| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G073054_T01 |
| Family | GH13 |
| Protein Properties | Length: 835 Molecular Weight: 93474.7 Isoelectric Point: 5.0875 |
| 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 | 345 | 665 | 5.6e-31 |
| LPRIKKLGYNAVQIMAIQEHSYYASFGYHVTNFFAPSSRFGTPEDLKSLIDKAHELGLLVLMDIVHSHSSNNTLDGLNGFDGTDTHYFHGGPRGHHWMWD SRLFNYGSWEVLRFLLSNARWWLEEYKFDGFRFDGVTSMMYTHHGLQVTFTGNYGEYFGFATDVDAVVYLMLVNDLIRGLYPEAVSIGEDVSGMPTFCIP VQDGGVGFDYRLHMAVPDKWIELLKQSDEYWEMGDIVHTLTNRRWLEKCVTYCESHDQALVGDKTIAFWLMDKDMYDFMALDRPSTPRIDRGIALHKMIR LVTMGLGGEGYLNFMGNEFGH | |||
| Full Sequence |
|---|
| Protein Sequence Length: 835 Download |
| MASFAVSGAR LGVVRPGGSA RSGGERRSAV DLPSGTVLSC AGAPGKVLVP GGGSDDLLSS 60 AEPVVDTQPE ELQIPEAELT VEKTSSSPTQ TTSAVAEASS GVEAEERPEL SEVIGVGGTG 120 GTKIDGAGIK AKAPLVEEKP RVIPPPGDGQ RIYEIDPMLE GFRGHLDYRY SEYKRLRAAI 180 DQHEGGLDAF SRGYEKLGFT RSAEGITYRE WAPGAYSAAL VGDFNNWNPN ADAMARNEYG 240 VWEIFLPNNA DGSPAIPHGS RVKIRMDTPS GVKDSIPAWI KFSVQAPGEI PYNGIYYDPP 300 EEEKYVFKHP QPKRPKSLRI YESHVGMSSP EPKINTYANF RDEVLPRIKK LGYNAVQIMA 360 IQEHSYYASF GYHVTNFFAP SSRFGTPEDL KSLIDKAHEL GLLVLMDIVH SHSSNNTLDG 420 LNGFDGTDTH YFHGGPRGHH WMWDSRLFNY GSWEVLRFLL SNARWWLEEY KFDGFRFDGV 480 TSMMYTHHGL QVTFTGNYGE YFGFATDVDA VVYLMLVNDL IRGLYPEAVS IGEDVSGMPT 540 FCIPVQDGGV GFDYRLHMAV PDKWIELLKQ SDEYWEMGDI VHTLTNRRWL EKCVTYCESH 600 DQALVGDKTI AFWLMDKDMY DFMALDRPST PRIDRGIALH KMIRLVTMGL GGEGYLNFMG 660 NEFGHPEWID FPRGPQSLPN GSVIPGNNNS FDKCRRRFDL GDADYLRYRG MQEFDQAMQH 720 LEGKYEFMTS DHSYVSRKHE EDKVIIFERG DLVFVFNFHW SNSYFDYRVG CFKPGKYKIV 780 LDSDDGLFGG FSRLDHDAEY FTADWPHDNR PCSFSVYAPS RTAVVYAPAG AEDE* 840 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PLN02960 | PLN02960 | 3.0e-9 | 162 | 246 | 91 | + alpha-amylase | ||
| PLN03244 | PLN03244 | 5.0e-133 | 254 | 826 | 579 | + alpha-amylase; Provisional | ||
| PLN02447 | PLN02447 | 0 | 140 | 834 | 699 | + 1,4-alpha-glucan-branching enzyme | ||
| cd11321 | AmyAc_bac_euk_BE | 0 | 301 | 716 | 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 | 254 | 826 | 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 | 834 | 11 | 814 | starch branching enzyme IIa [Zea mays] |
| DDBJ | BAA82828.1 | 0 | 1 | 827 | 1 | 837 | starch branching enzyme rbe4 [Oryza sativa] |
| GenBank | EEC77237.1 | 0 | 35 | 827 | 176 | 965 | hypothetical protein OsI_15790 [Oryza sativa Indica Group] |
| GenBank | EEE60949.1 | 0 | 1 | 827 | 1 | 837 | hypothetical protein OsJ_14706 [Oryza sativa Japonica Group] |
| RefSeq | XP_002447772.1 | 0 | 1 | 834 | 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 | 152 | 826 | 13 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
| PDB | 3aml_A | 0 | 152 | 826 | 13 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
| PDB | 3vu2_B | 0 | 152 | 826 | 13 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
| PDB | 3vu2_A | 0 | 152 | 826 | 13 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
| PDB | 1m7x_D | 7.00649e-45 | 192 | 790 | 9 | 577 | A Chain A, The X-Ray Crystallographic Structure Of Branching Enzyme |
| Hydropathy |
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