y
Basic Information | |
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Species | Citrus clementina |
Cazyme ID | Ciclev10030661m |
Family | CBM45 |
Protein Properties | Length: 903 Molecular Weight: 102126 Isoelectric Point: 6.4826 |
Chromosome | Chromosome/Scaffold: 4 Start: 23575399 End: 23582495 |
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 |
CBM45 | 319 | 395 | 1.4e-23 |
VHWGVCRDDSKNWEIPAEPYPPETIVFKNKALRTLLQPKEGGKGCSRLFTVDEEFAGFLFVLKLNENTWLKCMENDF | |||
CBM45 | 128 | 211 | 1.5e-27 |
LHWGVSFVGDNGSEWDQPPKKMRPPGSVSIKDYAIETPLKKLAEGDVFDQVKIDFDTRSDIAAINFVLKDEETGAWYQHRGRDF | |||
GH13 | 533 | 822 | 1.5e-36 |
EKATELSSLGFSVIWLPPPTESVSPEGYMPRDLYNLSSRYGNIDELKDVVNKFHDVGMKILGDVVLNHRCAHYQNQNGVWNIFGGRLNWDDRAVVADDPH FQGRGNKSSGDNFHAAPNIDHSQDFVRKDIKEWLCWLRNEIGYDGWRLDFVRGFWGGYVKDYLEATEPYFAVGEYWDSLSYTYGEMDHNQDAHRQRIIDW INAASGTAGAFDVTTKGILHSALDRCEYWRLSDEKGKPPGVVGWWPSRAVTFIENHDTGSTQGHWRFPGGREMQGYAYILTHPGTPSVFY |
Full Sequence |
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Protein Sequence Length: 903 Download |
MSTVTIRPLL PSYRRANLNF RDRTKILLKP NYINYSIKSA PNARRFCSFK KLQKITASSS 60 TSTSTSTSPA TSTDTTPVRP GDVFFKETFP LKRTHAVEGK IFVRLQKGKD EKNWQLSVGC 120 DIPGKWILHW GVSFVGDNGS EWDQPPKKMR PPGSVSIKDY AIETPLKKLA EGDVFDQVKI 180 DFDTRSDIAA INFVLKDEET GAWYQHRGRD FKVPLVDYLQ HDGNVIGTKS TFGLWPGALG 240 QLSKMILKAD TSQSGIQDSS SESCELKQEN KHLEGFYEEL PIVKEIIIEN TVSVSVRKCP 300 ETAKTLLNLE TDLTGDVVVH WGVCRDDSKN WEIPAEPYPP ETIVFKNKAL RTLLQPKEGG 360 KGCSRLFTVD EEFAGFLFVL KLNENTWLKC MENDFYIPLT SSSCLPAESV QEMLIPGKAE 420 EATQEVSQTA YTAGIIKEIR NLVSDFSSDI SRKTKSKEAQ KSILLEIEKL AAEAYSIFRT 480 SAPTFFEEAA VELEESKPPA KISPGTGTGF EILCQGFNWE SHKSGRWYTE LKEKATELSS 540 LGFSVIWLPP PTESVSPEGY MPRDLYNLSS RYGNIDELKD VVNKFHDVGM KILGDVVLNH 600 RCAHYQNQNG VWNIFGGRLN WDDRAVVADD PHFQGRGNKS SGDNFHAAPN IDHSQDFVRK 660 DIKEWLCWLR NEIGYDGWRL DFVRGFWGGY VKDYLEATEP YFAVGEYWDS LSYTYGEMDH 720 NQDAHRQRII DWINAASGTA GAFDVTTKGI LHSALDRCEY WRLSDEKGKP PGVVGWWPSR 780 AVTFIENHDT GSTQGHWRFP GGREMQGYAY ILTHPGTPSV FYDHIFSHYR QEIEALLSVR 840 KRNKIHCRSR VEIVKAERDV YAAIIDEKVA MKLGPGHYEP PSGSQNWCFV TEGRDYKVWE 900 AA* 960 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK09441 | PRK09441 | 4.0e-50 | 511 | 842 | 416 | + cytoplasmic alpha-amylase; Reviewed | ||
PLN00196 | PLN00196 | 6.0e-136 | 511 | 902 | 409 | + alpha-amylase; Provisional | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 1.0e-164 | 512 | 851 | 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. | ||
PLN02361 | PLN02361 | 4.0e-168 | 509 | 900 | 398 | + alpha-amylase | ||
PLN02784 | PLN02784 | 0 | 1 | 902 | 903 | + 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 |
GenBank | AAX33231.1 | 0 | 1 | 902 | 1 | 901 | plastid alpha-amylase [Malus x domestica] |
GenBank | AAX33233.1 | 0 | 1 | 902 | 1 | 895 | plastid alpha-amylase [Actinidia chinensis] |
EMBL | CBI32016.1 | 0 | 1 | 902 | 1 | 885 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002270049.1 | 0 | 1 | 902 | 1 | 901 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002520134.1 | 0 | 1 | 902 | 1 | 900 | 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 | 2qpu_C | 0 | 511 | 900 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_B | 0 | 511 | 900 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_A | 0 | 511 | 900 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 3bsg_A | 0 | 511 | 900 | 2 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
PDB | 1rpk_A | 0 | 511 | 900 | 2 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
EG631183 | 911 | 1 | 903 | 0 |
HO826981 | 407 | 497 | 903 | 0 |
DR932783 | 288 | 511 | 798 | 0 |
ES805448 | 328 | 468 | 795 | 0 |
HO826981 | 30 | 466 | 495 | 0.36 |
Sequence Alignments (This image is cropped. Click for full image.) |
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