Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 79072 |
Family | GH13 |
Protein Properties | Length: 504 Molecular Weight: 57543.8 Isoelectric Point: 4.7115 |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 37 | 333 | 7.49695e-43 |
EKAPVIAQAGVTDIWLPPPSQSVDRQGYLPSQLYDLNSSSYGNEAQLKELIDTLHEQGICCIADIVINHRSGWKQDAQGHWNIFEGGTPDKRLDWGPWAV VCNDIYRSGGQGKQDTGESYAAAPDLDHTNKQVQDELTDWLNWMKAEIGFDGWRFDFVKGYAPKYTKLYCQRTDPSFVVGELWTSLNYVSGRLAADQNFH RQQLCDWIDGTGGWGCAFDFTTKGVLQEAVKMELWRLRDKEGRPPGLVGWYPKKAVTFVDNHDTGSTQRHWHFPDEKVHLGYVYILTHPGIPCIFYD |
Full Sequence |
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Protein Sequence Length: 504 Download |
FFLFIDLAIE VFSFLCSSQG FNWESHSKKP WYVDLKEKAP VIAQAGVTDI WLPPPSQSVD 60 RQGYLPSQLY DLNSSSYGNE AQLKELIDTL HEQGICCIAD IVINHRSGWK QDAQGHWNIF 120 EGGTPDKRLD WGPWAVVCND IYRSGGQGKQ DTGESYAAAP DLDHTNKQVQ DELTDWLNWM 180 KAEIGFDGWR FDFVKGYAPK YTKLYCQRTD PSFVVGELWT SLNYVSGRLA ADQNFHRQQL 240 CDWIDGTGGW GCAFDFTTKG VLQEAVKMEL WRLRDKEGRP PGLVGWYPKK AVTFVDNHDT 300 GSTQRHWHFP DEKVHLGYVY ILTHPGIPCI FYDHYFYWGL QEQINQLLEL RLRNKINAES 360 KIKIQAADFD MYVATIADRL IVKLGPRFDM GPLLPKSSTW KLVMAGSEYA IWESTKKMAG 420 VAPSEPEIIV VKSGPSETGD ENIEVKITSD MSCETVNRIM EEVPDMVSNL HDVEKVVEEC 480 KVEYEDEEED EEEEESSKKK SRK* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK09441 | PRK09441 | 6.0e-48 | 19 | 351 | 419 | + cytoplasmic alpha-amylase; Reviewed | ||
PLN02784 | PLN02784 | 2.0e-137 | 12 | 415 | 405 | + alpha-amylase | ||
PLN02361 | PLN02361 | 2.0e-147 | 19 | 413 | 399 | + alpha-amylase | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 3.0e-166 | 19 | 362 | 347 | + 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 | 1.0e-171 | 1 | 413 | 418 | + alpha-amylase; Provisional |
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 | BAA33879.1 | 0 | 1 | 413 | 10 | 420 | alpha-amylase [Phaseolus vulgaris] |
RefSeq | XP_001754460.1 | 0 | 20 | 413 | 1 | 394 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001772280.1 | 0 | 18 | 387 | 3 | 373 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001777583.1 | 0 | 20 | 413 | 16 | 409 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002282184.1 | 0 | 1 | 413 | 12 | 423 | PREDICTED: hypothetical protein [Vitis vinifera] |
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 | 1bg9_A | 0 | 19 | 413 | 5 | 401 | A Chain A, F144yF258Y DOUBLE MUTANT OF EXO-Beta-1,3-Glucanase From Candida Albicans At 2 A |
PDB | 1ava_B | 0 | 19 | 413 | 5 | 401 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1ava_A | 0 | 19 | 413 | 5 | 401 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1amy_A | 0 | 19 | 413 | 5 | 401 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 3bsg_A | 0 | 19 | 419 | 6 | 409 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
starch degradation I | RXN-1823 | EC-3.2.1.1 | α-amylase |
starch degradation I | RXN-1825 | EC-3.2.1.1 | α-amylase |