| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G150796_T01 |
| Family | GH13 |
| Protein Properties | Length: 778 Molecular Weight: 87069.9 Isoelectric Point: 6.9056 |
| Chromosome | Chromosome/Scaffold: 7 Start: 129101505 End: 129113096 |
| Description | isoamylase 3 |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 269 | 632 | 0 |
| RGSYLGVIDKIPHLLELGVNAVELLPVFEFDELELKRFPNPRDHMVNTWGYSTINFFAPMSRYASAGGGPVAASKELKQMVKAFHNSGIEVILDVVYNHT NEADDVNPYMTSFRGIDNKVYYMLDLNNSAQLLNFSGCGNTLNCNHPVVKELVLDSLRHWVKEYHIDGFRFDLASVLCRGPDGSPLDAPPLIKEIAKDSV LSRCKIIAEPWDCGGLYLVGRFPNWDRWAEWNGKYRDDIRRFIKGDPGMKGVFATRVSGSADLYQVNNRKPYHSVNFVIAHDGFTLCDLVSYNSKHNDAN GEGGRDGCNDNYSWNCGIEGETNDLNVLSLRSRQMKNFHVALMISQGTPMMLMGDEYGHTRYGN | |||
| Full Sequence |
|---|
| Protein Sequence Length: 778 Download |
| MDSVGTNRPP LRPVAAAATR RSALLRPPSH LGLGNRFAET KLGIASGCGG GGGYFGKVQG 60 FDALRSTTTK VQSGKAGRSV TKEMGHTSSG NEVPLKYSSG KAFPLGVSQV DDGLNFAIFS 120 QHASSVTLCL NFPERGNQDD VDIVEFALDR QKNKTGDIWH VSVEGLPASG VLYGYRINGP 180 QGWQQGHRFD DSVILLDPYA KLVYGRKHFA VEKEKPSQLF GTYDFDSSPF DWGDNYKLPN 240 LPETDLVIYE MNVRAFTADE SSRLAPAIRG SYLGVIDKIP HLLELGVNAV ELLPVFEFDE 300 LELKRFPNPR DHMVNTWGYS TINFFAPMSR YASAGGGPVA ASKELKQMVK AFHNSGIEVI 360 LDVVYNHTNE ADDVNPYMTS FRGIDNKVYY MLDLNNSAQL LNFSGCGNTL NCNHPVVKEL 420 VLDSLRHWVK EYHIDGFRFD LASVLCRGPD GSPLDAPPLI KEIAKDSVLS RCKIIAEPWD 480 CGGLYLVGRF PNWDRWAEWN GKYRDDIRRF IKGDPGMKGV FATRVSGSAD LYQVNNRKPY 540 HSVNFVIAHD GFTLCDLVSY NSKHNDANGE GGRDGCNDNY SWNCGIEGET NDLNVLSLRS 600 RQMKNFHVAL MISQGTPMML MGDEYGHTRY GNNNSYGHDT HINNFQWGQL EERKDGHFRF 660 FSEMIKFRHN HPILRRDRFL NKNDVTWHEN RWENQDSKFL AFTIHDHSSG GDIYLAFNAH 720 EYFVDAVIPP PPHHKSWSRV VDTNLESPKD IVPEGVPFTG SGYRIAPYSS ILLKAKP* 780 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK14510 | PRK14510 | 5.0e-144 | 94 | 681 | 607 | + putative bifunctional 4-alpha-glucanotransferase/glycogen debranching enzyme; Provisional | ||
| PRK03705 | PRK03705 | 5.0e-171 | 99 | 730 | 665 | + glycogen debranching enzyme; Provisional | ||
| cd11326 | AmyAc_Glg_debranch | 0 | 230 | 671 | 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. | ||
| TIGR02100 | glgX_debranch | 0 | 99 | 762 | 706 | + 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]. | ||
| COG1523 | PulA | 0 | 94 | 751 | 692 | + Type II secretory pathway, pullulanase PulA and related glycosidases [Carbohydrate transport and metabolism] | ||
| 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 | BAD19754.1 | 0 | 80 | 777 | 1 | 700 | putative isoamylase-type starch debranching enzyme [Oryza sativa Japonica Group] |
| DDBJ | BAD89532.1 | 0 | 1 | 777 | 1 | 776 | isoamylase [Hordeum vulgare] |
| GenBank | EEC84730.1 | 0 | 165 | 777 | 41 | 653 | hypothetical protein OsI_31715 [Oryza sativa Indica Group] |
| GenBank | EEE69882.1 | 0 | 1 | 777 | 1 | 782 | hypothetical protein OsJ_29702 [Oryza sativa Japonica Group] |
| RefSeq | NP_001105198.1 | 0 | 84 | 777 | 1 | 694 | isoamylase-type starch debranching enzyme ISO3 [Zea mays] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2vuy_B | 0 | 100 | 680 | 15 | 600 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) Double Mutant Y105aY380A IN COMPLEX WITH INHIBITOR ACARBOSE |
| PDB | 2vuy_A | 0 | 100 | 680 | 15 | 600 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) Double Mutant Y105aY380A IN COMPLEX WITH INHIBITOR ACARBOSE |
| PDB | 2vr5_B | 0 | 100 | 680 | 15 | 600 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) Double Mutant Y105aY380A IN COMPLEX WITH INHIBITOR ACARBOSE |
| PDB | 2vr5_A | 0 | 100 | 680 | 15 | 600 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) Double Mutant Y105aY380A IN COMPLEX WITH INHIBITOR ACARBOSE |
| PDB | 2vnc_B | 0 | 100 | 680 | 15 | 600 | A Chain A, Crystal Structure Of Glycogen Debranching Enzyme Trex From Sulfolobus Solfataricus |
| Hydropathy |
|---|
 |