| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G073054_T02 |
| Family | GH13 |
| Protein Properties | Length: 845 Molecular Weight: 94794.3 Isoelectric Point: 5.2474 |
| Chromosome | Chromosome/Scaffold: 2 Start: 58586007 End: 58596234 |
| Description | starch branching enzyme 2.2 |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 355 | 675 | 5.8e-31 |
| LPRIKKLGYNAVQIMAIQEHSYYASFGYHVTNFFAPSSRFGTPEDLKSLIDKAHELGLLVLMDIVHSHSSNNTLDGLNGFDGTDTHYFHGGPRGHHWMWD SRLFNYGSWEVLRFLLSNARWWLEEYKFDGFRFDGVTSMMYTHHGLQVTFTGNYGEYFGFATDVDAVVYLMLVNDLIRGLYPEAVSIGEDVSGMPTFCIP VQDGGVGFDYRLHMAVPDKWIELLKQSDEYWEMGDIVHTLTNRRWLEKCVTYCESHDQALVGDKTIAFWLMDKDMYDFMALDRPSTPRIDRGIALHKMIR LVTMGLGGEGYLNFMGNEFGH | |||
| Full Sequence |
|---|
| Protein Sequence Length: 845 Download |
| MASFAVSGAR LGVVRPGGSA RSGGERRSAV DLPSVLFRRK DAFSRTVLSC AGAPGKVLVP 60 GGGSDDLLSS AEPVVDTQPE ELQIPEAELT VEKTSSSPTQ TTSAVAEASS GVEAEERPEL 120 SEVIGVGGTG GTKIDGAGIK AKAPLVEEKP RVIPPPGDGQ RIYEIDPMLE GFRGHLDYRY 180 SEYKRLRAAI DQHEGGLDAF SRGYEKLGFT RSAEGITYRE WAPGAYSAAL VGDFNNWNPN 240 ADAMARNEYG VWEIFLPNNA DGSPAIPHGS RVKIRMDTPS GVKDSIPAWI KFSVQAPGEI 300 PYNGIYYDPP EEEKYVFKHP QPKRPKSLRI YESHVGMSSP EPKINTYANF RDEVLPRIKK 360 LGYNAVQIMA IQEHSYYASF GYHVTNFFAP SSRFGTPEDL KSLIDKAHEL GLLVLMDIVH 420 SHSSNNTLDG LNGFDGTDTH YFHGGPRGHH WMWDSRLFNY GSWEVLRFLL SNARWWLEEY 480 KFDGFRFDGV TSMMYTHHGL QVTFTGNYGE YFGFATDVDA VVYLMLVNDL IRGLYPEAVS 540 IGEDVSGMPT FCIPVQDGGV GFDYRLHMAV PDKWIELLKQ SDEYWEMGDI VHTLTNRRWL 600 EKCVTYCESH DQALVGDKTI AFWLMDKDMY DFMALDRPST PRIDRGIALH KMIRLVTMGL 660 GGEGYLNFMG NEFGHPEWID FPRGPQSLPN GSVIPGNNNS FDKCRRRFDL GDADYLRYRG 720 MQEFDQAMQH LEGKYEFMTS DHSYVSRKHE EDKVIIFERG DLVFVFNFHW SNSYFDYRVG 780 CFKPGKYKIV LDSDDGLFGG FSRLDHDAEY FTADWPHDNR PCSFSVYAPS RTAVVYAPAG 840 AEDE* 900 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PLN02960 | PLN02960 | 3.0e-9 | 172 | 256 | 91 | + alpha-amylase | ||
| PLN03244 | PLN03244 | 5.0e-133 | 264 | 836 | 579 | + alpha-amylase; Provisional | ||
| PLN02447 | PLN02447 | 0 | 150 | 844 | 699 | + 1,4-alpha-glucan-branching enzyme | ||
| cd11321 | AmyAc_bac_euk_BE | 0 | 311 | 726 | 417 | + Alpha amylase catalytic domain found in bacterial and eukaryotic branching enzymes. Branching enzymes (BEs) catalyze the formation of alpha-1,6 branch points in either glycogen or starch by cleavage of the alpha-1,4 glucosidic linkage yielding a non-reducing end oligosaccharide chain, and subsequent attachment to the alpha-1,6 position. By increasing the number of non-reducing ends, glycogen is more reactive to synthesis and digestion as well as being more soluble. This group includes bacterial and eukaryotic proteins. 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. | ||
| PLN02960 | PLN02960 | 0 | 264 | 836 | 577 | + alpha-amylase | ||
| 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 |
| GenBank | AAB67316.1 | 0 | 31 | 844 | 1 | 814 | starch branching enzyme IIa [Zea mays] |
| DDBJ | BAA82828.1 | 0 | 1 | 837 | 1 | 837 | starch branching enzyme rbe4 [Oryza sativa] |
| GenBank | EEC77237.1 | 0 | 47 | 837 | 178 | 965 | hypothetical protein OsI_15790 [Oryza sativa Indica Group] |
| GenBank | EEE60949.1 | 0 | 1 | 837 | 1 | 837 | hypothetical protein OsJ_14706 [Oryza sativa Japonica Group] |
| RefSeq | XP_002447772.1 | 0 | 1 | 844 | 1 | 827 | hypothetical protein SORBIDRAFT_06g015360 [Sorghum bicolor] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3amk_A | 0 | 162 | 836 | 13 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
| PDB | 3aml_A | 0 | 162 | 836 | 13 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
| PDB | 3vu2_B | 0 | 162 | 836 | 13 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
| PDB | 3vu2_A | 0 | 162 | 836 | 13 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
| PDB | 1m7x_D | 8.40779e-45 | 202 | 800 | 9 | 577 | A Chain A, The X-Ray Crystallographic Structure Of Branching Enzyme |
| Hydropathy |
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