y
Basic Information | |
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Species | Eucalyptus grandis |
Cazyme ID | Eucgr.F03487.1 |
Family | GH13 |
Protein Properties | Length: 905 Molecular Weight: 103572 Isoelectric Point: 6.6182 |
Chromosome | Chromosome/Scaffold: 6 Start: 43627613 End: 43638834 |
Description | Alpha amylase family protein |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 423 | 748 | 3.1e-27 |
NEFTEKVLPHIKDAGYNAIQLIGVVEHKDYYTVGYRVTNFYAVSSRFGTPDDFKHLVDEAHGLGLLVFLDIVHSYSAADEMVGLSLFDGSNDCYFHTGKR GQHKYWGTRMFRYGDPDVLHFLLSNLNWWVVEYHVDGFHFHSLSSMMYTHNGFASFTGDFEEYCNQYVDRDALMYLILANEILHALHPNIVTIAEDATSY PGLCEPTSQGGLGFDYHVNLAVSEMWLSLLEKNPDQEWSMSKIVSTFIGNRHYADKMLIYAENHNQSISGGQSFAEILFGKISEHSSGSRDLLLRGCSLH KMIRLITFTLCGHAFLNFMGNEFGHP |
Full Sequence |
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Protein Sequence Length: 905 Download |
MSSSLSSLQF KFLHLSPNLA SPHFQPPLPP HQPIDFGRRT KLELRASSSS SSSSASKPPP 60 QRPKKRRSAS DADRGIDPTG FLTKLGISHK GFAQFLRERH KALKDLKDEI FNRHLNLKEM 120 ASGFEILGMH RHVEHRVDYM EWAPGARYCA LVGDFNGWSP TENCAREGHV GHDDYGYWFI 180 ILEDKLREGE KPDELYFQQY NYIDDYDKGD SGLTIEEIFR KANDEYWEPG EDRFVKNRYE 240 LPAKLYEQLF GPNGPQSIEE LGEIPDAETR YRAFKEEHKD DPPGSRPPFD VIDNGKNYDI 300 YNIAGDPVTY EKFKAKKPPI AYWLETRKGR KAWLKKYAPG IPHGSKYRVY FNTPSGPLER 360 VPAWATYVQP DAEGKQAFAI HWEPPPECAY KWKNPSPKVP VSLRIYECHV GISGSEAKVS 420 SFNEFTEKVL PHIKDAGYNA IQLIGVVEHK DYYTVGYRVT NFYAVSSRFG TPDDFKHLVD 480 EAHGLGLLVF LDIVHSYSAA DEMVGLSLFD GSNDCYFHTG KRGQHKYWGT RMFRYGDPDV 540 LHFLLSNLNW WVVEYHVDGF HFHSLSSMMY THNGFASFTG DFEEYCNQYV DRDALMYLIL 600 ANEILHALHP NIVTIAEDAT SYPGLCEPTS QGGLGFDYHV NLAVSEMWLS LLEKNPDQEW 660 SMSKIVSTFI GNRHYADKML IYAENHNQSI SGGQSFAEIL FGKISEHSSG SRDLLLRGCS 720 LHKMIRLITF TLCGHAFLNF MGNEFGHPER VEFPMPSNNF SYSLAKRRWD LLGNGVYQNL 780 FSFDKDMMKL DENERVISRG FPNIHHVNDS SMVISFIRGP LLFVFNFHPT ASYERYVIGV 840 EEAGEYQAIL NTDEKDYGGQ GLIEESQYLQ RTISRRADGL RNCLEVPVPS RTAQVYKLKR 900 ILRI* 960 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02447 | PLN02447 | 8.0e-14 | 90 | 184 | 95 | + 1,4-alpha-glucan-branching enzyme | ||
PLN02960 | PLN02960 | 0 | 71 | 904 | 834 | + alpha-amylase | ||
PLN03244 | PLN03244 | 0 | 71 | 904 | 836 | + alpha-amylase; Provisional | ||
PLN02447 | PLN02447 | 0 | 338 | 896 | 569 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 0 | 386 | 785 | 407 | + 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 | |
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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 | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
DDBJ | BAB02827.1 | 0 | 71 | 904 | 64 | 903 | starch-branching enzyme-like protein [Arabidopsis thaliana] |
EMBL | CBI26672.1 | 0 | 53 | 904 | 45 | 896 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_001154629.1 | 0 | 71 | 904 | 64 | 899 | alpha-amylase/ catalytic/ cation binding [Arabidopsis thaliana] |
RefSeq | XP_002278858.1 | 0 | 53 | 904 | 45 | 866 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002529457.1 | 0 | 1 | 895 | 1 | 892 | 1,4-alpha-glucan branching enzyme, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3amk_A | 0 | 339 | 863 | 114 | 650 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 339 | 863 | 114 | 650 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 339 | 863 | 114 | 650 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
BF272517 | 278 | 360 | 637 | 0 |
JG636329 | 270 | 347 | 616 | 0 |
DY965821 | 293 | 269 | 561 | 0 |
CO104525 | 273 | 387 | 659 | 0 |
EH718768 | 263 | 365 | 627 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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