y
Basic Information | |
---|---|
Species | Thellungiella halophila |
Cazyme ID | Thhalv10020019m |
Family | GH13 |
Protein Properties | Length: 898 Molecular Weight: 103035 Isoelectric Point: 6.2222 |
Chromosome | Chromosome/Scaffold: 13 Start: 2055133 End: 2062691 |
Description | Alpha amylase family protein |
View CDS |
External Links |
---|
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
GH13 | 418 | 741 | 5.6e-25 |
FTKKVLPHVKRAGYNAIQLIGIPEHKDYFTVGYRVTNFFAVSSRYGTPDDFKRLIDEAHGLGLLVFLDIVHSYAAADQMVGLSLFDGSNDCYFHYGKRGH HKHWGTRMFKYGDLDVLHFLISNLNWWITEYQVDGYQFHSLASMIYTHNGFASFNSGLDDYCNQYVDRDALMYLILANEILHVQHPNIITIAEDATYYPG LCDSVSQGGLGFDYYVNLSATDMWVSLLDSVPDNEWSMSKIVSTLVANKEYADKMLTYAESHNQSISGGRSFAEILFGGVENGSPGGRELLDRGVSLHKM IRLITFTIGGRAYLNFMGNEFGHP |
Full Sequence |
---|
Protein Sequence Length: 898 Download |
MVSLSNQTRF SFYPNNLFVS EKRLLGISGI NFPRKISVRI TCFAADQPRQ KKQKKKSQST 60 SDAEAGVDPV GFLTKLGIAD RIFAQFLRER HKALKDLKDE ILKRHFDLKD FASGFELLGM 120 HRHMEHRVDF MDWGPGARYG AIIGDFNGWS PTENSAREGL FGHDDYGYWF IILEDKLREG 180 EEPDELYFQQ YNYVDDYDKG DSGVSAEELF QKANDEYWEP GEDRFIKNRY EVPAKLYEQL 240 FGPNGPQTLE ELGDIPDAET RYKQYKEEHK NDPPSNLPPC DIIDKGQGKP YDIFNVVTSP 300 EWTKKFYEKE PPIPYWLETR KGRKAWLEKY IPAVPHGSKY RLYFNTPDGP LERVPAWATY 360 VQPEDEGKQA YAIHWEPSPE SAYKWKYSKP DKPKSLRIYE CHVGISGSEP KISSFEEFTK 420 KVLPHVKRAG YNAIQLIGIP EHKDYFTVGY RVTNFFAVSS RYGTPDDFKR LIDEAHGLGL 480 LVFLDIVHSY AAADQMVGLS LFDGSNDCYF HYGKRGHHKH WGTRMFKYGD LDVLHFLISN 540 LNWWITEYQV DGYQFHSLAS MIYTHNGFAS FNSGLDDYCN QYVDRDALMY LILANEILHV 600 QHPNIITIAE DATYYPGLCD SVSQGGLGFD YYVNLSATDM WVSLLDSVPD NEWSMSKIVS 660 TLVANKEYAD KMLTYAESHN QSISGGRSFA EILFGGVENG SPGGRELLDR GVSLHKMIRL 720 ITFTIGGRAY LNFMGNEFGH PERVEFPTQS NNFSFSLANR RWDLLESGIH HQLFSFDKEL 780 MDLDKSKGIL SRGLPSIHHV NDANMVISFS RGPFLFVFNF HPSSSYEKYN VGVEEAGEYT 840 MILNSDEVKF GGQGLLTENQ YLQRSISKRM DGQRNALEVF LPSRTAQVYK LTRILRI* 900 |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02447 | PLN02447 | 3.0e-11 | 83 | 175 | 93 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 1.0e-176 | 379 | 778 | 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. | ||
PLN02960 | PLN02960 | 0 | 1 | 897 | 899 | + alpha-amylase | ||
PLN03244 | PLN03244 | 0 | 1 | 897 | 902 | + alpha-amylase; Provisional | ||
PLN02447 | PLN02447 | 0 | 332 | 889 | 569 | + 1,4-alpha-glucan-branching enzyme |
Gene Ontology | |
---|---|
GO Term | Description |
GO:0003824 | catalytic activity |
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 |
DDBJ | BAB02827.1 | 0 | 1 | 897 | 1 | 903 | starch-branching enzyme-like protein [Arabidopsis thaliana] |
EMBL | CBI26672.1 | 0 | 1 | 897 | 1 | 896 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_001154629.1 | 0 | 1 | 897 | 1 | 899 | alpha-amylase/ catalytic/ cation binding [Arabidopsis thaliana] |
RefSeq | NP_188679.2 | 0 | 1 | 897 | 1 | 869 | alpha-amylase/ catalytic/ cation binding [Arabidopsis thaliana] |
RefSeq | XP_002529457.1 | 0 | 4 | 888 | 5 | 892 | 1,4-alpha-glucan branching enzyme, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3amk_A | 0 | 332 | 889 | 114 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 332 | 889 | 114 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 332 | 889 | 114 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
EST Download unfiltered results here | ||||
---|---|---|---|---|
Hit | Length | Start | End | EValue |
BF272517 | 278 | 353 | 630 | 0 |
DK500153 | 271 | 1 | 268 | 0 |
DY965821 | 295 | 260 | 554 | 0 |
CO104525 | 273 | 380 | 652 | 0 |
JG636329 | 270 | 340 | 609 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
---|