y
Basic Information | |
---|---|
Species | Citrus sinensis |
Cazyme ID | orange1.1g002787m |
Family | GH13 |
Protein Properties | Length: 882 Molecular Weight: 97303.6 Isoelectric Point: 5.9734 |
Chromosome | Chromosome/Scaffold: 00300 Start: 87990 End: 101318 |
Description | limit dextrinase |
View CDS |
External Links |
---|
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
GH13 | 372 | 775 | 1.1e-22 |
SHLKKLSNAGLTHVHLLPTFQFAGVDDRKENWKSVGSLPGLVFFGQNTFSSWWIVCACGIKSFADAEVLEKLPPDSTEQQAQITAIQNDDGYNWGYNPVL WGVPKGSYASNPNGSCRTIEFRRMVQALNHIGLHVVLDVVYNHLQGSGPFDDNSVLDKVVPGYYLRRNSDGFIEHSTCMNNTASEHYMVERLIIDDLLCW AVNYKVDGFRFDLMGHIMKSTMMKAKHALHSLTKEIHGVDGSSIYIYGEGWDFGEVAKNGRGVNASQFNLSGTGIGSFNDRIRDAMLGGSPFGPPLQQGF VTGLLLQPNGHDHGTKAVEEQMLAAAKDHIQVGLAANLRDFQLTNSEGNKVKGSEVKTYDGTPVAYALCPTETISYVSAHDNETLFDVVSLKGIPFFHCG DEIL |
Full Sequence |
---|
Protein Sequence Length: 882 Download |
MSSPVFLSSA FSTANGHLPL LSPRPATCPC PGFASKPTLA PTATFFYRES VHPRFRCCCC 60 CSSSSSSSSS SMPLELSTSA SDQDDDLGDS LLYSRAYWVS ESIIAWNVDV PDGSCYLYAS 120 RTAALSISYG GIQGADVEIE LQEDKGGLPA NVIEKFPHIR DYKAFKVPAG SDAKLLLKCQ 180 LAVADRKCSD ATGLQLPGIL DELFSYDGPL GALYAEETVS LYLWAPTAQS VSACIYRDPL 240 GGNPLEVVQL KENDGVWSIK GPKSWEGCYY VYEVSVYHPS ALQIEKCYAN DPYARGLSSD 300 GRRTLLVNLD SDTLKPEGWD KLVYEKPDIL SFSDISIYEL HVRDFSVSDH TVHPDFRGGY 360 LAFTLQNSAG VSHLKKLSNA GLTHVHLLPT FQFAGVDDRK ENWKSVGSLP GLVFFGQNTF 420 SSWWIVCACG IKSFADAEVL EKLPPDSTEQ QAQITAIQND DGYNWGYNPV LWGVPKGSYA 480 SNPNGSCRTI EFRRMVQALN HIGLHVVLDV VYNHLQGSGP FDDNSVLDKV VPGYYLRRNS 540 DGFIEHSTCM NNTASEHYMV ERLIIDDLLC WAVNYKVDGF RFDLMGHIMK STMMKAKHAL 600 HSLTKEIHGV DGSSIYIYGE GWDFGEVAKN GRGVNASQFN LSGTGIGSFN DRIRDAMLGG 660 SPFGPPLQQG FVTGLLLQPN GHDHGTKAVE EQMLAAAKDH IQVGLAANLR DFQLTNSEGN 720 KVKGSEVKTY DGTPVAYALC PTETISYVSA HDNETLFDVV SLKGIPFFHC GDEILRSKSL 780 DRDSYNSGDW LNRIDFSYNS NNWGVGLPPK EKNEKNWPLI RPRLADPSFK PQKSHILAAL 840 ENFSDVLRIR YSSPLFRLRT ANAIQVRRRH MSCLDCFPNC E* 900 |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd11341 | AmyAc_Pullulanase_LD-like | 1.0e-20 | 334 | 405 | 79 | + 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. | ||
COG1523 | PulA | 2.0e-75 | 209 | 802 | 631 | + Type II secretory pathway, pullulanase PulA and related glycosidases [Carbohydrate transport and metabolism] | ||
cd11341 | AmyAc_Pullulanase_LD-like | 3.0e-123 | 455 | 802 | 375 | + 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 | 93 | 870 | 807 | + alpha-amylase/limit dextrinase | ||
TIGR02103 | pullul_strch | 0 | 93 | 867 | 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 | |
---|---|
GO Term | Description |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0005975 | carbohydrate metabolic process |
Annotations - NR Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CBI31395.1 | 0 | 12 | 869 | 18 | 854 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_196056.2 | 0 | 89 | 869 | 83 | 863 | ATLDA (LIMIT DEXTRINASE); alpha-amylase/ limit dextrinase/ pullulanase [Arabidopsis thaliana] |
RefSeq | XP_002271820.1 | 0 | 76 | 869 | 12 | 805 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002315334.1 | 0 | 72 | 869 | 1 | 793 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002532780.1 | 0 | 68 | 869 | 65 | 864 | pullulanase, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 4aio_A | 0 | 94 | 869 | 6 | 783 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
PDB | 2y5e_A | 0 | 94 | 869 | 6 | 783 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
PDB | 2y4s_A | 0 | 94 | 869 | 6 | 783 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
PDB | 2fhf_A | 0 | 96 | 867 | 179 | 973 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
PDB | 2fhc_A | 0 | 96 | 867 | 179 | 973 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
EST Download unfiltered results here | ||||
---|---|---|---|---|
Hit | Length | Start | End | EValue |
CO128344 | 283 | 434 | 716 | 0 |
DT730114 | 305 | 234 | 538 | 0 |
EY835248 | 239 | 652 | 865 | 0 |
EL452695 | 294 | 326 | 619 | 0 |
EH717381 | 294 | 301 | 594 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
---|