Basic Information | |
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Species | Thellungiella halophila |
Cazyme ID | Thhalv10025232m |
Family | GH13 |
Protein Properties | Length: 438 Molecular Weight: 48669 Isoelectric Point: 5.2985 |
Chromosome | Chromosome/Scaffold: 1 Start: 6406427 End: 6408075 |
Description | alpha-amylase-like |
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 | 41 | 349 | 6.44597e-44 |
QEGGFYNSLQNSIDDISNSGITHIWLPPPSQSVSPEGYLPGKLYDLNSSKYGSETELKSLIAALNQRGIKSVADIVINHRTGERKDDHCGYCYFEGGTSD GRLDWDPSFVCRDDPKFPGTGNSDTGKDFDGAPDIDHLNPRVQKELSEWMNWLKSEIGFSGWRFDFVRGYAPSITKSYVKNTSPEFAVGEKWDDMKYGGD GKPEYDQDEHRSALRHWIEEAGGGGGVLTAFDFTTKGILQSAVGGELWRLKDSQGKPPGLIGIMPGNAVTFVDNHDTIRPNTWAFPSDKVLLGYVYILTH PGTPCIFYS |
Full Sequence |
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Protein Sequence Length: 438 Download |
MTCLNETLLL SCLLAFLVFF PTFTFSTLLL FQGFKWESWK QEGGFYNSLQ NSIDDISNSG 60 ITHIWLPPPS QSVSPEGYLP GKLYDLNSSK YGSETELKSL IAALNQRGIK SVADIVINHR 120 TGERKDDHCG YCYFEGGTSD GRLDWDPSFV CRDDPKFPGT GNSDTGKDFD GAPDIDHLNP 180 RVQKELSEWM NWLKSEIGFS GWRFDFVRGY APSITKSYVK NTSPEFAVGE KWDDMKYGGD 240 GKPEYDQDEH RSALRHWIEE AGGGGGVLTA FDFTTKGILQ SAVGGELWRL KDSQGKPPGL 300 IGIMPGNAVT FVDNHDTIRP NTWAFPSDKV LLGYVYILTH PGTPCIFYSH YMEWGLKDSI 360 TKLVAIRKRN GIGSTSSVTI KAAESDLYLA VIDDKVIMKI GPKMDLGTLV PSNYALAYSG 420 LDCAVWEKQL RNYSISL* |
Functional Domains Download unfiltered results here | ||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
PRK09441 | PRK09441 | 3.0e-45 | 32 | 376 | 418 | + cytoplasmic alpha-amylase; Reviewed |
PLN02784 | PLN02784 | 3.0e-123 | 32 | 428 | 399 | + alpha-amylase |
PLN02361 | PLN02361 | 2.0e-138 | 32 | 428 | 403 | + alpha-amylase |
cd11314 | AmyAc_arch_bac_plant_AmyA | 2.0e-153 | 32 | 378 | 351 | + Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes AmyA from bacteria, archaea, water fleas, and plants. 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. |
PLN00196 | PLN00196 | 0 | 32 | 428 | 399 | + alpha-amylase; Provisional |
Gene Ontology | |
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GO Term | Description |
GO:0003824 | catalytic activity |
GO:0004556 | alpha-amylase activity |
GO:0005509 | calcium ion binding |
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 |
PRF/SEQDB | 0 | 10 | 427 | 7 | 421 | UP10_LACSN Unknown protein 10 from 2D-PAGE | |
GenBank | AAM64582.1 | 0 | 1 | 429 | 1 | 423 | alpha-amylase-like protein [Arabidopsis thaliana] |
DDBJ | BAC02435.1 | 0 | 4 | 430 | 1 | 424 | alpha-amylase [Ipomoea nil] |
EMBL | CAB36742.1 | 0 | 1 | 429 | 1 | 428 | alpha-amylase-like protein [Arabidopsis thaliana] |
RefSeq | NP_567714.1 | 0 | 1 | 429 | 1 | 423 | AMY1 (ALPHA-AMYLASE-LIKE); alpha-amylase [Arabidopsis thaliana] |
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 | 2qpu_C | 0 | 29 | 429 | 3 | 405 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_B | 0 | 29 | 429 | 3 | 405 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_A | 0 | 29 | 429 | 3 | 405 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 3bsg_A | 0 | 29 | 429 | 3 | 405 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
PDB | 2qps_A | 0 | 29 | 429 | 3 | 405 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |