Basic Information | |
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Species | Cucumis sativus |
Cazyme ID | Cucsa.048450.1 |
Family | AA7 |
Protein Properties | Length: 531 Molecular Weight: 58928.5 Isoelectric Point: 8.7689 |
Chromosome | Chromosome/Scaffold: 00542 Start: 3172609 End: 3174659 |
Description | FAD-binding Berberine family protein |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA7 | 65 | 524 | 0 |
NARFNTSSAPKPVIIVTPLTESHVQSAVICSKKLGIQLKIRSGGHDYEGVSYISDVEFIILDMSNLRTVTVDVADQSAWVGAGATLGEVYYRIWEKSKVL GYPAGVCPTVGVGGHISGGGYGNMLRKYGLAVDHVLDARIVDVKGRILDSKSMGEDLFWAIKGGGGASFGVVLAYKIRLVPVPETVTIFRVERTIEQNAA DLVVRWQEVAPTTDENLFMRLLLQPVSSKIKKGTRTIRASVVALFLGKSEELVSLLKKELPELGLQKENCTEMSWIDSVLWWGNFDIGTSPEALLDRNVD SAGFLRRKSDYVQKPISRDGLNWLYKKMIEIGKTGLVFNPYGGKMSEISSTATPFPHRAGNLYKIQYSVNWNEPGPEADQEFVKQIRRLYSFMTPFVSKN PRQSFLNYRDLDIGINNNDKNSFEDGKVYGFKYFGENFERLVKVKTAVDPENFFWNEQSI |
Full Sequence |
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Protein Sequence Length: 531 Download |
MFPLIPLLCL LLLPFSAPTA AADSVYSTFL HCFQSNSNSS AGVSSIVFAR ENASYTSVLR 60 AYIRNARFNT SSAPKPVIIV TPLTESHVQS AVICSKKLGI QLKIRSGGHD YEGVSYISDV 120 EFIILDMSNL RTVTVDVADQ SAWVGAGATL GEVYYRIWEK SKVLGYPAGV CPTVGVGGHI 180 SGGGYGNMLR KYGLAVDHVL DARIVDVKGR ILDSKSMGED LFWAIKGGGG ASFGVVLAYK 240 IRLVPVPETV TIFRVERTIE QNAADLVVRW QEVAPTTDEN LFMRLLLQPV SSKIKKGTRT 300 IRASVVALFL GKSEELVSLL KKELPELGLQ KENCTEMSWI DSVLWWGNFD IGTSPEALLD 360 RNVDSAGFLR RKSDYVQKPI SRDGLNWLYK KMIEIGKTGL VFNPYGGKMS EISSTATPFP 420 HRAGNLYKIQ YSVNWNEPGP EADQEFVKQI RRLYSFMTPF VSKNPRQSFL NYRDLDIGIN 480 NNDKNSFEDG KVYGFKYFGE NFERLVKVKT AVDPENFFWN EQSIPTHSIG * 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam08031 | BBE | 6.0e-17 | 468 | 525 | 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. | ||
pfam01565 | FAD_binding_4 | 4.0e-21 | 76 | 213 | 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. | ||
COG0277 | GlcD | 2.0e-22 | 57 | 526 | 483 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] |
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 |
RefSeq | XP_002268606.1 | 0 | 21 | 525 | 30 | 529 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002299028.1 | 0 | 4 | 526 | 6 | 531 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002317087.1 | 0 | 15 | 526 | 23 | 530 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002523157.1 | 0 | 24 | 528 | 35 | 536 | Reticuline oxidase precursor, putative [Ricinus communis] |
RefSeq | XP_002523158.1 | 0 | 24 | 528 | 35 | 536 | 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 | 525 | 7 | 511 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 4dns_B | 0 | 17 | 525 | 1 | 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 | 17 | 525 | 1 | 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 | 15 | 525 | 2 | 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 | 15 | 525 | 2 | 494 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |