y
Basic Information | |
---|---|
Species | Ricinus communis |
Cazyme ID | 29908.m006089 |
Family | GH13 |
Protein Properties | Length: 783 Molecular Weight: 88877.1 Isoelectric Point: 6.4816 |
Chromosome | Chromosome/Scaffold: 29908 Start: 1537956 End: 1548756 |
Description | isoamylase 3 |
View CDS |
External Links |
---|
NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
GH13 | 274 | 638 | 0 |
IRGSYLGVIEKIPHLLELGVNAVELLPVFEFDEFELQRRPNPRDHMINTWGYSTINFFAPMSRYASGGGGPCNASREFKEMVKALHGAGIEVILDVVYNH TNEADDKNPYTTSFRGIDNMIYYMLDLNNKNQLLNFSGCGNTLNCNHPVVMELILESLRHWVTEYHVDGFRFDLASVLCRGTDGTPLNAPPVIRAIAKDA ILSRCKIISEPWDCGGLYLVGKFPNWDRWAEWNGMYRDDIRRYIKGDSGMKGSFATRVAGSADLYRVNKRKPFHSVNFVIAHDGFTLHDLVSYNFKHNDA NGEGGNDGSNDNFSWNCGFEGETDDPNIKALRSRQMKNFHLALMISQGTPMMLMGDEYGHTRYGN |
Full Sequence |
---|
Protein Sequence Length: 783 Download |
MLRSPLPLHY DSISAAKMPL FALSFANNST HISPCTGAFR AVDMGYVNKP FVAVAIEISV 60 RHSRRRAKHR TPNVYARGAQ ERVLQEEKVS QMSEMTPSFN LYPGQAFPLG VSEVDNGINF 120 ALFSQHATSV TLCLLLPQRG GSDSTDGGMI ELDLDPRMNK TGDIWHICVE DLPRSSVLYG 180 YRVDGPHNWD QGHRFDRSIV LLDPYAKLIE GRRYFGDATH KLSKFLGTYD FDSLPFDWGE 240 NYKLPNIPEK DLVIYEMNIR AFTADKSSGL EPKIRGSYLG VIEKIPHLLE LGVNAVELLP 300 VFEFDEFELQ RRPNPRDHMI NTWGYSTINF FAPMSRYASG GGGPCNASRE FKEMVKALHG 360 AGIEVILDVV YNHTNEADDK NPYTTSFRGI DNMIYYMLDL NNKNQLLNFS GCGNTLNCNH 420 PVVMELILES LRHWVTEYHV DGFRFDLASV LCRGTDGTPL NAPPVIRAIA KDAILSRCKI 480 ISEPWDCGGL YLVGKFPNWD RWAEWNGMYR DDIRRYIKGD SGMKGSFATR VAGSADLYRV 540 NKRKPFHSVN FVIAHDGFTL HDLVSYNFKH NDANGEGGND GSNDNFSWNC GFEGETDDPN 600 IKALRSRQMK NFHLALMISQ GTPMMLMGDE YGHTRYGNNN SYGHDTSINN FQWELLAAQR 660 NDHFQFFSEV IKFRRTHQVF RHDNFLNQND VTWHEDNWDN YESKFLAFTL HESNGADIYL 720 AFNAHDYFIK VLIPPPPSKR SWFRVADTNL KSPDDFVPEG VPGIGSAYNV APYSSILLEA 780 KLT 840 |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK14510 | PRK14510 | 1.0e-134 | 103 | 734 | 671 | + putative bifunctional 4-alpha-glucanotransferase/glycogen debranching enzyme; Provisional | ||
PRK03705 | PRK03705 | 5.0e-154 | 95 | 693 | 624 | + glycogen debranching enzyme; Provisional | ||
cd11326 | AmyAc_Glg_debranch | 0 | 236 | 677 | 445 | + Alpha amylase catalytic domain found in glycogen debranching enzymes. Debranching enzymes facilitate the breakdown of glycogen through glucosyltransferase and glucosidase activity. These activities are performed by a single enzyme in mammals, yeast, and some bacteria, but by two distinct enzymes in Escherichia coli and other bacteria. Debranching enzymes perform two activities: 4-alpha-D-glucanotransferase (EC 2.4.1.25) and amylo-1,6-glucosidase (EC 3.2.1.33). 4-alpha-D-glucanotransferase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. Amylo-alpha-1,6-glucosidase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. In Escherichia coli, GlgX is the debranching enzyme and malQ is the 4-alpha-glucanotransferase. TreX, an archaeal glycogen-debranching enzyme has dual activities like mammals and yeast, but is structurally similar to GlgX. TreX exists in two oligomeric states, a dimer and tetramer. Isoamylase (EC 3.2.1.68) is one of the starch-debranching enzymes that catalyzes the hydrolysis of alpha-1,6-glucosidic linkages specific in alpha-glucans such as amylopectin or glycogen and their beta-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 | 0 | 101 | 766 | 701 | + Type II secretory pathway, pullulanase PulA and related glycosidases [Carbohydrate transport and metabolism] | ||
TIGR02100 | glgX_debranch | 0 | 103 | 748 | 688 | + glycogen debranching enzyme GlgX. This family consists of the GlgX protein from the E. coli glycogen operon and probable equivalogs from other prokaryotic species. GlgX is not required for glycogen biosynthesis, but instead acts as a debranching enzyme for glycogen catabolism. This model distinguishes GlgX from pullanases and other related proteins that also operate on alpha-1,6-glycosidic linkages. In the wide band between the trusted and noise cutoffs are functionally similar enzymes, mostly from plants, that act similarly but usually are termed isoamylase [Energy metabolism, Biosynthesis and degradation of polysaccharides]. |
Gene Ontology | |
---|---|
GO Term | Description |
GO:0003824 | catalytic activity |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0005975 | carbohydrate metabolic process |
GO:0043169 | cation binding |
Annotations - NR Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
DDBJ | BAF52943.1 | 0 | 7 | 781 | 5 | 782 | isoamylase-type starch-debranching enzyme 3 [Phaseolus vulgaris] |
EMBL | CBI19205.1 | 0 | 14 | 782 | 9 | 775 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002284042.1 | 0 | 14 | 782 | 21 | 787 | PREDICTED: similar to isoamylase-type starch-debranching enzyme 3 [Vitis vinifera] |
RefSeq | XP_002301076.1 | 0 | 71 | 781 | 71 | 818 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002513977.1 | 0 | 1 | 783 | 1 | 783 | isoamylase, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 2vuy_B | 0 | 101 | 760 | 12 | 699 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt85h2- Insights Into The Structural Basis Of A Multifunctional (Iso) Flavonoid Glycosyltransferase |
PDB | 2vuy_A | 0 | 101 | 760 | 12 | 699 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt85h2- Insights Into The Structural Basis Of A Multifunctional (Iso) Flavonoid Glycosyltransferase |
PDB | 2vr5_B | 0 | 101 | 760 | 12 | 699 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt85h2- Insights Into The Structural Basis Of A Multifunctional (Iso) Flavonoid Glycosyltransferase |
PDB | 2vr5_A | 0 | 101 | 760 | 12 | 699 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt85h2- Insights Into The Structural Basis Of A Multifunctional (Iso) Flavonoid Glycosyltransferase |
PDB | 2vnc_B | 0 | 101 | 760 | 12 | 699 | A Chain A, Crystal Structure Of Glycogen Debranching Enzyme Trex From Sulfolobus Solfataricus |
EST Download unfiltered results here | ||||
---|---|---|---|---|
Hit | Length | Start | End | EValue |
HO798725 | 454 | 198 | 651 | 0 |
HO430858 | 266 | 518 | 781 | 0 |
HO430858 | 167 | 356 | 522 | 0 |
HO430858 | 129 | 231 | 359 | 0 |
HO798725 | 35 | 666 | 700 | 0.00005 |
Sequence Alignments (This image is cropped. Click for full image.) |
---|