y
Basic Information | |
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Species | Malus domestica |
Cazyme ID | MDP0000142103 |
Family | GH13 |
Protein Properties | Length: 976 Molecular Weight: 108363 Isoelectric Point: 6.0264 |
Chromosome | Chromosome/Scaffold: 013926319 Start: 7744 End: 16514 |
Description | limit dextrinase |
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 |
GH13 | 389 | 790 | 2.9e-32 |
HLKKLSNAGITHVHLLPAFQFAGVDDENENWKNVDFKILEKFAPDSDEQQALITAIQNDDGYNWGYNPVLWGVPKGSYASNANGTYRAIEFRKMVQALNR YGLRVVLDAVYNHLSESGPFSVNSVLDKIVPGYYLRRNTDGFIENSTCVNNTASEHFMVERLIVDDLLHWAVDYKVDGFRFDLMGHIMRRTMVKAKDALC SLTKERDGVDGSSIYIYGEGWDFGEVANNGRGINASQSNLRGTGIGSFNDRIRDAILGGSPFGHPLQQGFVTGLLLQPNGHDHGPESVAKHMLAESKDHI QVGMAANLRDFVLTDYEGKEVKGAEVLTYGGTPVAYTLSPTETINYVSAHDNETLFDIVALKTSMEISLEERCRINHLATSIIALGQGIPFFHAGDELLR SK |
Full Sequence |
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Protein Sequence Length: 976 Download |
MPLLYSSTFL LNRPPSTAPT TNRHFPPQRP ATCPSSSLRR RFASARKPLL PPLPLRSAGV 60 FRHPNLQCSS SSSSSVSMSA EEEPTSTSQR GEQLQSGFLY SRAFWVSESI IAWNVDVGNG 120 SCYLFVSKTA ALSCSSDGIL GEDIKVKLEE DKHGLPENVK EKFPHIKDYR AFNVPPDLDA 180 KPLLKCQLEV ATFDANGRCS DATGLQLPGI LDELFSYNGP LGALYSEESV SLYLWAPTAQ 240 EVCVCIYKEP LGGGNPQEVV QLEEVNGVWS TKGPKSWEGC YYVYEVSVYH PSTLKIEKCY 300 ANDPYARGLS SDGRRTLLVN LDSDDIKPEG WDKLAYEKPD IISFSDISIY ELHIRDFSCH 360 CSANDQTVHS EFRGGYLAFT LQDSAGAFHL KKLSNAGITH VHLLPAFQFA GVDDENENWK 420 NVDFKILEKF APDSDEQQAL ITAIQNDDGY NWGYNPVLWG VPKGSYASNA NGTYRAIEFR 480 KMVQALNRYG LRVVLDAVYN HLSESGPFSV NSVLDKIVPG YYLRRNTDGF IENSTCVNNT 540 ASEHFMVERL IVDDLLHWAV DYKVDGFRFD LMGHIMRRTM VKAKDALCSL TKERDGVDGS 600 SIYIYGEGWD FGEVANNGRG INASQSNLRG TGIGSFNDRI RDAILGGSPF GHPLQQGFVT 660 GLLLQPNGHD HGPESVAKHM LAESKDHIQV GMAANLRDFV LTDYEGKEVK GAEVLTYGGT 720 PVAYTLSPTE TINYVSAHDN ETLFDIVALK TSMEISLEER CRINHLATSI IALGQGIPFF 780 HAGDELLRSK SLDRDSYNSG DWFNRLDFTY SSNNWGVGLP PKEKNEHSWP LMKPRLADPS 840 FKPQKSHILA ALENFSNLLR IRYTSPLFRL RTANAIQERV RFHNTGPSLV PGVIVMSIED 900 GHEGVPGFSY IVVIINACPT EVSFASPPLQ SRTLQLHPVQ VTSTDEIVKR STYDASSGCF 960 TVPPRTTSVF IEPRRV 1020 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG1523 | PulA | 3.0e-91 | 220 | 972 | 823 | + Type II secretory pathway, pullulanase PulA and related glycosidases [Carbohydrate transport and metabolism] | ||
TIGR02104 | pulA_typeI | 6.0e-138 | 212 | 927 | 733 | + 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 | 9.0e-169 | 346 | 814 | 479 | + 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 | 80 | 974 | 902 | + alpha-amylase/limit dextrinase | ||
TIGR02103 | pullul_strch | 0 | 100 | 974 | 915 | + 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 | CBI31395.1 | 0 | 30 | 976 | 16 | 956 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_196056.2 | 0 | 87 | 974 | 74 | 963 | ATLDA (LIMIT DEXTRINASE); alpha-amylase/ limit dextrinase/ pullulanase [Arabidopsis thaliana] |
RefSeq | XP_002271820.1 | 0 | 94 | 976 | 23 | 907 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002315334.1 | 0 | 95 | 974 | 11 | 893 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002532780.1 | 0 | 61 | 974 | 58 | 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 | 101 | 974 | 6 | 883 | A Chain A, Crystal Structure Of A Beta-Galactosidase From Bacteroides Thetaiotaomicron |
PDB | 2y5e_A | 0 | 101 | 974 | 6 | 883 | A Chain A, Crystal Structure Of A Beta-Galactosidase From Bacteroides Thetaiotaomicron |
PDB | 2y4s_A | 0 | 101 | 974 | 6 | 883 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
PDB | 2fhf_A | 0 | 97 | 974 | 173 | 1070 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
PDB | 2fhc_A | 0 | 97 | 974 | 173 | 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 |
CO128344 | 288 | 417 | 704 | 0 |
EH773847 | 274 | 638 | 911 | 0 |
GO872243 | 341 | 607 | 940 | 0 |
DV135457 | 264 | 596 | 859 | 0 |
AM733410 | 287 | 658 | 937 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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