Basic Information | |
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Species | Phaseolus vulgaris |
Cazyme ID | Phvul.008G033800.1 |
Family | GH13 |
Protein Properties | Length: 964 Molecular Weight: 109039 Isoelectric Point: 5.305 |
Chromosome | Chromosome/Scaffold: 08 Start: 2810430 End: 2821727 |
Description | alpha-amylase-like 3 |
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 | 595 | 878 | 1.6e-36 |
LSHCGVTAVWLPPPTQSVAPQGYMPSDLYNLNSSYGSVEELKYCIEEMHSQDLLALGDVVLNHRCAQQQSPNGVWNIFGGKLAWGPEAIVCDDPNFEGRG NPSSGDIFHAAPNIDHSQDFVRKDIKGWLNWLRNDIGFDGWRLDFVRGFSGTYVKEYIEASNPVFAIGEYWDSLGYEHGSLCYNQDPHRQRIINWINATG GTSSAFDITTKGILHSALHNEYWRLIDPQGKPTGVMGWWPSRAVTFLENHDTGSTQGHWPFPRDKLMQGYAYILTHPGTPAIFY |
Full Sequence |
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Protein Sequence Length: 964 Download |
MGAAMLPDAA FGLFPRCSLV PRHPLICRIT SARLIRKRNY FFADQRISKS AHIVFSHSND 60 SDDTLTDVVV DEDDLSGRSD VIGIEDEIVI AKKALSEAQH REEVFEKERD QLLEELARSE 120 AKNQEYINTI LHDKEVAIAE LEAAKSLFQK KLEDSVEEKF SLESKLVLAK QDAVDLAVQV 180 EKLAEVAFQQ ATSHILEDAQ LRISSAETTA AEAAHLIEKQ IKDATEGTIS SIVEKSSHAI 240 ERALVVAEEA GELAKRSVET FIDGTSAFTE VADVQAENIK LQGIISDIES QLMVARNEAD 300 KLNLELENTR EQLLAFEQRA NDAEKALLDF QESSSKNRLK QEEEMKSMLD KVKKDVAERA 360 KAISKAFKAD LKNIKATVEA AKEVVHSKDY AYLRRCEALQ RSLKASEDTL KTWRQRAEMA 420 ESLLLKGRLQ DEGDEDSIYV VNGGRIDLLT DVDSQKWKLL SDGPRREIPQ WMARRINAVS 480 PKFPPKKVDV AEAFTSKFRS LELPTADEVW SIAREKPKDG DALVEHVYER ETIEKKRKAL 540 ERALQRKTVQ WQRAPEQTTL EPGTGTGREI VFQGFNWESW RRRWYLELAA KTADLSHCGV 600 TAVWLPPPTQ SVAPQGYMPS DLYNLNSSYG SVEELKYCIE EMHSQDLLAL GDVVLNHRCA 660 QQQSPNGVWN IFGGKLAWGP EAIVCDDPNF EGRGNPSSGD IFHAAPNIDH SQDFVRKDIK 720 GWLNWLRNDI GFDGWRLDFV RGFSGTYVKE YIEASNPVFA IGEYWDSLGY EHGSLCYNQD 780 PHRQRIINWI NATGGTSSAF DITTKGILHS ALHNEYWRLI DPQGKPTGVM GWWPSRAVTF 840 LENHDTGSTQ GHWPFPRDKL MQGYAYILTH PGTPAIFYDH FYDFGIHDMI TELIEARRRA 900 GIHCRSSIKI FHANNEGYVS QVGDALVLKL GQFDWNPSKE NQLEGSWQKF VDKGPDYQVW 960 LRQ* |
Functional Domains Download unfiltered results here | ||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
PRK09441 | PRK09441 | 1.0e-44 | 569 | 899 | 419 | + cytoplasmic alpha-amylase; Reviewed |
PLN00196 | PLN00196 | 7.0e-147 | 569 | 960 | 406 | + alpha-amylase; Provisional |
cd11314 | AmyAc_arch_bac_plant_AmyA | 8.0e-167 | 570 | 908 | 343 | + 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. |
PLN02784 | PLN02784 | 0 | 557 | 960 | 406 | + alpha-amylase |
PLN02361 | PLN02361 | 0 | 567 | 960 | 399 | + alpha-amylase |
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 |
EMBL | CBI21221.1 | 0 | 1 | 963 | 1 | 975 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_001782830.1 | 0 | 571 | 962 | 14 | 404 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002276872.1 | 0 | 1 | 956 | 1 | 968 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002324108.1 | 0 | 572 | 963 | 10 | 401 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002526120.1 | 0 | 1 | 963 | 1 | 972 | alpha-amylase, putative [Ricinus communis] |
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 | 3bsg_A | 0 | 568 | 932 | 1 | 378 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
PDB | 2qps_A | 0 | 568 | 932 | 1 | 378 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
PDB | 1rpk_A | 0 | 568 | 932 | 1 | 378 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
PDB | 1p6w_A | 0 | 568 | 932 | 1 | 378 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
PDB | 1ht6_A | 0 | 568 | 932 | 1 | 378 | A Chain A, Crystal Structure At 1.5a Resolution Of The Barley Alpha- Amylase Isozyme 1 |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO795567 | 639 | 326 | 964 | 0 |
HO778903 | 517 | 77 | 593 | 0 |
HO778903 | 105 | 591 | 695 | 0 |
HO785297 | 258 | 574 | 831 | 0 |
HO785297 | 103 | 851 | 953 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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