Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 1257 |
Family | AA7 |
Protein Properties | Length: 535 Molecular Weight: 56899.5 Isoelectric Point: 7.7388 |
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 | 101 | 279 | 7.20267e-43 |
SSISQVQAAIHFARQHFLRIVVKSTGHDYLGRSFARGSLSIWTHNLKSIQFSEEFVEEGCDPHSSGASAVEVGAGVQWRELYTAAHAQGKLVVGALSSSV ATAGGYVQGGGHSPAAYGLAADNVLQFTIVTPGGTVRYANRCVNRDLFWALRGGGGGTFGVVTAAVHRTFPAPSNILSA |
Full Sequence |
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Protein Sequence Length: 535 Download |
RCRCTADQSC FPNAKHWERF NLTVGGALIQ VRPPASPCYD ADGTAQCATA RANWHDSAWR 60 STQVEHPNWE AYGTQSCPLP PNGTALPSAS SCSQVLAVNV SSISQVQAAI HFARQHFLRI 120 VVKSTGHDYL GRSFARGSLS IWTHNLKSIQ FSEEFVEEGC DPHSSGASAV EVGAGVQWRE 180 LYTAAHAQGK LVVGALSSSV ATAGGYVQGG GHSPAAYGLA ADNVLQFTIV TPGGTVRYAN 240 RCVNRDLFWA LRGGGGGTFG VVTAAVHRTF PAPSNILSAV HVLAASGVGS YRQLIGQFTQ 300 LSAALYRQGW AGYFVMGGTS LTLRYHALNQ TTAFHDQSFG SFLEWIARHN ATVRAVGGGV 360 RSYPSFLEWY NDTMCSFYPS ARGICNDDLG TNRVLISRLV PASAIESSGG EISDALVTLL 420 QSNATSNAIL GVAVSGGAAV AGAGDAVAVN PAWRQASPSS SSPSSLDSPA IGASIRERMD 480 RLTAANAQLR DLTPGSWAYF NEADYNEPDW QQSLFGNNYQ RLLTVKTQVD PRGLL 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam08031 | BBE | 1.0e-9 | 498 | 534 | 37 | + 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-11 | 96 | 280 | 192 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 7.0e-18 | 98 | 237 | 143 | + 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 - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3tsj_B | 0.00000000001 | 88 | 276 | 47 | 229 | A Chain A, Structure Of The Gh47 Processing Alpha-1,2-mannosidase From Caulobacter Strain K31 |
PDB | 3tsj_A | 0.00000000001 | 88 | 276 | 47 | 229 | A Chain A, Structure Of The Gh47 Processing Alpha-1,2-mannosidase From Caulobacter Strain K31 |
PDB | 3tsh_A | 0.00000000001 | 88 | 276 | 47 | 229 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
PDB | 2bvh_D | 0.0000000001 | 102 | 305 | 47 | 234 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
PDB | 2bvh_C | 0.0000000001 | 102 | 305 | 47 | 234 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
Sequence Alignments (This image is cropped. Click for full image.) |
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