Basic Information | |
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Species | Malus domestica |
Cazyme ID | MDP0000258604 |
Family | GH13 |
Protein Properties | Length: 1661 Molecular Weight: 187617 Isoelectric Point: 8.026 |
Chromosome | Chromosome/Scaffold: 009118352 Start: 25731 End: 34313 |
Description | ERD (early-responsive to dehydration stress) family protein |
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 | 1170 | 1498 | 2.2e-29 |
NIAGTFSGLTEKLEHLKHLGVNAVLLEPIFPFDEQKGPYFPIHFFSPMNWFGPSRGPVSAVNSMKDMVKKFHADGIEVLLEVVFTHTAEGEALQGIDISS YYHINGVADLKARNALNCNYPVVQQMVLDSLRYWVTEFHVDGFCFINASSLMRGSKGEYLSRPPLVEAIAFDPLLSKTKIIADRWDPHGSVPKETRFPHW KRWAEVNSKFSKDVRNFLRGEGLLSDLATRLCGNGDIFSDGRGPAFAFNFISRNSGLPLVDLVSFSGVKLASELSWNCGEEGPTDKTAVLERRLKQIRNF LFILFVSLGVPVLNMGDECGQSTGGSPAY |
Full Sequence |
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Protein Sequence Length: 1661 Download |
MANFQDIMMS AAINILSAFG FLVAFGLLRL QPFNDRVYFP KWYLKGMRGS PTSSGATVRK 60 FVNLDAKTYF KFLNWMPAAL RMPEPELIDH AGLDSAAYIR IYVLGLKIFV PITALALGVL 120 VPVNYMSNTL ERSREVVFSD IDKLSISNIP SGSPKFFAHL VMSYVFTFWT CFVLYHEYKT 180 VATKRLQFLA SEKRRPDQFT VLVRNVPPDP DESVSEHIEH FFCVNHPGHY LTHQVSELLN 240 LVVYNANKLA QVVDKKKSTK NWLVYYQNKF ERNPKTKPTT KTGFLGLWGD RVDAIDYYND 300 TIKKLVEEEK QEREKVISDP DAIMPAAFVS FKTRWGAAVC AQTQQSRNPT IWLTEWAPEP 360 RDIYWNNLAI PYVELNVRKL LMGVAFFFLT FFFMIPIAFV QSLANIEGIQ KALPFLKPLL 420 QISSVKSVVQ GFLPGIALKI FLAILPMILM LMSKIEGLTS LSHLDRRSAA KYHLFILINV 480 FLGSIVTGTA LQQLEKLMNE PSTEFTKTVG RSIPMKGTFF ITYVMVDGWS GIAAEILRLV 540 PLILFHLKNT FLVKTEQDRE QATDPGSLNF ATNEPRTQLY FLLGLVYSVV TPILLPFILI 600 FFAFAYVVYR HQIINVYDQK YESGAAFWPQ VHLRVIIGLI IAQVLLMGLF STLGVAKSTF 660 ILIPQPILTL WFHRVCKGRF ESAFLKFPLQ EAMVKDTVER ATEPNLNLLN YLKDAYVHPV 720 FKGGQMQNHE VDVDEEESSP LVVTKRTSQM GSKHESDAGP EIRTIHRVIW KKFLNNASGH 780 LSRRPSCLRS RMATLPLSIA MQASCCLNCG TTELSKLTAA NRYRHRHNGL RGSVKLGIER 840 NLVFGEVVQN FKETPLRDRD LKVYATSRVS VEPMEQRVYT STETEEAGKV STYRFRTETG 900 DMVKVFVRMK NAKCIVNIEV SSLHLSSNDR LLVLSWGIYR SDSSSFMPSN FRSSTPADRT 960 TTLETPFTET CSGRFTLELE FEAKQIPFYL SFILKSPADA DSSDLDIRSH RKTNFCFPVG 1020 FGRGYPAPLG LSFSNDGSMN FAIFSRNAES VVLCLYGETT AEKPVLELDL DPYVNRSGDI 1080 WHASFESGWD FVSYGYRFDE GNVLLDPYAK IISRSVPHGT GLKYLGRLCE EPAFNWAGDV 1140 RPDLAMEKLV VYRLNVTRFT EHKSSNLPTN IAGTFSGLTE KLEHLKHLGV NAVLLEPIFP 1200 FDEQKGPYFP IHFFSPMNWF GPSRGPVSAV NSMKDMVKKF HADGIEVLLE VVFTHTAEGE 1260 ALQGIDISSY YHINGVADLK ARNALNCNYP VVQQMVLDSL RYWVTEFHVD GFCFINASSL 1320 MRGSKGEYLS RPPLVEAIAF DPLLSKTKII ADRWDPHGSV PKETRFPHWK RWAEVNSKFS 1380 KDVRNFLRGE GLLSDLATRL CGNGDIFSDG RGPAFAFNFI SRNSGLPLVD LVSFSGVKLA 1440 SELSWNCGEE GPTDKTAVLE RRLKQIRNFL FILFVSLGVP VLNMGDECGQ STGGSPAYSD 1500 RKAFDWNALG TGFATQTTQF IAFLSSFRIR RSDLLQERNF LKEENIDWYG SDQSSPKWED 1560 PSCKFLAMKL KPDEEEATEP GDVSPPIWGD LFVAFSAAAR SETVILPPPP EGMGWFRLVD 1620 TALPFPGFFS TDGEPVPEQM AGLFAYQMKS HSCALFEARC L |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam02714 | DUF221 | 2.0e-108 | 327 | 650 | 326 | + Domain of unknown function DUF221. This family consists of hypothetical transmembrane proteins none of which have any function, the aligned region is at 538 residues at maximum length. | ||
COG1523 | PulA | 2.0e-111 | 1024 | 1624 | 691 | + Type II secretory pathway, pullulanase PulA and related glycosidases [Carbohydrate transport and metabolism] | ||
