y
Basic Information | |
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Species | Mimulus guttatus |
Cazyme ID | mgv1a001162m |
Family | GH13 |
Protein Properties | Length: 875 Molecular Weight: 100620 Isoelectric Point: 6.4163 |
Chromosome | Chromosome/Scaffold: 24 Start: 527242 End: 534984 |
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 | 429 | 751 | 1.9e-23 |
TFNEFTDNVLAHVKKAGYNAIQLFGVVEHKDYFTAGYRVTNFFAVSSRFGTPEDFKRLVDEAHGLGLLVFLDIVHSYAAPDEMVGLSSFDGLNDCYFHSG KRGQHKFWGTRMFKYEDHEVLHFLLSNLNWWITEYQVDGFYFHSLPSMMYTHNGFATFTGDVEEYCNQYVDRDAMLYLIFANEMLHFLHPNIITIAEDAT LYPGLCEPTSQGGLGFDYYANISASELWLSFLENVPEHEWSMSKLVSTLVGNKYSAAKMLLYAENHNQSISGGRSFAEILFGSAKTDEALLRGCSLHKMI RLITFTIGGPAYLNFMGNEFGHP |
Full Sequence |
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Protein Sequence Length: 875 Download |
MISLTHSLQI SSFPIKSPIS NTNCAAHRCG GRVFLRRTNG NKCRYKGKCF AAEQPQSQPE 60 VSQQKSKRPR KKTPEIDKKK NAVDPVGFLT KHEINNKAFN HFLRERYKAL KDLKEELSNR 120 HYEVQDLASG YEILGMHRNV QHRVDFMDWA PGARYCALVG DFNRWSPTEN SAREGNLGHD 180 DYGYWFIILE DKLREGEEPD QVYFQQYNYV DEYDKGDSGV TVEEIFKKAN DEYWEPGEDR 240 FTKSPYELAS KLYEQIFGPN GPQTEEEMEE ILDPQTRYNE WREKHKDDPP SNLPPCDVII 300 DDGTEDEEFD VVTDPAWKAK FKAKQAPIAY WLETRKGRKA WLEKYLPGIP HGSKYRVYFN 360 TPMGPLERVP AWATYVIPEA DGNQSFAVHW EPTPEIAHKW RHKHPPKPKS LRIYECHVGI 420 SGMDPRIATF NEFTDNVLAH VKKAGYNAIQ LFGVVEHKDY FTAGYRVTNF FAVSSRFGTP 480 EDFKRLVDEA HGLGLLVFLD IVHSYAAPDE MVGLSSFDGL NDCYFHSGKR GQHKFWGTRM 540 FKYEDHEVLH FLLSNLNWWI TEYQVDGFYF HSLPSMMYTH NGFATFTGDV EEYCNQYVDR 600 DAMLYLIFAN EMLHFLHPNI ITIAEDATLY PGLCEPTSQG GLGFDYYANI SASELWLSFL 660 ENVPEHEWSM SKLVSTLVGN KYSAAKMLLY AENHNQSISG GRSFAEILFG SAKTDEALLR 720 GCSLHKMIRL ITFTIGGPAY LNFMGNEFGH PKDMMKLDID GKIMQRGSGG IPNVHHVKDK 780 EMVISYLRGP FVFVFNFHPT NSYERYSLGV EEAGEYQIVL NTDEEIYGGQ GLISQDQYTQ 840 RTISRRTDGM RVCLEVPLPS RTAQVYKLTR IRRA* 900 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02447 | PLN02447 | 3.0e-12 | 99 | 191 | 93 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 2.0e-151 | 410 | 751 | 352 | + 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. | ||
PLN02447 | PLN02447 | 7.0e-177 | 347 | 866 | 574 | + 1,4-alpha-glucan-branching enzyme | ||
PLN02960 | PLN02960 | 0 | 1 | 874 | 927 | + alpha-amylase | ||
PLN03244 | PLN03244 | 0 | 1 | 873 | 922 | + alpha-amylase; Provisional |
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 | 1 | 873 | 1 | 902 | starch-branching enzyme-like protein [Arabidopsis thaliana] |
EMBL | CBI26672.1 | 0 | 1 | 873 | 1 | 895 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_001154629.1 | 0 | 1 | 873 | 1 | 898 | alpha-amylase/ catalytic/ cation binding [Arabidopsis thaliana] |
RefSeq | XP_002278858.1 | 0 | 1 | 873 | 1 | 865 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002529457.1 | 0 | 4 | 865 | 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 | 347 | 836 | 114 | 653 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3aml_A | 0 | 347 | 836 | 114 | 653 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 347 | 836 | 114 | 653 | 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 |
GO947396 | 242 | 303 | 544 | 0 |
DY965821 | 293 | 276 | 568 | 0 |
CO104525 | 258 | 410 | 667 | 0 |
BF272517 | 278 | 368 | 645 | 0 |
GO947396 | 17 | 545 | 561 | 0.14 |
Sequence Alignments (This image is cropped. Click for full image.) |
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