFKVGKT VGEGAVDLIM KWQSFAHSTD RNLFVRLTLT LVNGTKPGEN 300 TVLATFIGMY LGRSDKLLTV MNRDFPELKL KKTDCTEMRW IDSVLFWDDY PVGTPTSVLL 360 NPLVAKKLFM KRKSDYVKRL ISRTDLGLIL KKLVEVEKVK MNWNPYGGRM GEIPSSRTPF 420 PHRAGNLFNI EYIIDWSEAG DNVEKKYLAL ANEFYRFMTP YVSSNPREAF LNYRDLDIGS 480 SVKSTYQEGK IYGAKYFKEN FERLVDIKTT IDAENFWKNE QSIPVRR* 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG0277 | GlcD | 1.0e-7 | 75 | 249 | 186 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam08031 | BBE | 2.0e-13 | 469 | 524 | 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 | 4.0e-18 | 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:0003824 | catalytic activity |
GO:0008762 | UDP-N-acetylmuramate dehydrogenase activity |
GO:0009055 | electron carrier activity |
GO:0012505 | endomembrane system |
GO:0016491 | oxidoreductase activity |
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 | 28 | 524 | 31 | 527 | hypothetical protein [Vitis vinifera] |
RefSeq | NP_174359.1 | 0 | 1 | 527 | 1 | 527 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
RefSeq | NP_174360.1 | 0 | 1 | 527 | 1 | 526 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
RefSeq | XP_002317086.1 | 0 | 1 | 526 | 1 | 526 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002523155.1 | 0 | 3 | 526 | 2 | 524 | 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 | 3vte_A | 0 | 29 | 524 | 7 | 511 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 4dns_B | 0 | 29 | 524 | 13 | 494 | 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 | 29 | 524 | 13 | 494 | 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 | 29 | 524 | 11 | 494 | 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 | 29 | 524 | 11 | 494 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
cannabinoid biosynthesis | RXN-7854 | EC-1.21.3 | tetrahydrocannabinolic acid synthase |