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Basic Information | |
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Species | Eucalyptus grandis |
Cazyme ID | Eucgr.G02746.1 |
Family | GH13 |
Protein Properties | Length: 817 Molecular Weight: 91058 Isoelectric Point: 5.5284 |
Chromosome | Chromosome/Scaffold: 7 Start: 45507850 End: 45519923 |
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 | 220 | 623 | 1e-33 |
MRHLKKLSDAGITHVHLLPTFQFAGVDDEKEKWKFVDVKKLEMLPPDSDEQQFQITAIQNEDGYNWGYNPVLWGVPKGSYASNPNGPSRTVQFRKMVQAL NKIGLRVVMDVVYNHLNASGPFDENSVLDKIVPGYYLRRNADGFIEHSTCINNTASEHFMVERLIIDDLLCWAVDYKVDGFRFDLMGHIMKRTMLRAKAA LHGLSKERDGVDGSCIYIYGEGWDFGEVAKNGRGINASQFNLGGTGIGSFNDRIRDAILGGSPFGHPLQQGFATGLFLQRNGYDHGTQAKEKLMLALSKD HIQVGMAANLRDYVFTNHEGNEVKGSEVLTYDGSPVAYALSPTETVNYVSAHDNETLFDIVSLKTPMSISVDERCRMNHLATSIIALAQGVPFFHCGDEL LRSK |
Full Sequence |
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Protein Sequence Length: 817 Download |
MLNQDKYTRP IACYELVGSE VIGLYYFSSH ETANGRCCEA TGLQLPGVLD ELFAYTGPLG 60 AVFSDEAISL YLWAPTAQTV RAFLYREPLG GDPFKIVSLE EVEGVWTAKG PKDWEGCYYV 120 YEVCVYHWTT LQVEKCYAND PYSRGLSSNG RRTLLVNLKS EALKNEEWDK LADEKPCIKS 180 FADISIYELH IRDFSANDST VSPDVRGGYE AFTLQESAGM RHLKKLSDAG ITHVHLLPTF 240 QFAGVDDEKE KWKFVDVKKL EMLPPDSDEQ QFQITAIQNE DGYNWGYNPV LWGVPKGSYA 300 SNPNGPSRTV QFRKMVQALN KIGLRVVMDV VYNHLNASGP FDENSVLDKI VPGYYLRRNA 360 DGFIEHSTCI NNTASEHFMV ERLIIDDLLC WAVDYKVDGF RFDLMGHIMK RTMLRAKAAL 420 HGLSKERDGV DGSCIYIYGE GWDFGEVAKN GRGINASQFN LGGTGIGSFN DRIRDAILGG 480 SPFGHPLQQG FATGLFLQRN GYDHGTQAKE KLMLALSKDH IQVGMAANLR DYVFTNHEGN 540 EVKGSEVLTY DGSPVAYALS PTETVNYVSA HDNETLFDIV SLKTPMSISV DERCRMNHLA 600 TSIIALAQGV PFFHCGDELL RSKSLDRDSY NSGDWFNRLD FTYNDSNWGV GLPPKEKNEK 660 NWPLIKPRLA DPSFKPQKSN ILAAVDNFLN MLRIRYSSPL FRLKTANAIQ ERVRFLNTGP 720 SQIPGVIVMS IEDGHEGVPG LTQLDPIYSY IAIVINTGPS EVSFASPALQ GKALQLHPVQ 780 VMSTDEVVKS SSFEASSVCF TIPARTTSVF IEPRNI* 840 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG1523 | PulA | 1.0e-94 | 1 | 800 | 848 | + Type II secretory pathway, pullulanase PulA and related glycosidases [Carbohydrate transport and metabolism] | ||
TIGR02104 | pulA_typeI | 6.0e-131 | 50 | 768 | 736 | + 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 | 7.0e-176 | 183 | 647 | 475 | + 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 | 33 | 814 | 782 | + alpha-amylase/limit dextrinase | ||
TIGR02103 | pullul_strch | 0 | 33 | 814 | 816 | + 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 | 32 | 816 | 172 | 956 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_196056.2 | 0 | 33 | 815 | 182 | 964 | ATLDA (LIMIT DEXTRINASE); alpha-amylase/ limit dextrinase/ pullulanase [Arabidopsis thaliana] |
RefSeq | XP_002271820.1 | 0 | 32 | 816 | 123 | 907 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002315334.1 | 0 | 33 | 814 | 112 | 893 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002532780.1 | 0 | 33 | 814 | 183 | 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 | 33 | 814 | 103 | 883 | A Chain A, Crystal Structure Of Chondroitin Polymerase From Escherichia Coli Strain K4 (K4cp) Complexed With Udp-Glcua And Udp |
PDB | 2y5e_A | 0 | 33 | 814 | 103 | 883 | A Chain A, Crystal Structure Of Chondroitin Polymerase From Escherichia Coli Strain K4 (K4cp) Complexed With Udp-Glcua And Udp |
PDB | 2y4s_A | 0 | 33 | 814 | 103 | 883 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
PDB | 2fhf_A | 0 | 15 | 814 | 255 | 1070 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
PDB | 2fhc_A | 0 | 15 | 814 | 255 | 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 | 287 | 250 | 536 | 0 |
GO872243 | 341 | 440 | 780 | 0 |
EH773847 | 282 | 471 | 752 | 0 |
DV135457 | 264 | 429 | 692 | 0 |
AM733410 | 287 | 491 | 777 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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