| Basic Information | |
|---|---|
| Species | Carica papaya |
| Cazyme ID | evm.model.supercontig_14.168 |
| Family | GH13 |
| Protein Properties | Length: 801 Molecular Weight: 90167.7 Isoelectric Point: 5.7395 |
| Chromosome | Chromosome/Scaffold: 14 Start: 1947685 End: 1958803 |
| Description | alpha-amylase-like 3 |
| 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 | 603 | 793 | 1.4e-25 |
| ADLSHCGVTAVWLPPPTESVAPQGYMPSDLYNLNSAYGSEEELKYCIEEMHSQNLLALGDVVLNHRCAHKQSPNGIWNIFGGKLAWGPEAIVCDDPNFQG QGNPSNGDIFHAAPNIDHSQDFVRKDITEWLNWLRNYIGFDGWRLDFVRGFSGTYVKEYIEASNPAFAIGEYWDSLAYEHGDLCYNQGNHL | |||
| Full Sequence |
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| Protein Sequence Length: 801 Download |
| MGVMLMSGLT SGILPFRPVV SSVKRRGRVS DLHNGHSLLS SGGPSRVKRK FLHNENWKPK 60 SRAIVFSTDD STDAFADGYG DGYSSSRSGV LRKIEDELTE VKKALSEAQA RQGSIEQERN 120 QLLDELARAE VKQQEYVAAI LHDKEIAIAE LEAAKSLFHQ KLQASVEEKF ALESKLVLAK 180 QDAVELAVQV EKLAEIAFQQ TTSQILEDAR MRVSAAETSA AEAAYQIEEQ IRNATEGTIL 240 SIVEQSKNAI EKVLDVAEKA GDHATKAVAI FSDSLNPLDE IASLQQEKTK LQRVIGDLES 300 ELLLKRSEVD MLKLELEQAH AQVNAFELRA NDTEKALREF QESSTKKILQ QEEGIKSVVE 360 KMKKDAATRK KAMYKAFKTE MESVRATIEA VKETARLKDN ASIRRCDALQ RSLRASEAAS 420 KTWRQRAEKA ESLLTKDGLV DGEDRDAIYV VNGGRIDLLT DDDSLKWKLL SDGPRREIPQ 480 WMARKIRAIC PKFPPRKVNA LEVLTSKFQT LDSPSVDEVW SIAQEKPKEG DTFIEHVIEK 540 ETIEKKRKTL EQTLQRNTIQ WQRTLEQTKL ESGTGTGREI VFQGFNWESW RRQWYLDLAS 600 KTADLSHCGV TAVWLPPPTE SVAPQGYMPS DLYNLNSAYG SEEELKYCIE EMHSQNLLAL 660 GDVVLNHRCA HKQSPNGIWN IFGGKLAWGP EAIVCDDPNF QGQGNPSNGD IFHAAPNIDH 720 SQDFVRKDIT EWLNWLRNYI GFDGWRLDFV RGFSGTYVKE YIEASNPAFA IGEYWDSLAY 780 EHGDLCYNQG NHLAVFRFNR * |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| smart00642 | Aamy | 3.0e-17 | 579 | 670 | 98 | + Alpha-amylase domain. | ||
| PLN00196 | PLN00196 | 1.0e-69 | 570 | 792 | 233 | + alpha-amylase; Provisional | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 9.0e-81 | 580 | 798 | 230 | + 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. | ||
| PLN02361 | PLN02361 | 5.0e-83 | 577 | 792 | 219 | + alpha-amylase | ||
| PLN02784 | PLN02784 | 2.0e-113 | 567 | 792 | 227 | + alpha-amylase | ||
| 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 |
| EMBL | CBI21221.1 | 0 | 1 | 792 | 1 | 794 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_001768202.1 | 0 | 582 | 792 | 1 | 211 | predicted protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_002276872.1 | 0 | 1 | 792 | 1 | 794 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002324108.1 | 0 | 582 | 792 | 10 | 220 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002526120.1 | 0 | 1 | 792 | 1 | 791 | 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 | 579 | 780 | 1 | 211 | A Chain A, Structure Of Rabbit Muscle Glycogen Phosphorylase In Complex With Ligand |
| PDB | 1ava_B | 0 | 579 | 780 | 1 | 211 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 1ava_A | 0 | 579 | 780 | 1 | 211 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 1amy_A | 0 | 579 | 780 | 1 | 211 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 3bsg_A | 0 | 578 | 779 | 1 | 211 | 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 |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
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| Hit | Length | Start | End | EValue |
| HO795567 | 457 | 336 | 792 | 0 |
| HO778903 | 510 | 94 | 603 | 0 |
| HO778903 | 105 | 601 | 705 | 0 |
| CF210524 | 300 | 448 | 747 | 0 |
| CO484505 | 282 | 511 | 792 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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