| Basic Information | |
|---|---|
| Species | Thellungiella halophila |
| Cazyme ID | Thhalv10016496m |
| Family | AA7 |
| Protein Properties | Length: 535 Molecular Weight: 59668.4 Isoelectric Point: 7.3223 |
| Chromosome | Chromosome/Scaffold: 10 Start: 7921050 End: 7923531 |
| Description | FAD-binding Berberine family protein |
| View CDS | |
| External Links |
|---|
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA7 | 73 | 309 | 0 |
| NLRYLTPSNPKPVFIFEPLYETHVQAAVVCAKKLQLHLRVRSGGHDYEGLSFVSENETPFVIVDLSKLRQIDVDLDSNSAWAHAGATIGEVYYRIQEKSQ THGFPAGLCSSLGVGGHLVGGAYGSMMRKFGLGADNVLDARIVDANGKILDRAAMGEDVFWAIRGGGGGSFGVILAWKIKLVPVPAIVTVFTVTKTLEQD GTKVLYKWQQVADKLDEDLFIRVIIQTAGKTTKTGNR | |||
| Full Sequence |
|---|
| Protein Sequence Length: 535 Download |
| MAFAVSKRNA IMAFLVTLLL VVSVPLSSST LQQDFMQCLV DNSDISFPIT ASFFSPDQNA 60 TLFKEELEST AQNLRYLTPS NPKPVFIFEP LYETHVQAAV VCAKKLQLHL RVRSGGHDYE 120 GLSFVSENET PFVIVDLSKL RQIDVDLDSN SAWAHAGATI GEVYYRIQEK SQTHGFPAGL 180 CSSLGVGGHL VGGAYGSMMR KFGLGADNVL DARIVDANGK ILDRAAMGED VFWAIRGGGG 240 GSFGVILAWK IKLVPVPAIV TVFTVTKTLE QDGTKVLYKW QQVADKLDED LFIRVIIQTA 300 GKTTKTGNRT ISTSYQGQFL GDSNRLLQVM QKSFPELGLT KKDCVEMSWI KSVMYIAGFP 360 NSAAPEALLD GKSLFKNHFK AKSDFVKEPI PVEGLEGLWK KLLQEDSPLT IWNPYGGMMA 420 RIAESEIPFP HRNGTLFKIQ WLTTWSDGKA SEAKHMKWMR EMYSYMEKYV SKNPRAAYVN 480 YRDLDLGVNE EESDAREWGS KYFKGNFERL VKIKGEFDPE NLFRHEQSIP TKIG* 540 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG0277 | GlcD | 5.0e-16 | 96 | 532 | 452 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam01565 | FAD_binding_4 | 2.0e-18 | 84 | 223 | 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. | ||
| pfam08031 | BBE | 2.0e-19 | 477 | 530 | 54 | + 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 | |
|---|---|
| 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 |
| RefSeq | NP_174363.1 | 0 | 29 | 533 | 29 | 533 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
| RefSeq | NP_181025.1 | 0 | 1 | 534 | 1 | 532 | MEE23 (MATERNAL EFFECT EMBRYO ARREST 23); FAD binding / catalytic/ electron carrier/ oxidoreductase [Arabidopsis thaliana] |
| RefSeq | XP_002268361.1 | 0 | 9 | 530 | 5 | 525 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002523162.1 | 0 | 35 | 530 | 33 | 529 | Reticuline oxidase precursor, putative [Ricinus communis] |
| RefSeq | XP_002523164.1 | 0 | 35 | 530 | 33 | 529 | 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 | 530 | 4 | 511 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 4dns_B | 0 | 25 | 530 | 3 | 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 | 25 | 530 | 3 | 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 | 32 | 533 | 8 | 497 | 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 | 32 | 533 | 8 | 497 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
