| Basic Information | |
|---|---|
| Species | Arabidopsis thaliana |
| Cazyme ID | AT5G04360.1 |
| Family | GH13 |
| Protein Properties | Length: 966 Molecular Weight: 107067 Isoelectric Point: 6.3472 |
| Chromosome | Chromosome/Scaffold: 5 Start: 1221566 End: 1228678 |
| Description | Alpha amylase, catalytic domain containing protein, expressed |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 365 | 772 | 1.7e-30 |
| DSAGVKHLQKLVDAGLTHLHLLPTFQFGDVDDEKENWKSVDTSLLEGLRPDSTEAQARITEIQNDDGYNWGYNPVLWGVPKGSYASDPTGPCRIIEFRKM VQALNCTGLNVVLDVVYNHLHASGPHDKESVLDKIVPGYYLRRNSDGFIENSTCVNNTASEHYMVDRLIRDDLLNWVVNYKVDGFRFDLMGHIMKATIVN AKSAIGSLRKETDGVDGSRIYLYGEGWNFGEVAENGRGINASQFNLGGTGIGSFNDRIRDATLGGSPFGHPLQQGFITGLLLQPNAHDHGSEATQELMLS TAKNHIQTGMAANLKDYMLTNHEGKEVKGSEVLMHDATPVAYASLPTETINYVSAHDNETLFDIISLKTPMEISVDERCRINHLASSMIALSQGIPFFHA GDEILRSK | |||
| Full Sequence |
|---|
| Protein Sequence Length: 966 Download |
| MALTLTPTSS VHLLSSISVA RPRIFAADFN LRSRWRRRRP VTSISNFRLR LPSKTSLHCL 60 CSSSSASSPM SLEVSSPNSQ FLDCLIYSRA YWVTQGVIAW NVDVGEGSCY FYASKSAGLS 120 FSEDGIDGYD LRIKLEAESG SLPADVIEKF PHIRNYKSFK VPKDLDIRDL VKSQLAVVCF 180 DAEGRLIQGT GLQLPGVLDE LFSYDGPLGA HFTPEGVSLH LWAPTAQAVS VCIYKNPLDK 240 SPMEICPLKE ANGVWSTEGA CSWGGCYYVY KVSVYHPSTM KLETCYANDP YARGLSADGR 300 KTFLVNLDSD DLKPEGWDNL ADKKPCLRSF SDISIYELHV RDFSANDETV EPENRGGYLA 360 FTSKDSAGVK HLQKLVDAGL THLHLLPTFQ FGDVDDEKEN WKSVDTSLLE GLRPDSTEAQ 420 ARITEIQNDD GYNWGYNPVL WGVPKGSYAS DPTGPCRIIE FRKMVQALNC TGLNVVLDVV 480 YNHLHASGPH DKESVLDKIV PGYYLRRNSD GFIENSTCVN NTASEHYMVD RLIRDDLLNW 540 VVNYKVDGFR FDLMGHIMKA TIVNAKSAIG SLRKETDGVD GSRIYLYGEG WNFGEVAENG 600 RGINASQFNL GGTGIGSFND RIRDATLGGS PFGHPLQQGF ITGLLLQPNA HDHGSEATQE 660 LMLSTAKNHI QTGMAANLKD YMLTNHEGKE VKGSEVLMHD ATPVAYASLP TETINYVSAH 720 DNETLFDIIS LKTPMEISVD ERCRINHLAS SMIALSQGIP FFHAGDEILR SKSLDRDSYN 780 SGDWFNRLDF SYSSNNWGVG LPPKGKNEHN WPLIKPRLQD PSFKPKSSHI VATLHNFLDL 840 LRIRYSSPLF RLDTARAIQE RVRFHNTGPS SIPGAIVMSI EDGHRGIPSV SQIDPIYSLI 900 VVIFNARPSE FSYPSPALKD RKLELHPVQV MSADEIVKKS VYDSFSGGFT VPARTTTVFV 960 ESRNG* 1020 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG1523 | PulA | 5.0e-98 | 200 | 959 | 800 | + Type II secretory pathway, pullulanase PulA and related glycosidases [Carbohydrate transport and metabolism] | ||
| TIGR02104 | pulA_typeI | 4.0e-136 | 199 | 917 | 732 | + 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 | 3.0e-164 | 332 | 796 | 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 | 1 | 963 | 970 | + alpha-amylase/limit dextrinase | ||
| TIGR02103 | pullul_strch | 0 | 84 | 963 | 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 | |
|---|---|
| GO Term | Description |
| GO:0003824 | catalytic activity |
| GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
| GO:0004556 | alpha-amylase activity |
| GO:0005975 | carbohydrate metabolic process |
| GO:0005983 | starch catabolic process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CBI31395.1 | 0 | 69 | 963 | 60 | 954 | unnamed protein product [Vitis vinifera] |
| RefSeq | NP_196056.2 | 0 | 1 | 965 | 1 | 965 | ATLDA (LIMIT DEXTRINASE); alpha-amylase/ limit dextrinase/ pullulanase [Arabidopsis thaliana] |
| Swiss-Prot | Q8GTR4 | 0 | 1 | 965 | 1 | 965 | PULA1_ARATH RecName: Full=Pullulanase 1, chloroplastic; Short=AtPU1; AltName: Full=Protein LIMIT DEXTRINASE; Short=AtLDA; Flags: Precursor |
| RefSeq | XP_002315334.1 | 0 | 70 | 963 | 1 | 893 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002532780.1 | 0 | 2 | 963 | 9 | 964 | pullulanase, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 4aio_A | 0 | 88 | 963 | 6 | 883 | A Chain A, The Structure Of Soybean Peroxidase |
| PDB | 2y5e_A | 0 | 88 | 963 | 6 | 883 | A Chain A, The Structure Of Soybean Peroxidase |
| PDB | 2y4s_A | 0 | 88 | 963 | 6 | 883 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
| PDB | 2fhf_A | 0 | 90 | 959 | 179 | 1066 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
| PDB | 2fhc_A | 0 | 90 | 959 | 179 | 1066 | 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 |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| DK558130 | 279 | 209 | 482 | 0 |
| GO872243 | 341 | 589 | 929 | 0 |
| EX123200 | 281 | 629 | 881 | 0 |
| CO128344 | 287 | 399 | 685 | 0 |
| EH773847 | 282 | 620 | 901 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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