Basic Information | |
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Species | Picea abies |
Cazyme ID | MA_10429723g0010 |
Family | CBM41 |
Protein Properties | Length: 313 Molecular Weight: 35016.9 Isoelectric Point: 8.8343 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CBM41 | 82 | 173 | 5.8e-23 |
MRIHYNRKDRKYENWGLHVWGDVNVHTFWEKPLYATGSDGFGLYWDVQVKPNGVLSFVIHKGEIKDFSGSILIGHADVWVMSECSTVFTEKP |
Full Sequence |
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Protein Sequence Length: 313 Download |
MAAVPCSSSP VLVPQEKRPF QASRGVLSGF LYQGNRATVF KKEWDRGSSV TDSRSRKLGV 60 ICGTSMQDAA SQFGEPPEFT VMRIHYNRKD RKYENWGLHV WGDVNVHTFW EKPLYATGSD 120 GFGLYWDVQV KPNGVLSFVI HKGEIKDFSG SILIGHADVW VMSECSTVFT EKPDLDSMPK 180 GNLSFARAYW VSQNLLAWNM EIEHAQFYMF ASKNANLNLS AGGVKGEDLV IRLEEEQGRL 240 PTKVIEKFPH IAHYKALKLP VGVDTKDLVK SQLVIACIDG RGDEGMGFGD GWKVPPKLQR 300 MEGRAQQKNT KGN |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR02102 | pullulan_Gpos | 0.0002 | 73 | 133 | 63 | + pullulanase, extracellular, Gram-positive. Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. In contrast, a glycogen debranching enzyme such GlgX, homologous to this family, can release glucose at alpha,1-6 linkages from glycogen first subjected to limit degradation by phosphorylase. Characterized members of this family include a surface-located pullulanase from Streptococcus pneumoniae (PMID:11083842) and an extracellular bifunctional amylase/pullulanase with C-terminal pullulanase activity (PMID:8798645). | ||
TIGR02103 | pullul_strch | 1.0e-20 | 183 | 277 | 96 | + alpha-1,6-glucosidases, pullulanase-type. Members of this protein family include secreted (or membrane-anchored) pullulanases of Gram-negative bacteria and pullulanase-type starch debranching enzymes of plants. Both enzymes hydrolyze alpha-1,6 glycosidic linkages. Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. This family is closely homologous to, but architecturally different from, the Gram-positive pullulanases of Gram-positive bacteria (TIGR02102) [Energy metabolism, Biosynthesis and degradation of polysaccharides]. | ||
pfam03714 | PUD | 9.0e-21 | 82 | 173 | 102 | + Bacterial pullanase-associated domain. Domain is found in pullanase - carbohydrate de-branching - proteins. It is found both to the N or the C terminii of of the alpha-amylase active site region. This domain contains several conserved aromatic residues that are suggestive of a carbohydrate binding function. | ||
cd10315 | CBM41_pullulanase | 5.0e-22 | 80 | 172 | 100 | + Family 41 Carbohydrate-Binding Module from pullulanase-like enzymes. Pullulanases (EC 3.2.1.41) are a group of starch-debranching enzymes, catalyzing the hydrolysis of the alpha-1,6-glucosidic linkages of alpha-glucans, preferentially pullulan. Pullulan is a polysaccharide in which alpha-1,4 linked maltotriosyl units are combined via an alpha-1,6 linkage. These enzymes are of importance in the starch industry, where they are used to hydrolyze amylopectin starch. Pullulanases consist of multiple distinct domains, including a catalytic domain belonging to the glycoside hydrolase (GH) family 13 and carbohydrate-binding modules (CBM), including CBM41. | ||
PLN02877 | PLN02877 | 7.0e-35 | 163 | 278 | 116 | + alpha-amylase/limit dextrinase |
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 | NP_196056.2 | 4e-26 | 183 | 301 | 85 | 201 | ATLDA (LIMIT DEXTRINASE); alpha-amylase/ limit dextrinase/ pullulanase [Arabidopsis thaliana] |
Swiss-Prot | Q8GTR4 | 4e-26 | 183 | 301 | 85 | 201 | PULA1_ARATH RecName: Full=Pullulanase 1, chloroplastic; Short=AtPU1; AltName: Full=Protein LIMIT DEXTRINASE; Short=AtLDA; Flags: Precursor |
RefSeq | XP_001415537.1 | 1e-25 | 81 | 282 | 68 | 280 | predicted protein [Ostreococcus lucimarinus CCE9901] |
RefSeq | XP_001771764.1 | 0 | 21 | 282 | 109 | 364 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | ZP_04036526.1 | 4e-31 | 69 | 282 | 132 | 351 | alpha-1,6-glucosidase, pullulanase-type [Meiothermus silvanus DSM 9946] |
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 | 4aio_A | 8e-18 | 186 | 282 | 6 | 105 | A Chain A, Arabidopsis Thaliana Peroxidase A2 |
PDB | 2y5e_A | 8e-18 | 186 | 282 | 6 | 105 | A Chain A, Arabidopsis Thaliana Peroxidase A2 |
PDB | 2y4s_A | 8e-18 | 186 | 282 | 6 | 105 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
PDB | 2fhf_A | 0.0000003 | 117 | 282 | 103 | 270 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
PDB | 2fhc_A | 0.0000003 | 117 | 282 | 103 | 270 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
EX023229 | 97 | 182 | 278 | 4e-24 |
DK473507 | 97 | 182 | 278 | 9e-24 |
DK494420 | 97 | 182 | 278 | 1e-23 |
DK498558 | 97 | 182 | 278 | 1e-23 |
DK502193 | 97 | 182 | 278 | 1e-23 |
Orthologous Group | |||||
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Species | ID | ||||
Physcomitrella patens | Pp1s142_79V6.1.101.191 |
Sequence Alignments (This image is cropped. Click for full image.) |
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