| Basic Information | |
|---|---|
| Species | Cucumis sativus |
| Cazyme ID | Cucsa.308730.1 |
| Family | GH13 |
| Protein Properties | Length: 961 Molecular Weight: 107240 Isoelectric Point: 6.1393 |
| Chromosome | Chromosome/Scaffold: 02978 Start: 719877 End: 732666 |
| Description | limit dextrinase |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 359 | 768 | 8e-34 |
| DSAGINHLKKLSNAGLSHVHLLPTFQFGGVDDDKTKWKFVDTELLENLPPDSAEQQSLIADIQNSDGYNWGYNPIMWGVPKGSYASDSNGPCRLVEFRKM VQALNQIGLRVVLDVVYNHLHGHGPFDPNSVLDKIVPGYYLRRNTDGFIENSTCVNNTASEHFMVERMIVDDILHWVVDYKVDGFRFDLMGHLMKSTMLK AKDALRGLTKEKNGVDGSSIYIYGEGWDFGEVAKNGRGVNASQFNLFGTGIGSFNDRVRDAILGGSPFGHPLQQGFVTGLLLEPNDHDHGTHEVAESMLA VSKDHIEVAMAANLRDYILTNFEGKEVKGLEVLTHDRSPVAYASCPTETVNYVSAHDNETLFDIVSLKTPRNITVDDRCRINHLATSIIALSQGIPFFHC GDELLRSKSM | |||
| Full Sequence |
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| Protein Sequence Length: 961 Download |
| MSLLFSSSLH FFPPSAFPTS LCYQLHHPFA AFSSSPPAAG TSLSPGFRHN FRTGPLYCSP 60 SSSMSLEEST STSQLEDSLL YSRAFWVSKH VIAWNVEVES GSCYLFASKM ATLRVEDGVV 120 EGYDVKIRLE KDRSQLPENV IKKFPHIQNY CPFTVPPASD VEALLKCQLA VATFNSYGEC 180 KNITCLQLPG VLDDLFSYEG PLGAIYSKEA VSLYLWAPTA QAVRAQIFRD PVGGMPFEVI 240 PLEEVDGIWR TKGPKSWKGC YYEYEVTVYH PSTLQVEKCF TTDPYSRGVS SDGRRTLFVD 300 LFSDDLIPKG WDKLADEKPP VDSFSDISIY ELHVRDFSIS DQSVHPDLRG GYMAFTLQDS 360 AGINHLKKLS NAGLSHVHLL PTFQFGGVDD DKTKWKFVDT ELLENLPPDS AEQQSLIADI 420 QNSDGYNWGY NPIMWGVPKG SYASDSNGPC RLVEFRKMVQ ALNQIGLRVV LDVVYNHLHG 480 HGPFDPNSVL DKIVPGYYLR RNTDGFIENS TCVNNTASEH FMVERMIVDD ILHWVVDYKV 540 DGFRFDLMGH LMKSTMLKAK DALRGLTKEK NGVDGSSIYI YGEGWDFGEV AKNGRGVNAS 600 QFNLFGTGIG SFNDRVRDAI LGGSPFGHPL QQGFVTGLLL EPNDHDHGTH EVAESMLAVS 660 KDHIEVAMAA NLRDYILTNF EGKEVKGLEV LTHDRSPVAY ASCPTETVNY VSAHDNETLF 720 DIVSLKTPRN ITVDDRCRIN HLATSIIALS QGIPFFHCGD ELLRSKSMDR DSYNSGDWFN 780 RLDFTYMTNN WGVGLPLKEK NQYNWPLIKP RLADPSFKPS KSHILAAVEN FTNLLQIRYS 840 SPLFRLKTSN AIQKRVRFHN SGTSLIPGLI VMSIEDGHNG IPGLSQLDST YSYIVVVVNA 900 RPTEISFPCP ALRAKTLQLH PIQLMSTDPV VKNSTYEPST GCFMVPPRTT SVFVEPRMHE 960 * 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-94 | 194 | 953 | 803 | + Type II secretory pathway, pullulanase PulA and related glycosidases [Carbohydrate transport and metabolism] | ||
| TIGR02104 | pulA_typeI | 7.0e-136 | 193 | 911 | 737 | + 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 | 2.0e-172 | 326 | 790 | 475 | + 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 | 81 | 957 | 877 | + alpha-amylase/limit dextrinase | ||
| TIGR02103 | pullul_strch | 0 | 81 | 957 | 913 | + 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 | |
|---|---|
| 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 - NR Download unfiltered results here | |||||||
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| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CAA58803.1 | 0 | 58 | 957 | 63 | 962 | pullulanase [Spinacia oleracea] |
| EMBL | CBI31395.1 | 0 | 26 | 957 | 22 | 954 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002271820.1 | 0 | 57 | 957 | 7 | 905 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002315334.1 | 0 | 64 | 957 | 1 | 893 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002532780.1 | 0 | 6 | 957 | 23 | 964 | pullulanase, 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 | 4aio_A | 0 | 82 | 957 | 6 | 883 | A Chain A, Crystal Structure Of The R3 Form Of Pectate Lyase A, Erwinia Chrysanthemi |
| PDB | 2y5e_A | 0 | 82 | 957 | 6 | 883 | A Chain A, Crystal Structure Of The R3 Form Of Pectate Lyase A, Erwinia Chrysanthemi |
| PDB | 2y4s_A | 0 | 82 | 957 | 6 | 883 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
| PDB | 2fhf_A | 0 | 84 | 957 | 179 | 1070 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
| PDB | 2fhc_A | 0 | 84 | 957 | 179 | 1070 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
| Hydropathy |
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| EST Download unfiltered results here | ||||
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| Hit | Length | Start | End | EValue |
| AM733410 | 287 | 634 | 920 | 0 |
| AM722646 | 246 | 716 | 961 | 0 |
| CO128344 | 286 | 395 | 680 | 0 |
| GO872243 | 341 | 583 | 923 | 0 |
| EH773847 | 282 | 614 | 895 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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