| Basic Information | |
|---|---|
| Species | Sorghum bicolor |
| Cazyme ID | Sb06g001540.1 |
| Family | GH13 |
| Protein Properties | Length: 967 Molecular Weight: 106143 Isoelectric Point: 5.3556 |
| Chromosome | Chromosome/Scaffold: 6 Start: 2431511 End: 2446095 |
| Description | limit dextrinase |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 367 | 774 | 2.4e-30 |
| DSAGIEHLKKLSDAGLTHVHLLPSFQFGGVDDIKNNWKCVDEAELSKLPPGSDLQQAAIVAIQEDDPYNWGYNPVLWGVPKGSYASNPDGPSRIIEYRQM VQALNRLGLRVVMDVVYNHLYSSGPFAITSVLDKIVPGYYLRRDSNGQIENSAAVNNTASEHFMVDRLIVDDLLNWAVNYKVDGFRFDLMGHIMKRTMVR AKSALQSLTIDEHGVDGSKIYLYGEGWDFGEVAQNQRGINGSQLNMSGTGIGSFNDRVRDAINGGSPFGNPLQQGFSTGLFLEPNGFYQGNETETRRTLA TYADHIQIGLAGNLKDYVLISQTGEARKGSEIRTFDGSPVGYASSPIETINYASAHDNETLFDIISLKTPMNLSIDERCRINHLSTSMIALSQGIPFFHA GDEILRSK | |||
| Full Sequence |
|---|
| Protein Sequence Length: 967 Download |
| MQMLLHAGPS FQLAPPPRFA AAAAPSSASP RRSRTPQSSP PTSHSARAAA PGARRVRPVA 60 PRAPMATGEE GAGSDVGLAV PAPTPVFLLD ARAYWVTGSL IAWDVSDQET SLFLYASRNA 120 TMCMSSGVIE GYDSKVELQP ENDGLPSSVT QKFPFISSYR AFRIPSSVDV DTLVKCQLAV 180 ASFDAHGNRQ DVTGLQLPGV LDDMFAYTGP LGTIFSEGAV SMYLWAPTAQ DVSVNFYDGP 240 AGPLLETVQL NESNGVWSVT GPRNWENRYY LYEVTVYHPA TANIEKCLAA DPYARGLSAN 300 STRTWLVDIN NETLKPLAWD GLAAEKPKLD SFSDISIYEL HIRDFSAHDS TADCHFRGGF 360 CAFTCQDSAG IEHLKKLSDA GLTHVHLLPS FQFGGVDDIK NNWKCVDEAE LSKLPPGSDL 420 QQAAIVAIQE DDPYNWGYNP VLWGVPKGSY ASNPDGPSRI IEYRQMVQAL NRLGLRVVMD 480 VVYNHLYSSG PFAITSVLDK IVPGYYLRRD SNGQIENSAA VNNTASEHFM VDRLIVDDLL 540 NWAVNYKVDG FRFDLMGHIM KRTMVRAKSA LQSLTIDEHG VDGSKIYLYG EGWDFGEVAQ 600 NQRGINGSQL NMSGTGIGSF NDRVRDAING GSPFGNPLQQ GFSTGLFLEP NGFYQGNETE 660 TRRTLATYAD HIQIGLAGNL KDYVLISQTG EARKGSEIRT FDGSPVGYAS SPIETINYAS 720 AHDNETLFDI ISLKTPMNLS IDERCRINHL STSMIALSQG IPFFHAGDEI LRSKSLDRDS 780 YNSGDWFNKI DFTYETNNWG VGLPPREKNE GSWPLMKPRL ENPSFKPAKC DIIATLDKFV 840 DILKIRYSSP LFRLTTASDI EQRVHFHNTG PSSVPGVIVM SIEDARNDRH EMAQIDKTFS 900 CVVTVFNVCP HEVTIEIPDL ASLGLQLHPV QVNSSDALVR QSAYEATTGR FTVPKRTTAV 960 FVEPRC* 1020 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG1523 | PulA | 3.0e-93 | 181 | 961 | 797 | + Type II secretory pathway, pullulanase PulA and related glycosidases [Carbohydrate transport and metabolism] | ||
| TIGR02104 | pulA_typeI | 3.0e-137 | 202 | 919 | 730 | + 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-175 | 334 | 798 | 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 | 67 | 965 | 903 | + alpha-amylase/limit dextrinase | ||
| TIGR02103 | pullul_strch | 0 | 91 | 965 | 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:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
| GO:0005975 | carbohydrate metabolic process |
| 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 | 966 | 1 | 960 | H0806H05.4 [Oryza sativa (indica cultivar-group)] |
| GenBank | EEC76742.1 | 0 | 1 | 966 | 60 | 1021 | hypothetical protein OsI_14800 [Oryza sativa Indica Group] |
| GenBank | EEE60487.1 | 0 | 65 | 966 | 1 | 895 | hypothetical protein OsJ_13773 [Oryza sativa Japonica Group] |
| RefSeq | NP_001104920.1 | 0 | 3 | 966 | 1 | 962 | pullulanase-type starch debranching enzyme1 [Zea mays] |
| RefSeq | XP_002446086.1 | 0 | 1 | 966 | 1 | 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 | 87 | 966 | 2 | 884 | A Chain A, Bacillus Subtilis Pectate Lyase |
| PDB | 2y5e_A | 0 | 87 | 966 | 2 | 884 | A Chain A, Bacillus Subtilis Pectate Lyase |
| PDB | 2y4s_A | 0 | 87 | 966 | 2 | 884 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
| PDB | 2fhf_A | 0 | 91 | 965 | 177 | 1070 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
| PDB | 2fhc_A | 0 | 91 | 965 | 177 | 1070 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
| Metabolic Pathways | |||
|---|---|---|---|
| Pathway Name | Reaction | EC | Protein Name |
| starch degradation I | RXN-1824 | EC-3.2.1.41 | pullulanase |
| Hydropathy |
|---|
 |
| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| GO872243 | 341 | 591 | 931 | 0 |
| JG932549 | 288 | 519 | 806 | 0 |
| JG937368 | 286 | 637 | 922 | 0 |
| DN229072 | 256 | 529 | 784 | 0 |
| CO455864 | 261 | 344 | 604 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
|---|
 |
| Phylogeny |
|---|
 |