y
Basic Information | |
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Species | Ricinus communis |
Cazyme ID | 29475.m000230 |
Family | GH13 |
Protein Properties | Length: 964 Molecular Weight: 107483 Isoelectric Point: 6.7765 |
Chromosome | Chromosome/Scaffold: 29475 Start: 31008 End: 44589 |
Description | limit dextrinase |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 372 | 772 | 5.4e-32 |
HLKKLSNAGITHVHLLPTFQFAGVDDVKENWKCVDNKMLETLLPDSIEQQAQITAVQDNDGYNWGYNPVLWGVPKGSYASNPNGPSRTIQFRKMVQALNR IGLRVVLDVVYNHLHGSGPFDENSVLDKIVPGYYLRRNIDGIIENSTCVNNTASEHYMVERLIIDDLLNWAVNYKVDGFRFDLMGHLMKSTMVKAKIALH SLSVERDGVDGSSLYIYGEGWDFGEVAKNGRGVNASQFNLYGTGIGSFNDRIRDAMLGGSPFGHPLHQGFVTGLMLQPNGHDHGGKDVEELMLTTAKDHI QVGMAANLRDFVLINSEGKEVKGSEITTYGGEPVAYALSPTETINYVSAHDNETLFDIVSMKTPMEISVDERCRLNHLATSIIALSQGIPFFHAGDEMLR S |
Full Sequence |
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Protein Sequence Length: 964 Download |
MSLLFSFQAL PLVPSLTITG ISSSSLPYGL PHRFNPKLNN DNSHRQLLYR SSNPKTSFKY 60 PIRCSSSSMP LQELSTSTSQ FQDSLLYSRA FWVSKTIIAW NVDVGDNGSC FLYASDTGSL 120 SVSNAGIQGH DVEVKLEKYN GGLPENVVVK FPHIRDYRAF KAPPTLDAKS LLKCQLAVAS 180 YEADGKCRSA TGLQLPGILD ELYSYDGPLG AHYSKNAVSL HLWAPTAQAV LVYIYKDSFS 240 KVPLEIHQLK EVNGVWSIKG PKDWEGCYYV YEVSVYHPST LRIEKCYAND PYARGLSSDG 300 KRTLLVNLTS ESLKPEGWDN LAKEKPSLLS FCDISLYELH IRDFSANDQT VHPDFRGGYL 360 AFTFENSAGV LHLKKLSNAG ITHVHLLPTF QFAGVDDVKE NWKCVDNKML ETLLPDSIEQ 420 QAQITAVQDN DGYNWGYNPV LWGVPKGSYA SNPNGPSRTI QFRKMVQALN RIGLRVVLDV 480 VYNHLHGSGP FDENSVLDKI VPGYYLRRNI DGIIENSTCV NNTASEHYMV ERLIIDDLLN 540 WAVNYKVDGF RFDLMGHLMK STMVKAKIAL HSLSVERDGV DGSSLYIYGE GWDFGEVAKN 600 GRGVNASQFN LYGTGIGSFN DRIRDAMLGG SPFGHPLHQG FVTGLMLQPN GHDHGGKDVE 660 ELMLTTAKDH IQVGMAANLR DFVLINSEGK EVKGSEITTY GGEPVAYALS PTETINYVSA 720 HDNETLFDIV SMKTPMEISV DERCRLNHLA TSIIALSQGI PFFHAGDEML RSKSLDRDSY 780 NSGDWFNRLD FSYNSNNWAV GLPPQKKNEK NWPLIKPRLA DPSFKPQKHH IVAATENFLD 840 VLQMRYSSPL FRLTTANAIQ ERVRFHNTGP SWIPGVIVMS IEDGHEGFPG LSQLDPIYSY 900 IVVIFNTRPT KVSFTSPALR ARTFELHPVQ VKSADEVVKN SRYEASSGCF TVPPITTSVF 960 VEHR 1020 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG1523 | PulA | 9.0e-98 | 201 | 964 | 805 | + Type II secretory pathway, pullulanase PulA and related glycosidases [Carbohydrate transport and metabolism] | ||
TIGR02104 | pulA_typeI | 3.0e-139 | 200 | 918 | 736 | + pullulanase, type I. Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. This family consists of pullulanases related to the subfamilies described in TIGR02102 and TIGR02103 but having a different domain architecture with shorter sequences. Members are called type I pullulanases. | ||
cd11341 | AmyAc_Pullulanase_LD-like | 1.0e-167 | 332 | 797 | 476 | + Alpha amylase catalytic domain found in Pullulanase (also called dextrinase; alpha-dextrin endo-1,6-alpha glucosidase), limit dextrinase, and related proteins. Pullulanase is an enzyme with action similar to that of isoamylase; it cleaves 1,6-alpha-glucosidic linkages in pullulan, amylopectin, and glycogen, and in alpha-and beta-amylase limit-dextrins of amylopectin and glycogen. Pullulanases are very similar to limit dextrinases, although they differ in their action on glycogen and the rate of hydrolysis of 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. | ||
PLN02877 | PLN02877 | 0 | 1 | 964 | 970 | + alpha-amylase/limit dextrinase | ||
TIGR02103 | pullul_strch | 0 | 85 | 964 | 915 | + alpha-1,6-glucosidases, pullulanase-type. Members of this protein family include secreted (or membrane-anchored) pullulanases of Gram-negative bacteria and pullulanase-type starch debranching enzymes of plants. Both enzymes hydrolyze alpha-1,6 glycosidic linkages. Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. This family is closely homologous to, but architecturally different from, the Gram-positive pullulanases of Gram-positive bacteria (TIGR02102) [Energy metabolism, Biosynthesis and degradation of polysaccharides]. |
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:0043169 | cation binding |
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 | 4aio_A | 0 | 88 | 964 | 6 | 883 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
PDB | 2y5e_A | 0 | 88 | 964 | 6 | 883 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
PDB | 2y4s_A | 0 | 88 | 964 | 6 | 883 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
PDB | 2fhf_A | 0 | 90 | 960 | 179 | 1066 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
PDB | 2fhc_A | 0 | 90 | 960 | 179 | 1066 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |