Basic Information | |
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Species | Picea abies |
Cazyme ID | MA_186285g0010 |
Family | AA7 |
Protein Properties | Length: 501 Molecular Weight: 55835.4 Isoelectric Point: 7.5466 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA7 | 45 | 497 | 0 |
QNLRYTESSVRKPYVLIVPQSKQQVQKTVACCIEHGWEIRVRSGGHSYEGLSSTSDIPFVIIDLMNLDAINIDMASKTAWVEAGATVGQLYDAIADRTAI YGFPAGVCTTMGTGGHFSGGGLSLLSRKHGIAADNIIDALFVDASGNLLNRQKMGEDVFWALRGGGGGSWGVVVAWRIKLVSVPSVVTVFNVYRTGREAV TKLVNQWQSIAPAVEEDLFIRVVISGTQLNGGQRDVKLTFNGMYLGPLHQLLETVNKSFPEMGMVSGDCKETSWIDSISYTAYTNRTELRNRYNSNKNYF KAKSDVVKTPIPASALEGAWKFLEEELSSYVIFYPLGGIMDQIPSSEIAFPHRAGNLYLIQYQVTWNDPSKDAEYIARIRGLYEYMTPYVSNSPRASYVN YLDLDLGVAPNGTATVEEARSWGEKYFVHNYDRLVKIKSTIDPYNVFRNSQSI |
Full Sequence |
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Protein Sequence Length: 501 Download |
MLFSFLSAGV GCRISTRWAH IMPDEKFYYS SSSSEYYKLL NFSVQNLRYT ESSVRKPYVL 60 IVPQSKQQVQ KTVACCIEHG WEIRVRSGGH SYEGLSSTSD IPFVIIDLMN LDAINIDMAS 120 KTAWVEAGAT VGQLYDAIAD RTAIYGFPAG VCTTMGTGGH FSGGGLSLLS RKHGIAADNI 180 IDALFVDASG NLLNRQKMGE DVFWALRGGG GGSWGVVVAW RIKLVSVPSV VTVFNVYRTG 240 REAVTKLVNQ WQSIAPAVEE DLFIRVVISG TQLNGGQRDV KLTFNGMYLG PLHQLLETVN 300 KSFPEMGMVS GDCKETSWID SISYTAYTNR TELRNRYNSN KNYFKAKSDV VKTPIPASAL 360 EGAWKFLEEE LSSYVIFYPL GGIMDQIPSS EIAFPHRAGN LYLIQYQVTW NDPSKDAEYI 420 ARIRGLYEYM TPYVSNSPRA SYVNYLDLDL GVAPNGTATV EEARSWGEKY FVHNYDRLVK 480 IKSTIDPYNV FRNSQSIPVN K |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02465 | PLN02465 | 0.009 | 63 | 140 | 79 | + L-galactono-1,4-lactone dehydrogenase | ||
pfam08031 | BBE | 1.0e-14 | 441 | 498 | 58 | + 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. | ||
COG0277 | GlcD | 3.0e-18 | 55 | 498 | 466 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 1.0e-21 | 57 | 194 | 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 | 1 | 498 | 11 | 525 | hypothetical protein [Vitis vinifera] |
RefSeq | XP_002264336.1 | 0 | 31 | 498 | 51 | 532 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002268361.1 | 0 | 1 | 498 | 11 | 525 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002277310.1 | 0 | 23 | 498 | 46 | 529 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002317089.1 | 0 | 22 | 498 | 43 | 527 | predicted protein [Populus trichocarpa] |
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 | 24 | 498 | 21 | 511 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3fw9_A | 0 | 28 | 498 | 17 | 492 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Scoulerine |
PDB | 4ec3_A | 0 | 28 | 498 | 23 | 498 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |
PDB | 3gsy_A | 0 | 28 | 498 | 23 | 498 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
PDB | 3d2j_A | 0 | 28 | 498 | 42 | 517 | 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 |
CO485022 | 244 | 258 | 501 | 0 |
DT634895 | 280 | 219 | 497 | 0 |
CO481591 | 253 | 250 | 501 | 0 |
DR476420 | 231 | 272 | 501 | 0 |
GW745828 | 230 | 273 | 501 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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