| Basic Information | |
|---|---|
| Species | Carica papaya |
| Cazyme ID | evm.model.supercontig_49.17 |
| Family | GH13 |
| Protein Properties | Length: 424 Molecular Weight: 47156.4 Isoelectric Point: 5.6183 |
| Chromosome | Chromosome/Scaffold: 49 Start: 77075 End: 78561 |
| Description | alpha-amylase-like |
| 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 | 52 | 341 | 3.9e-37 |
| DIANAGITHVWLPPPSNSGADAPQGYKPAKLYDLNSNYGTRDQLSSLIAAYHQSGIKCMADIVINHRSPERQTETDIFFEGGTPDDRLDWGPAMVCSTDK NFPHGTGNPDTGDDFPFAIDIDHTNPRVQNELSDWLNWLKTEVGFNGGWRIDYAVGFAPSITKIYVDRTKPDLAVAEYWHPPCNEKLPPGDNRKRDELRK WIQDAGGVVAAFDFPLKESLQVAVTGELFRLNNTDGKPPGLLGVLPEKAVTFIDNHDTWSQDFCKFPSDKVMLGYVYILTHPGTPTIFYD | |||
| Full Sequence |
|---|
| Protein Sequence Length: 424 Download |
| MSSVITSLCF LFLLSSIFPA FVSPAVLFQG FTWASSEKRG ELYNFLKNSA TDIANAGITH 60 VWLPPPSNSG ADAPQGYKPA KLYDLNSNYG TRDQLSSLIA AYHQSGIKCM ADIVINHRSP 120 ERQTETDIFF EGGTPDDRLD WGPAMVCSTD KNFPHGTGNP DTGDDFPFAI DIDHTNPRVQ 180 NELSDWLNWL KTEVGFNGGW RIDYAVGFAP SITKIYVDRT KPDLAVAEYW HPPCNEKLPP 240 GDNRKRDELR KWIQDAGGVV AAFDFPLKES LQVAVTGELF RLNNTDGKPP GLLGVLPEKA 300 VTFIDNHDTW SQDFCKFPSD KVMLGYVYIL THPGTPTIFY DHYFEWGLKE PITNILAIRK 360 KHGINERSRV KILAAQSDLY VAEIDEKIIM KIGPNGGLGN LIPPNFKLVP NGAGKDYAVW 420 EKI* |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK09441 | PRK09441 | 3.0e-50 | 26 | 362 | 415 | + cytoplasmic alpha-amylase; Reviewed | ||
| PLN02784 | PLN02784 | 3.0e-99 | 26 | 422 | 403 | + alpha-amylase | ||
| PLN02361 | PLN02361 | 4.0e-112 | 26 | 422 | 405 | + alpha-amylase | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 1.0e-132 | 26 | 370 | 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-156 | 26 | 423 | 408 | + alpha-amylase; Provisional | ||
| Gene Ontology | |
|---|---|
| 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 | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PRF/SEQDB | 0 | 5 | 421 | 4 | 421 | UP10_LACSN Unknown protein 10 from 2D-PAGE | |
| DDBJ | BAA33879.1 | 0 | 5 | 421 | 4 | 420 | alpha-amylase [Phaseolus vulgaris] |
| DDBJ | BAC76729.1 | 0 | 5 | 421 | 4 | 421 | alpha-amylase [Vigna angularis] |
| RefSeq | XP_002327139.1 | 0 | 7 | 422 | 5 | 423 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002510218.1 | 0 | 5 | 422 | 1 | 420 | alpha-amylase, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1bg9_A | 0 | 26 | 423 | 2 | 403 | A Chain A, Barley 1,3-1,4-Beta-Glucanase In Monoclinic Space Group |
| PDB | 1ava_B | 0 | 26 | 423 | 2 | 403 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 1ava_A | 0 | 26 | 423 | 2 | 403 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 1amy_A | 0 | 26 | 423 | 2 | 403 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 3bsg_A | 0 | 26 | 422 | 3 | 404 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| Metabolic Pathways | |||
|---|---|---|---|
| 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 |
