Basic Information | |
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Species | Picea abies |
Cazyme ID | MA_26891g0010 |
Family | AA7 |
Protein Properties | Length: 502 Molecular Weight: 55647.2 Isoelectric Point: 8.0904 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA7 | 45 | 495 | 0 |
QNLRYTESGVRKPNVVIVPGSSEQVQKSVGCCIRVRSGGHSYEGLSSTSDVPFVIIDLMNLDAINIDLPSKTAWVEGGATLGQLYFAIAQKTANYGFPEG VCPTIGTGGHFSGGGFGLLSRKYGLSADNIIDALLVDARGNLLNRQKMGEDVFWALRGGGGGSWGIVVSWRIKLVAVPPVVTVFNVARPGRDAVTKLVHR WQSVAPSVEENLFIRVFVSGTQLKGGQRDVMLTFNGMYLGPRHQLLQSVNQSFPDLAMVSADCKETSWIDSISYIGSTSTTQLSNRFNYRKNYFKAKSDF VKAPIPASALKGAWKFLEEELNGILFFDPLGGRNDQIKPSQIPFPHRAGNLYFIQYFVSWQREASAKPDTEYIAWLRRLYEYMTPYVSSSPRASYVNYVD LDLGEAPTEGSTTVEEAKSWGHKYFLQNYDRLVRAKTTIDPRNIFRNAQSI |
Full Sequence |
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Protein Sequence Length: 502 Download |
MLMTFTVQED DSALISCLEA NAITNFTTSS SCSQDFYSLL NFSLQNLRYT ESGVRKPNVV 60 IVPGSSEQVQ KSVGCCIRVR SGGHSYEGLS STSDVPFVII DLMNLDAINI DLPSKTAWVE 120 GGATLGQLYF AIAQKTANYG FPEGVCPTIG TGGHFSGGGF GLLSRKYGLS ADNIIDALLV 180 DARGNLLNRQ KMGEDVFWAL RGGGGGSWGI VVSWRIKLVA VPPVVTVFNV ARPGRDAVTK 240 LVHRWQSVAP SVEENLFIRV FVSGTQLKGG QRDVMLTFNG MYLGPRHQLL QSVNQSFPDL 300 AMVSADCKET SWIDSISYIG STSTTQLSNR FNYRKNYFKA KSDFVKAPIP ASALKGAWKF 360 LEEELNGILF FDPLGGRNDQ IKPSQIPFPH RAGNLYFIQY FVSWQREASA KPDTEYIAWL 420 RRLYEYMTPY VSSSPRASYV NYVDLDLGEA PTEGSTTVEE AKSWGHKYFL QNYDRLVRAK 480 TTIDPRNIFR NAQSIPPATF ME |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG0277 | GlcD | 3.0e-13 | 55 | 498 | 469 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam08031 | BBE | 2.0e-15 | 438 | 496 | 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. | ||
pfam01565 | FAD_binding_4 | 3.0e-19 | 57 | 188 | 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. |
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 | CAN81654.1 | 0 | 24 | 497 | 46 | 526 | hypothetical protein [Vitis vinifera] |
RefSeq | XP_002264336.1 | 0 | 9 | 497 | 26 | 533 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002277281.1 | 0 | 14 | 496 | 31 | 526 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002277310.1 | 0 | 36 | 497 | 59 | 530 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002533924.1 | 0 | 16 | 497 | 33 | 534 | 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 | 3fw9_A | 0 | 14 | 497 | 2 | 493 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Scoulerine |
PDB | 4ec3_A | 0 | 9 | 497 | 3 | 499 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |
PDB | 3gsy_A | 0 | 9 | 497 | 3 | 499 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
PDB | 3d2j_A | 0 | 1 | 497 | 14 | 518 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
PDB | 3d2h_A | 0 | 1 | 497 | 14 | 518 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
DT634895 | 281 | 216 | 495 | 0 |
CO485022 | 245 | 252 | 496 | 0 |
GE476590 | 287 | 13 | 293 | 0 |
CO481591 | 255 | 244 | 496 | 0 |
HO777438 | 499 | 21 | 502 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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