y
Basic Information | |
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Species | Mimulus guttatus |
Cazyme ID | mgv1a001246m |
Family | GH13 |
Protein Properties | Length: 855 Molecular Weight: 94837.5 Isoelectric Point: 5.717 |
Chromosome | Chromosome/Scaffold: 16 Start: 1226280 End: 1232647 |
Description | limit dextrinase |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 271 | 661 | 1.3e-25 |
DSAGILHLKKLSSAGITHIHLLPTYQFAGVDDKKAKWQSVDFEMLESFPPDSDEQQASITAIQNEDGFNWGYNPVLWGVPKGSYATKPSGSSRIIEFRKM VQALNRIGLRVVLDVVYNHLHASGPNGDDSVLDKIVPGYYLRRNLDGLIENSTCTNNTASEHSMVERLIIDDLLHWAINYKVKARSVLQSLSKQNDGVDG SSIYIYGEGWDFAEVANDGRGVNASQFNLCGTEIGSFNDRIRDAMIGGSPFGHPLQQGFITGLSLEPNDHDHGSNSDVEHTLAVSKDRIQVAMAANLKDF VLTNHEGKEVKGSEISMHDGAPLAYASSPIETVNYVSAHDNETLFDIVSLKTPLNISVDSRCRMNHLATSVIALSQGIPFFHAGDEILRSK |
Full Sequence |
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Protein Sequence Length: 855 Download |
MSYSRAFWVS KETIAWNVDA GNGSYFLFGS KNATLAVVNG EIQGYDVKIE LEQSSETLPK 60 HVIERFPHIR DFKPLQVPRD LDAKNLLKYR LAVAILGSGG ECTSITGLQL PGILDELFYY 120 SGPLGAVFSS EAVSLYLWAP TAQKVNVLIY GEGEGGDHLE IVPLEESNGV WSAKGPLTWE 180 GCYYVYEVYV YHHSTSRIEK CTANDPYARG LSADGRRTLL VNIDSEALKP ESWDRLVDEK 240 RDLCFVFRHH ATDDTVPSDF RGGYLAFTSE DSAGILHLKK LSSAGITHIH LLPTYQFAGV 300 DDKKAKWQSV DFEMLESFPP DSDEQQASIT AIQNEDGFNW GYNPVLWGVP KGSYATKPSG 360 SSRIIEFRKM VQALNRIGLR VVLDVVYNHL HASGPNGDDS VLDKIVPGYY LRRNLDGLIE 420 NSTCTNNTAS EHSMVERLII DDLLHWAINY KVKARSVLQS LSKQNDGVDG SSIYIYGEGW 480 DFAEVANDGR GVNASQFNLC GTEIGSFNDR IRDAMIGGSP FGHPLQQGFI TGLSLEPNDH 540 DHGSNSDVEH TLAVSKDRIQ VAMAANLKDF VLTNHEGKEV KGSEISMHDG APLAYASSPI 600 ETVNYVSAHD NETLFDIVSL KTPLNISVDS RCRMNHLATS VIALSQGIPF FHAGDEILRS 660 KSLDRDSYNS GDWFNRLDFS YNLNNWGVGL PPREKNERHW PLMKTRLADP SFKPRRSHIL 720 AALESFCCFI SIRYSSPLFR LSTANAIQER VRFHNTGPSW VPGVIVMSIE DGHEGVPGLS 780 QLDPTYSYIV VIINASPNDI TFTSPSLRGK RLQLHPIQMN SGDEIVKGSN YDNSSGSFSI 840 PFRTTSVFVE PRPI* 900 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam11852 | DUF3372 | 1.0e-79 | 680 | 852 | 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 | 1.0e-109 | 115 | 806 | 724 | + 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 | 5.0e-140 | 253 | 685 | 460 | + 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 | 1 | 852 | 879 | + alpha-amylase/limit dextrinase | ||
TIGR02103 | pullul_strch | 0 | 1 | 852 | 907 | + 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 - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CAA58803.1 | 0 | 1 | 854 | 84 | 964 | pullulanase [Spinacia oleracea] |
EMBL | CBI31395.1 | 0 | 3 | 854 | 78 | 956 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002271820.1 | 0 | 3 | 854 | 29 | 907 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002315334.1 | 0 | 3 | 852 | 16 | 893 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002532780.1 | 0 | 3 | 852 | 87 | 964 | pullulanase, 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 | 4aio_A | 0 | 1 | 852 | 3 | 883 | A Chain A, The Structure Of Soybean Peroxidase |
PDB | 2y5e_A | 0 | 1 | 852 | 3 | 883 | A Chain A, The Structure Of Soybean Peroxidase |
PDB | 2y4s_A | 0 | 1 | 852 | 3 | 883 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
PDB | 2fhf_A | 0 | 1 | 852 | 174 | 1070 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
PDB | 2fhc_A | 0 | 1 | 852 | 174 | 1070 | 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 |
GR088431 | 247 | 303 | 532 | 0 |
EH773847 | 282 | 509 | 790 | 0 |
GO872243 | 341 | 478 | 818 | 0 |
AM733410 | 287 | 529 | 815 | 0 |
BQ509860 | 263 | 504 | 766 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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