| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G088753_T01 |
| Family | GH13 |
| Protein Properties | Length: 824 Molecular Weight: 92884.7 Isoelectric Point: 7.1962 |
| Chromosome | Chromosome/Scaffold: 5 Start: 63317874 End: 63324803 |
| Description | starch branching enzyme 2.2 |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 279 | 604 | 2e-27 |
| LPRIRANNYNTVQLMAVMEHSYYASFGYHVTNFFAVSSRSGTPEDLKYLVDKAHSLGLRVLMDVVHSHASNNVTDGLNGYDVGQSTQESYFHAGDRGYHK LWDSRLFNYANWEVLRFLLSNLRYWLDEFMFDGFRFDGVTSMLYHHHGINVGFTGNYQEYFSLDTAVDAVVYMMLANHLMHKLLPEATVVAEDVSGMPVL CRPVDEGGVGFDYRLAMAIPDRWIDYLKNKDDSEWSMGEIAHTLTNRRYTEKCIAYAESHDQSIVGDKTIAFLLMDKEMYTGMSDLQPASPTIDRGIALQ KMIHFITMALGGDGYLNFMGNEFGHP | |||
| Full Sequence |
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| Protein Sequence Length: 824 Download |
| MLCLVSPSSS PTPLPPPRRS RSHADRAAPP GIAGGGNVRL SVLSVQCKAR RSGVRKVKSK 60 FATAATVQED KTMATAKGDV DHLPIYDLDP KLEIFKDHFR YRMKRFLEQK GSIEENEGSL 120 ESFSKGYLKF GINTNEDGTV YREWAPAAQE AELIGDFNDW NGANHKMEKD KFGVWSIKID 180 HVKGKPAIPH NSKVKFRFLH GGVWVDRIPA LIRYATVDAS KFGAPYDGVH WDPPASERYT 240 FKHPRPSKPA APRIYEAHVG MSGEKPAVST YREFADNVLP RIRANNYNTV QLMAVMEHSY 300 YASFGYHVTN FFAVSSRSGT PEDLKYLVDK AHSLGLRVLM DVVHSHASNN VTDGLNGYDV 360 GQSTQESYFH AGDRGYHKLW DSRLFNYANW EVLRFLLSNL RYWLDEFMFD GFRFDGVTSM 420 LYHHHGINVG FTGNYQEYFS LDTAVDAVVY MMLANHLMHK LLPEATVVAE DVSGMPVLCR 480 PVDEGGVGFD YRLAMAIPDR WIDYLKNKDD SEWSMGEIAH TLTNRRYTEK CIAYAESHDQ 540 SIVGDKTIAF LLMDKEMYTG MSDLQPASPT IDRGIALQKM IHFITMALGG DGYLNFMGNE 600 FGHPEWIDFP REGNNWSYDK CRRQWSLVDT DHLRYKYMNA FDQAMNALDE RFSFLSSSKQ 660 IVSDMNDEEK VIVFERGDLV FVFNFHPKKT YEGYKVGCDL PGKYRVALDS DALVFGGHGR 720 VGHDVDHFTS PEGVPGVPET NFNNRPNSFK VLSPPRTCVA YYRVDEAGAG RRLHAKAETG 780 KTSPAESIDV KASRASSKED KEATAGGKKG WKFARQPSDQ DTK* 840 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PLN02960 | PLN02960 | 7.0e-7 | 23 | 180 | 164 | + alpha-amylase | ||
| PLN03244 | PLN03244 | 5.0e-134 | 186 | 711 | 528 | + alpha-amylase; Provisional | ||
| PLN02960 | PLN02960 | 2.0e-180 | 186 | 711 | 527 | + alpha-amylase | ||
| PLN02447 | PLN02447 | 0 | 24 | 767 | 745 | + 1,4-alpha-glucan-branching enzyme | ||
| cd11321 | AmyAc_bac_euk_BE | 0 | 236 | 643 | 408 | + 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. | ||
| 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 | AAD50279.2 | 0 | 1 | 823 | 1 | 832 | seed starch branching enzyme [Sorghum bicolor] |
| GenBank | AAO20100.1 | 0 | 1 | 823 | 1 | 823 | starch branching enzyme I [Zea mays] |
| GenBank | ABQ15209.1 | 0 | 1 | 823 | 1 | 823 | starch branching enzyme I [Zea mays] |
| DDBJ | BAA01854.1 | 0 | 2 | 823 | 1 | 822 | branching enzyme-I precursor [Zea mays] |
| RefSeq | NP_001105370.1 | 0 | 1 | 823 | 1 | 823 | starch branching enzyme1 [Zea mays] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3aml_A | 0 | 73 | 823 | 1 | 755 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
| PDB | 3amk_A | 0 | 73 | 766 | 1 | 695 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
| PDB | 3vu2_B | 0 | 73 | 766 | 1 | 695 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
| PDB | 3vu2_A | 0 | 73 | 766 | 1 | 695 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
| PDB | 1m7x_D | 4.00001e-41 | 138 | 717 | 26 | 577 | A Chain A, The X-Ray Crystallographic Structure Of Branching Enzyme |
| Hydropathy |
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