Basic Information | |
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Species | Phaseolus vulgaris |
Cazyme ID | Phvul.007G113300.1 |
Family | AA7 |
Protein Properties | Length: 551 Molecular Weight: 61412.8 Isoelectric Point: 5.6039 |
Chromosome | Chromosome/Scaffold: 07 Start: 14963499 End: 14965839 |
Description | FAD-binding Berberine family protein |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA7 | 69 | 535 | 0 |
NLRFAEPVIPKPIAIVLPGSLEQLQKSVACSRESSMEIRVRCGGHSYEGTSYVADDGTPFVIIDMMNLNHVWVDMETETAWVEGGATLGETYYAISQASN EYGFSAGSCPTVGVGGHIGGGGFGLLSRKYGLAADNVVDALLVDADQNLLDRETMGEDVFWAIRGGGGGLWGIIYAWKIQLLKVPQVVTSFTVSRTGTKS HVANLVHKWQYVAPNLEDDFYLSCFVGAGLPQAKTKGLSLTLNGFYLGPKTDAISILHHAFPELGVTEEECIEMSWIQSIVFFSGLSDGASVSDLKNRYV QEKEYFKAKSDYVKNHIPLVGIETALDILEKEPKGYVILDAYGGKMHNISNDAIAFPHRRGNLFTIQYLIYWKEADKEKSSDYVDWIRGFYDAMSPFVSS APRAAYINYMDFDLGVRKRIRSYGDVEDGVENARDWGEKYFLSNYDRLVRVKTMVDPNNVFTNEQGI |
Full Sequence |
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Protein Sequence Length: 551 Download |
MFYFLKRLCL LCFLLLSLEV SLWSCASHTD LASCLLNHNI KNFTTLPYKE HDQPSSHDYF 60 KILNFSIQNL RFAEPVIPKP IAIVLPGSLE QLQKSVACSR ESSMEIRVRC GGHSYEGTSY 120 VADDGTPFVI IDMMNLNHVW VDMETETAWV EGGATLGETY YAISQASNEY GFSAGSCPTV 180 GVGGHIGGGG FGLLSRKYGL AADNVVDALL VDADQNLLDR ETMGEDVFWA IRGGGGGLWG 240 IIYAWKIQLL KVPQVVTSFT VSRTGTKSHV ANLVHKWQYV APNLEDDFYL SCFVGAGLPQ 300 AKTKGLSLTL NGFYLGPKTD AISILHHAFP ELGVTEEECI EMSWIQSIVF FSGLSDGASV 360 SDLKNRYVQE KEYFKAKSDY VKNHIPLVGI ETALDILEKE PKGYVILDAY GGKMHNISND 420 AIAFPHRRGN LFTIQYLIYW KEADKEKSSD YVDWIRGFYD AMSPFVSSAP RAAYINYMDF 480 DLGVRKRIRS YGDVEDGVEN ARDWGEKYFL SNYDRLVRVK TMVDPNNVFT NEQGIPPLSL 540 ASPSFKAQNK * |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG0277 | GlcD | 9.0e-15 | 80 | 538 | 472 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam08031 | BBE | 6.0e-17 | 473 | 536 | 64 | + 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 | 1.0e-18 | 80 | 199 | 121 | + 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 | CBI16966.1 | 0 | 25 | 541 | 301 | 770 | unnamed protein product [Vitis vinifera] |
EMBL | CBI16966.1 | 0 | 376 | 516 | 85 | 224 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002264336.1 | 0 | 2 | 541 | 8 | 537 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002329230.1 | 0 | 25 | 548 | 11 | 536 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002533924.1 | 0 | 13 | 548 | 15 | 545 | d-lactate dehydrogenase, 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 | 3d2j_A | 0 | 12 | 539 | 7 | 520 | A Chain A, Crystal Structure Of Nxg1-Deltayniig In Complex With Xllg, A Xyloglucan Derived Oligosaccharide |
PDB | 3d2h_A | 0 | 12 | 539 | 7 | 520 | A Chain A, Crystal Structure Of Nxg1-Deltayniig In Complex With Xllg, A Xyloglucan Derived Oligosaccharide |
PDB | 3d2d_A | 0 | 12 | 539 | 7 | 520 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Reticuline |
PDB | 3fw9_A | 0 | 30 | 539 | 1 | 495 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Scoulerine |
PDB | 4ec3_A | 0 | 30 | 539 | 7 | 501 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |