| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G158043_T02 |
| Family | GH13 |
| Protein Properties | Length: 963 Molecular Weight: 106240 Isoelectric Point: 5.2892 |
| Chromosome | Chromosome/Scaffold: 2 Start: 108630218 End: 108681539 |
| Description | limit dextrinase |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 366 | 770 | 4.1e-30 |
| GIEHLKKLSDAGLTHVHLLPSFQFGGVDDIKSNWKCVDEIELSKLPPGSDLQQAAIVAIQEEDPYNWGYNPVVWGVPKGSYASNPDGPSRIIEYRLMVQA LNRLGLRVVMDVVYNHLYSSGPFAITSVLDKIVPGYYLRRDSNGQTENSAAVNNTASEHFMVDRLIVDDLLNWAVNYKVDGFRFDLMGHIMKKTMIRAKS ALQSLTIDEHGVDGSKIYLYGEGWNFGEVAENQRGINGSQLNMSGTGIGSFNDRIRDAINGGSPFGNPLQQGFSTGLFLEPNGFYQGNETETRLTLATYA DHIQIGLAGNLKDYVVISHTGEARKGSEIRTFDGSPVGYASSPIETINYASAHDNETLFDIISLKTPMDLSIDERCRINHLSTSMIALSQGIPFFHAGDE ILRSK | |||
| Full Sequence |
|---|
| Protein Sequence Length: 963 Download |
| MLLHAGPSFL LAPPPRFAAA PSSASPRRSR TPQSSPPTSH FARPADPVAQ RVRPVAPRPP 60 MATAEEGASS DVGVAVAESA QGFLLDARAY WVTKSLIAWN ISDQKTSLFL YASRNATMCM 120 SSQDMKGYDS KVELQPENDG LPSSVTQKFP FISSYRAFRI PSSVDVATLV KCQLAVASFD 180 AHGNRQDVTG LQLPGVLDDM FAYTGPLGTI FSEEAVSMYL WAPTAQDVSV SFYDGPAGPL 240 LETVQLNELN GVWSVTGPRN WENRYYLYEV TVYHQTTGNI EKCLAADPYA RGLSANSTRT 300 WLVDINNETL KPLAWDGLAA EKPRLDSFSD ISIYELHIRD FSAHDSTVDC PFRGGFCAFT 360 FQDSVGIEHL KKLSDAGLTH VHLLPSFQFG GVDDIKSNWK CVDEIELSKL PPGSDLQQAA 420 IVAIQEEDPY NWGYNPVVWG VPKGSYASNP DGPSRIIEYR LMVQALNRLG LRVVMDVVYN 480 HLYSSGPFAI TSVLDKIVPG YYLRRDSNGQ TENSAAVNNT ASEHFMVDRL IVDDLLNWAV 540 NYKVDGFRFD LMGHIMKKTM IRAKSALQSL TIDEHGVDGS KIYLYGEGWN FGEVAENQRG 600 INGSQLNMSG TGIGSFNDRI RDAINGGSPF GNPLQQGFST GLFLEPNGFY QGNETETRLT 660 LATYADHIQI GLAGNLKDYV VISHTGEARK GSEIRTFDGS PVGYASSPIE TINYASAHDN 720 ETLFDIISLK TPMDLSIDER CRINHLSTSM IALSQGIPFF HAGDEILRSK SLDRDSYDSG 780 DWFNKIDFTY ETNNWGVGLP PREKNEGSWP LMKPRLENPS FKPAKHDIIA ALDKFIDILK 840 IRYSSPLFRL TTASDIVQRV HFHNTGPSLV PGVIVMSIED ARNDRHDMAQ IDETFSCVVT 900 VFNVCPYEVS IEIPDLASLR LQLHPVQVNS SDALARQSAY DTATGRFTVP KRTAAVFVEP 960 RC* 1020 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG1523 | PulA | 2.0e-89 | 177 | 957 | 797 | + Type II secretory pathway, pullulanase PulA and related glycosidases [Carbohydrate transport and metabolism] | ||
| TIGR02104 | pulA_typeI | 9.0e-134 | 198 | 915 | 731 | + 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 | 5.0e-173 | 330 | 794 | 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 | 65 | 961 | 901 | + alpha-amylase/limit dextrinase | ||
| TIGR02103 | pullul_strch | 0 | 87 | 961 | 910 | + 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 | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CAC09471.2 | 0 | 1 | 962 | 3 | 960 | H0806H05.4 [Oryza sativa (indica cultivar-group)] |
| GenBank | EEC76742.1 | 0 | 1 | 962 | 62 | 1021 | hypothetical protein OsI_14800 [Oryza sativa Indica Group] |
| GenBank | EEE60487.1 | 0 | 61 | 962 | 1 | 895 | hypothetical protein OsJ_13773 [Oryza sativa Japonica Group] |
| RefSeq | NP_001104920.1 | 0 | 1 | 962 | 1 | 962 | pullulanase-type starch debranching enzyme1 [Zea mays] |
| RefSeq | XP_002446086.1 | 0 | 1 | 962 | 3 | 966 | hypothetical protein SORBIDRAFT_06g001540 [Sorghum bicolor] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 4aio_A | 0 | 83 | 962 | 2 | 884 | A Chain A, Choline Binding Domain Of The Major Autolysin (C-Lyta) From Streptococcus Pneumoniae |
| PDB | 2y5e_A | 0 | 83 | 962 | 2 | 884 | A Chain A, Choline Binding Domain Of The Major Autolysin (C-Lyta) From Streptococcus Pneumoniae |
| PDB | 2y4s_A | 0 | 83 | 962 | 2 | 884 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
| PDB | 2fhf_A | 0 | 87 | 961 | 177 | 1070 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
| PDB | 2fhc_A | 0 | 87 | 961 | 177 | 1070 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
| Hydropathy |
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