TIGR02100 | glgX_debranch | 2.0e-115 | 1024 | 1626 | 694 | + glycogen debranching enzyme GlgX. This family consists of the GlgX protein from the E. coli glycogen operon and probable equivalogs from other prokaryotic species. GlgX is not required for glycogen biosynthesis, but instead acts as a debranching enzyme for glycogen catabolism. This model distinguishes GlgX from pullanases and other related proteins that also operate on alpha-1,6-glycosidic linkages. In the wide band between the trusted and noise cutoffs are functionally similar enzymes, mostly from plants, that act similarly but usually are termed isoamylase [Energy metabolism, Biosynthesis and degradation of polysaccharides]. | ||
cd11326 | AmyAc_Glg_debranch | 4.0e-118 | 1134 | 1528 | 436 | + Alpha amylase catalytic domain found in glycogen debranching enzymes. Debranching enzymes facilitate the breakdown of glycogen through glucosyltransferase and glucosidase activity. These activities are performed by a single enzyme in mammals, yeast, and some bacteria, but by two distinct enzymes in Escherichia coli and other bacteria. Debranching enzymes perform two activities: 4-alpha-D-glucanotransferase (EC 2.4.1.25) and amylo-1,6-glucosidase (EC 3.2.1.33). 4-alpha-D-glucanotransferase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. Amylo-alpha-1,6-glucosidase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. In Escherichia coli, GlgX is the debranching enzyme and malQ is the 4-alpha-glucanotransferase. TreX, an archaeal glycogen-debranching enzyme has dual activities like mammals and yeast, but is structurally similar to GlgX. TreX exists in two oligomeric states, a dimer and tetramer. Isoamylase (EC 3.2.1.68) is one of the starch-debranching enzymes that catalyzes the hydrolysis of alpha-1,6-glucosidic linkages specific in alpha-glucans such as amylopectin or glycogen and their beta-limit dextrins. 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. | ||
cd11346 | AmyAc_plant_IsoA | 1.0e-135 | 1147 | 1536 | 403 | + Alpha amylase catalytic domain family found in plant isoamylases. Two types of debranching enzymes exist in plants: isoamylase-type (EC 3.2.1.68) and a pullulanase-type (EC 3.2.1.41, also known as limit-dextrinase). These efficiently hydrolyze alpha-(1,6)-linkages in amylopectin and pullulan. This group does not contain the conserved catalytic triad present in other alpha-amylase-like proteins. 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. |
Gene Ontology | |
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GO Term | Description |
GO:0003824 | catalytic activity |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0005975 | carbohydrate metabolic process |
GO:0016020 | membrane |
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 | AAN15318.1 | 0 | 792 | 1661 | 1 | 859 | isoamylase isoform 2 [Solanum tuberosum] |
DDBJ | BAF52942.1 | 0 | 856 | 1658 | 49 | 860 | isoamylase-type starch-debranching enzyme 2 [Phaseolus vulgaris] |
RefSeq | NP_192199.1 | 0 | 1 | 805 | 1 | 785 | early-responsive to dehydration protein-related / ERD protein-related [Arabidopsis thaliana] |
RefSeq | XP_002271798.1 | 0 | 792 | 1661 | 1 | 880 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002533079.1 | 0 | 792 | 1658 | 1 | 867 | isoamylase, 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 | 2vuy_B | 0 | 1024 | 1531 | 15 | 598 | A Chain A, Solution Structure Of The Inner Dysf Domain Of Human Myoferlin |
PDB | 2vuy_A | 0 | 1024 | 1531 | 15 | 598 | A Chain A, Solution Structure Of The Inner Dysf Domain Of Human Myoferlin |
PDB | 2vr5_B | 0 | 1024 | 1531 | 15 | 598 | A Chain A, Solution Structure Of The Inner Dysf Domain Of Human Myoferlin |
PDB | 2vr5_A | 0 | 1024 | 1531 | 15 | 598 | A Chain A, Solution Structure Of The Inner Dysf Domain Of Human Myoferlin |
PDB | 2vnc_B | 0 | 1024 | 1531 | 15 | 598 | A Chain A, Crystal Structure Of Glycogen Debranching Enzyme Trex From Sulfolobus Solfataricus |