| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G005298_T01 |
| Family | GH13 |
| Protein Properties | Length: 900 Molecular Weight: 103438 Isoelectric Point: 6.2393 |
| Chromosome | Chromosome/Scaffold: 8 Start: 141990059 End: 141994717 |
| Description | Alpha amylase family protein |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 420 | 742 | 1.2e-24 |
| FQEFTSKVLPHIKKAGYNAVQLIGVVEHKDYSSIGYKVTNYFAVSSRFGTPDDFKKLVDEAHGLGLVVLLDIIHSYASADELVGLSLFDGSNDCYFHSGK RGHHKYWGTRMFKYDDVDVLHFLLSNLNWWVTEYRIDGFQFHSLSSMLYTHNGFSTFTGAMEEYCNQYVDKDALIYLILANEMLHRLHPDIVTIAEDATF YPGLCEPITQGGLGFNYWVNLSIPEMWLWHLENVPEQEWSMNKIIKVLVSSNQNMLSYVENHNQSISGRKSFAEIILNSRECSVGSVDDNLIRASSLLKL MKLITFTTSGGAYLNFMGNEFAH | |||
| Full Sequence |
|---|
| Protein Sequence Length: 900 Download |
| MASCPLFLLV PRPPPSLVGA DRCPGSAGCS DLPTSCRPHP GRRHGYPFRC NSSSSSSAPR 60 ERPPRQRPGG RGDAIDPVGF LTKLGVSDRA FAQFLRDRHK ALKDRRWELC SRFIDLKEAS 120 SGFELLGMHR HRQHRIDFME WAPGARYCSL IGDFNQWSPT ENCAREGHLG HDDFGYWFII 180 LEDKLREGQE QDEYFFQEYN YVDDYDKGDN GIDADEIMRR MKEEYWEPGE IRSRQSQLEM 240 VVKLYEQMFG PNGPQTEEEL GEIPDAQTRY NEFKASQKAD SSSQPSYDII DNGQEFDIFS 300 VVTDRASFEK FQAKKPPLAY WVEMRKGRIA WLEKYVPTIS HKDKYRVYFN TPDGALERIP 360 AWAAYVLPDA EGKQSYAVHW EPPPEEIYKW RFGRPKVKGS LRIYECHVGI SGSEQKVSSF 420 QEFTSKVLPH IKKAGYNAVQ LIGVVEHKDY SSIGYKVTNY FAVSSRFGTP DDFKKLVDEA 480 HGLGLVVLLD IIHSYASADE LVGLSLFDGS NDCYFHSGKR GHHKYWGTRM FKYDDVDVLH 540 FLLSNLNWWV TEYRIDGFQF HSLSSMLYTH NGFSTFTGAM EEYCNQYVDK DALIYLILAN 600 EMLHRLHPDI VTIAEDATFY PGLCEPITQG GLGFNYWVNL SIPEMWLWHL ENVPEQEWSM 660 NKIIKVLVSS NQNMLSYVEN HNQSISGRKS FAEIILNSRE CSVGSVDDNL IRASSLLKLM 720 KLITFTTSGG AYLNFMGNEF AHPEKVEFPM PSNDYSFELA NRQWELLDKV FHKHIFNFDK 780 DVMSLDENER IISRGPPNIL HCDDTSMVIS FTRGPLFFIF NFNPQVSHQS YRVGVDEAGE 840 YQLIFNTDET KYGGCETLKS SQYMRRTSDK RADGCRNSLE LALPSRSAQI YKLVRILRI* 900 960 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PLN02447 | PLN02447 | 2.0e-10 | 89 | 183 | 95 | + 1,4-alpha-glucan-branching enzyme | ||
| cd11321 | AmyAc_bac_euk_BE | 1.0e-166 | 384 | 780 | 409 | + 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 | 1 | 899 | 905 | + alpha-amylase | ||
| PLN03244 | PLN03244 | 0 | 74 | 899 | 832 | + alpha-amylase; Provisional | ||
| PLN02447 | PLN02447 | 0 | 336 | 894 | 572 | + 1,4-alpha-glucan-branching enzyme | ||
| 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 |
| EMBL | CBI26672.1 | 0 | 29 | 899 | 16 | 896 | unnamed protein product [Vitis vinifera] |
| RefSeq | NP_001057611.1 | 0 | 1 | 899 | 1 | 903 | Os06g0367100 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | NP_001108121.1 | 0 | 1 | 899 | 1 | 899 | starch branching enzyme III [Zea mays] |
| RefSeq | NP_001154629.1 | 0 | 74 | 899 | 68 | 899 | alpha-amylase/ catalytic/ cation binding [Arabidopsis thaliana] |
| RefSeq | XP_002455921.1 | 0 | 1 | 899 | 1 | 906 | hypothetical protein SORBIDRAFT_03g027310 [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 | 337 | 894 | 114 | 693 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
| PDB | 3vu2_B | 0 | 337 | 894 | 114 | 693 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
| PDB | 3vu2_A | 0 | 337 | 894 | 114 | 693 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
| Hydropathy |
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