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Basic Information | |
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Species | Fragaria vesca |
Cazyme ID | mrna23425.1-v1.0-hybrid |
Family | GH13 |
Protein Properties | Length: 950 Molecular Weight: 105009 Isoelectric Point: 5.9695 |
Chromosome | Chromosome/Scaffold: 7 Start: 13640874 End: 13650745 |
Description | limit dextrinase |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 357 | 754 | 2.9e-26 |
DSAGVSHLKKLSKAGMTHVHLLPAFQFSGVDDEKENWKSIAAELLVASCVYDIWPDSKILEKFPSDSSEQQALITAIQNDDGYNWGYNPVLWGVPKGSYA SNANGSYRAREFRKMVQALNRLGLRVVLDVVYNHLHGSGPFDANSVLDKVMIVPGYYLRRNTDGFIENSTCVNNTASEHFMVERLILDDLLHWAVDYKVD GFRFDLMGHMMKRTMVKAKDALCSLTKDRDGVDGSSIYIYGEGWDFGEVANNGRGVNASQFNICGTGIGSFNDRIRDAILGGSPFGHPLQQGFVTGLLLQ PNGYDHGPEAVAERMLAEAKDHIQVGMAANLRDFVLTNCEGKEVKGSEVLTYGGTSVAYALDPTETVNYASAHDNETLFDIVSLKGIPFFHCGDEILR |
Full Sequence |
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Protein Sequence Length: 950 Download |
MGIYTCSLLL PPPTVNSHFP NHIRHAFSSS SIRCRFTSHP KPKPIFSFPP TSANFSRLQC 60 SASLPMSAQQ DSASTSPSQV EGSLLKSRAF WVSESIIAWN VDTGDDSCYL FASKTAALSL 120 TGDGVSGEDV KVELREDRHG LPQNVKEKFP HIKDYRAFNV PSDLDVKSLL KAQLAVATFS 180 CDGRCSDATG LQLPGILDEL FSYEGPLGAV FSKEAVSLYL WAPTSQEPLG GNPLEIVQLE 240 EVNGVWSTRG PKSWEGCYYV YEVSVYHPST LQIEKCYAND PYARGRLSSD GRRTLFINLD 300 SDSIKPDGWD KLVDEKPDIL SSSDISIYEL HIRDFSANDQ TVLPEFRGGY LAFTSQDSAG 360 VSHLKKLSKA GMTHVHLLPA FQFSGVDDEK ENWKSIAAEL LVASCVYDIW PDSKILEKFP 420 SDSSEQQALI TAIQNDDGYN WGYNPVLWGV PKGSYASNAN GSYRAREFRK MVQALNRLGL 480 RVVLDVVYNH LHGSGPFDAN SVLDKVMIVP GYYLRRNTDG FIENSTCVNN TASEHFMVER 540 LILDDLLHWA VDYKVDGFRF DLMGHMMKRT MVKAKDALCS LTKDRDGVDG SSIYIYGEGW 600 DFGEVANNGR GVNASQFNIC GTGIGSFNDR IRDAILGGSP FGHPLQQGFV TGLLLQPNGY 660 DHGPEAVAER MLAEAKDHIQ VGMAANLRDF VLTNCEGKEV KGSEVLTYGG TSVAYALDPT 720 ETVNYASAHD NETLFDIVSL KGIPFFHCGD EILRSKSLDR DSYNSGDWFN RIDFTYNSNN 780 WGVGLPPKEK NEKSWPLMKP RLAEPSFKPQ KSHIHAAVEN FSDLLHIRYS SPLFRLRTAN 840 AIQERLRFHN TGPSSVPGLI LMSIEDGHEG LPGLSQLDPI YSYIVVIVNA RPTEVSFTSS 900 SIRGRALQLH PVQVKSNDEI VKKSTYDTGS ACFTVPARTT SVFVEPRGV* 960 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam11852 | DUF3372 | 4.0e-80 | 775 | 947 | 173 | + Domain of unknown function (DUF3372). This domain is functionally uncharacterized. This domain is found in bacteria and eukaryotes. This presumed domain is about 170 amino acids in length. | ||
TIGR02104 | pulA_typeI | 8.0e-118 | 198 | 898 | 749 | + pullulanase, type I. 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 consists of pullulanases related to the subfamilies described in TIGR02102 and TIGR02103 but having a different domain architecture with shorter sequences. Members are called type I pullulanases. | ||
cd11341 | AmyAc_Pullulanase_LD-like | 2.0e-153 | 324 | 780 | 491 | + Alpha amylase catalytic domain found in Pullulanase (also called dextrinase; alpha-dextrin endo-1,6-alpha glucosidase), limit dextrinase, and related proteins. Pullulanase is an enzyme with action similar to that of isoamylase; it cleaves 1,6-alpha-glucosidic linkages in pullulan, amylopectin, and glycogen, and in alpha-and beta-amylase limit-dextrins of amylopectin and glycogen. Pullulanases are very similar to limit dextrinases, although they differ in their action on glycogen and the rate of hydrolysis of limit dextrins. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase. | ||
PLN02877 | PLN02877 | 0 | 9 | 947 | 982 | + alpha-amylase/limit dextrinase | ||
TIGR02103 | pullul_strch | 0 | 84 | 947 | 917 | + 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]. |
Gene Ontology | |
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GO Term | Description |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0005975 | carbohydrate metabolic process |
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 | 0 | 87 | 947 | 6 | 883 | A Chain A, Endopolygalacturonase From The Phytopathogenic Fungus Fusarium Moniliforme |
PDB | 2y5e_A | 0 | 87 | 947 | 6 | 883 | A Chain A, Endopolygalacturonase From The Phytopathogenic Fungus Fusarium Moniliforme |
PDB | 2y4s_A | 0 | 87 | 947 | 6 | 883 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
PDB | 2fhf_A | 0 | 89 | 948 | 179 | 1071 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
PDB | 2fhc_A | 0 | 89 | 948 | 179 | 1071 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
Sequence Alignments (This image is cropped. Click for full image.) |
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