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Basic Information | |
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Species | Physcomitrella patens |
Cazyme ID | Pp1s142_79V6.1 |
Family | CBM41 |
Protein Properties | Length: 1080 Molecular Weight: 119365 Isoelectric Point: 6.4691 |
Chromosome | Chromosome/Scaffold: 142 Start: 572664 End: 581449 |
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 |
CBM41 | 101 | 191 | 4.3e-23 |
KIHYYRKNGVYDHWGLHIWGRIASPTEWNSPLAPAGSDEFGIYWEVDAMDGEVHFVVHQGDSKDCEGTISSGKDIEVWLVSGRPTVFSQKP | |||
GH13 | 481 | 888 | 2e-34 |
DSAGVTHLKKLAEAGLTHVHLLPSFDFSSVDERKETWKTVDEDKLSMYAPNSEEQQKAIVAIQDQDAFNWGYDPIYWGVPEGSYATDPNGPARTVEFRTM VQALNRSGLRVILDVVYNHLHGSGPSGHHSCLDKVVPHYYLRLNKDGYVENSTCMNNTACEHYMVDRLIVDDLKHWAVNYKVDGFRFDLMGHLMKHTMVR AKEVLRRLTLQKDGVDGSKIYIYGEGWDFGEVANNARGVNAVQQNLAGTGIGSFNDRIRDTCLGGSPFGDPLQQGLVTGLALQPNSLFQGGEDAMHNALA ATTDWVMLGIAANLKDYSFVSYKGNEVKGDEVLTHDGKPVAYASSPEELVNYVSAHDNETLFDIVMLKSADEVTLEQRCRINHLATSIVALAQGIPFFHA GDELLRSK |
Full Sequence |
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Protein Sequence Length: 1080 Download |
MVTPVASSSP ALHLIPALCA SSRNASLHSK ESKIIWSTSK SKLKQDPSAT LSSPWRASRS 60 AALFSSEVVR PSPRPRNLTS SISVQLTEKM ADNADKTVRY KIHYYRKNGV YDHWGLHIWG 120 RIASPTEWNS PLAPAGSDEF GIYWEVDAMD GEVHFVVHQG DSKDCEGTIS SGKDIEVWLV 180 SGRPTVFSQK PDPKCLPQGD LSKSRAFWIK EDLLAWNASN ENDKFFLHSS NAASLKVTAN 240 GVEGADVVVK LAEDPNGLPP KVLDKFPHIS GYRALRIPTD VDVKKILKTQ LALSATDEQG 300 QATDATGIQV GGVLDDLFAY DGPLGANAIK DGVSINLWAP TAQNVRLFLY STPTGGEPEE 360 KLQLHESNGV WSTFGPISWK GKYYLYEVTV YHPASRVVEV SLANDPYSRG LSVNGEKSLI 420 IDMADAHLAP EGWTNLGNEK PHLESFNDMA IYELHIRDFS ISDKTVDPAV AGGYLAFAQK 480 DSAGVTHLKK LAEAGLTHVH LLPSFDFSSV DERKETWKTV DEDKLSMYAP NSEEQQKAIV 540 AIQDQDAFNW GYDPIYWGVP EGSYATDPNG PARTVEFRTM VQALNRSGLR VILDVVYNHL 600 HGSGPSGHHS CLDKVVPHYY LRLNKDGYVE NSTCMNNTAC EHYMVDRLIV DDLKHWAVNY 660 KVDGFRFDLM GHLMKHTMVR AKEVLRRLTL QKDGVDGSKI YIYGEGWDFG EVANNARGVN 720 AVQQNLAGTG IGSFNDRIRD TCLGGSPFGD PLQQGLVTGL ALQPNSLFQG GEDAMHNALA 780 ATTDWVMLGI AANLKDYSFV SYKGNEVKGD EVLTHDGKPV AYASSPEELV NYVSAHDNET 840 LFDIVMLKSA DEVTLEQRCR INHLATSIVA LAQGIPFFHA GDELLRSKSL DRDSYNSGDW 900 FNRLDFSYES NNWGVGLPPM GKNGEKWPLM RHLLGNPAFK PSRKHILAAL ANFQEFLRIR 960 FSSPLFRLRT ANAVQARLNF HNTGPSSIPG VIMFSLHDGD EGKPGLTQLD PNFRCIAVVI 1020 NARPTKLDFE VNTFKHCNLT LHPIQEHSAD EVVKKSSFEP SKAIFRVPPR TTAVFVELR* 1080 1140 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02877 | PLN02877 | 2.0e-16 | 2 | 84 | 83 | + alpha-amylase/limit dextrinase | ||
TIGR02104 | pulA_typeI | 8.0e-144 | 315 | 1030 | 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 | 1.0e-172 | 447 | 912 | 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 | 78 | 1079 | 1009 | + alpha-amylase/limit dextrinase | ||
TIGR02103 | pullul_strch | 0 | 200 | 1079 | 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 | |
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GO Term | Description |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0005975 | carbohydrate metabolic process |
GO:0030246 | carbohydrate 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 | CBI31395.1 | 0 | 198 | 1079 | 73 | 954 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_001771764.1 | 0 | 1 | 1079 | 65 | 1160 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002271820.1 | 0 | 198 | 1079 | 24 | 905 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002315334.1 | 0 | 198 | 1079 | 11 | 893 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002532780.1 | 0 | 198 | 1079 | 82 | 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 | 201 | 1079 | 3 | 883 | A Chain A, Crystal Structure Of A 6-Sst6-Sft From Pachysandra Terminalis |
PDB | 2y5e_A | 0 | 201 | 1079 | 3 | 883 | A Chain A, Crystal Structure Of A 6-Sst6-Sft From Pachysandra Terminalis |
PDB | 2y4s_A | 0 | 201 | 1079 | 3 | 883 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
PDB | 2fhf_A | 0 | 116 | 1075 | 77 | 1066 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
PDB | 2fhc_A | 0 | 116 | 1075 | 77 | 1066 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
starch degradation I | RXN-1824 | EC-3.2.1.41 | pullulanase |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
FC348048 | 260 | 806 | 1065 | 0 |
BY958476 | 217 | 650 | 866 | 0 |
GO872243 | 341 | 705 | 1045 | 0 |
JG932549 | 286 | 634 | 919 | 0 |
FE484997 | 280 | 568 | 847 | 0 |
Orthologous Group | |||||
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Species | ID | ||||
Physcomitrella patens | Pp1s142_79V6.1.101.191 | ||||
Picea abies | MA_10429723g0010 |
Sequence Alignments (This image is cropped. Click for full image.) |
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