y
Basic Information | |
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Species | Chlamydomonas reinhardtii |
Cazyme ID | Cre11.g476650.t1.3 |
Family | GH13 |
Protein Properties | Length: 1121 Molecular Weight: 119890 Isoelectric Point: 6.8075 |
Chromosome | Chromosome/Scaffold: 11 Start: 2660725 End: 2677044 |
Description | limit dextrinase |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 510 | 919 | 3.4e-30 |
SHLAALRGAGLNHLHLLPTYDFATVPERAEDQRGVQEDLTRHPPDSPQQQAAVLAVADNDGFNWGYDPVHYGVPEGSYATDPDGVARIREFREMVQSLHG QGWRVVQDVVYNHTFASGPHSKYSVLDKVVPGYYHRRHEDGGICDSTCCNNTATEHAMCERLVVDDITHWASNYRVDGFRFDIMGHLMMSTMSKIRTSLD SLTPDKDHGVSGRSIYIYGEAWDFGEVAGNQRGRNAAQMNLAGSGLGAFNDRLRDGAMGGGPFAPPQFQGLVTGLALAPNPAAAQAGQGGGGGGGGSEAA RAELLVLSDWARSALAGNLRAYPLHLCDGSTRPGEQVLAHGLPLAYGGLPCEHVAFIGCHDNKTQFDQIIEKASVNESGEERMRMAVMCLALITLSQGVP FIHAGDDLLR |
Full Sequence |
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Protein Sequence Length: 1121 Download |
MLAKKHYGIK QQHCGSLRKL AAPRQPARNN LTFHGAATQR LGLEDSASFP QWVSGQAGTA 60 ILRSVACSAS DASAANAAPA VDPGMLIIHY VRKDHNYKGW GLHVWGDSSS CTQWQQPLKP 120 TRVTERGLVW ELPLRSGARR VGALVHKGEQ KAASGEVTIS AHGSTMSVDQ ATGAAVQEAW 180 LVGAEQSAFA FPPDMSRIPA GSINKQAAHW VSPGLLLWRQ AAEDVVGRRR FRLHYSRAGY 240 MHITGAGVQG ADASWDLEPQ PPAAAAPGVK RFPHLYGCTA LAVPPEAGAA AAAAEGGGIL 300 TGQLLVSVHD AAGDALDATG VQIQGVLDEL MSYDGPLGDH PDVGGDGHSI TLWAPTAQKV 360 ELLYWGSAPR GGQPQVHAMC RGPCGAWSLR RPAAWLWSYY TYRVTVYCPW TARMETVEVT 420 DPYSRGLAAD GGRTQVVDLE HPDTMPAGWH SHVPPALAQW TDISVYEMHV RDFSITDASV 480 PPPLRGKYLA FVPERVAAAA GGSPLSAGLS HLAALRGAGL NHLHLLPTYD FATVPERAED 540 QRGVQEDLTR HPPDSPQQQA AVLAVADNDG FNWGYDPVHY GVPEGSYATD PDGVARIREF 600 REMVQSLHGQ GWRVVQDVVY NHTFASGPHS KYSVLDKVVP GYYHRRHEDG GICDSTCCNN 660 TATEHAMCER LVVDDITHWA SNYRVDGFRF DIMGHLMMST MSKIRTSLDS LTPDKDHGVS 720 GRSIYIYGEA WDFGEVAGNQ RGRNAAQMNL AGSGLGAFND RLRDGAMGGG PFAPPQFQGL 780 VTGLALAPNP AAAQAGQGGG GGGGGSEAAR AELLVLSDWA RSALAGNLRA YPLHLCDGST 840 RPGEQVLAHG LPLAYGGLPC EHVAFIGCHD NKTQFDQIIE KASVNESGEE RMRMAVMCLA 900 LITLSQGVPF IHAGDDLLRS KSLDRDSYNS GDWFNRIDWT GASNGFGSGL PVSTKNGGSW 960 SYMGPLLREA GRLTPTPEHM KTATAIFQAL LRVRYSSPLF RLAATADVIR QLAFHNTGPQ 1020 QNPGVIVMEL TSAPAPGGGG GGSEQNQGVY DPKYERLVTV FNCAPYVNDV PYPPGAARLQ 1080 LHSDLVAVGD ARLSSAAAEE ASRTLHLPPR TAAVFVQPRQ * 1140 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR02104 | pulA_typeI | 7.0e-12 | 859 | 1030 | 172 | + 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. | ||
TIGR02104 | pulA_typeI | 6.0e-92 | 328 | 764 | 443 | + 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 | 4.0e-143 | 461 | 944 | 487 | + 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 | 172 | 1119 | 957 | + alpha-amylase/limit dextrinase | ||
TIGR02103 | pullul_strch | 0 | 203 | 1119 | 952 | + 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]. |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | AAS88886.1 | 0 | 36 | 1119 | 27 | 1057 | SPU [Ostreococcus tauri] |
RefSeq | XP_001697294.1 | 0 | 43 | 894 | 12 | 778 | pullulanase-type starch debranching enzyme [Chlamydomonas reinhardtii] |
RefSeq | XP_001697294.1 | 0 | 1021 | 1120 | 769 | 868 | pullulanase-type starch debranching enzyme [Chlamydomonas reinhardtii] |
RefSeq | XP_001771764.1 | 0 | 61 | 1119 | 142 | 1160 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | ZP_04036526.1 | 0 | 55 | 1119 | 108 | 1117 | alpha-1,6-glucosidase, pullulanase-type [Meiothermus silvanus DSM 9946] |
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 | 208 | 1119 | 8 | 883 | A Chain A, Wif Domain-Epidermal Growth Factor (Egf)-Like Domains 1-3 Of Human Wnt Inhibitory Factor 1 In Complex With 1,2-Dipalmitoylphosphatidylcholine |
PDB | 2y5e_A | 0 | 208 | 1119 | 8 | 883 | A Chain A, Wif Domain-Epidermal Growth Factor (Egf)-Like Domains 1-3 Of Human Wnt Inhibitory Factor 1 In Complex With 1,2-Dipalmitoylphosphatidylcholine |
PDB | 2y4s_A | 0 | 208 | 1119 | 8 | 883 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
PDB | 2fhf_A | 0 | 96 | 1119 | 71 | 1070 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
PDB | 2fhc_A | 0 | 96 | 1119 | 71 | 1070 | 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 |
FE436024 | 244 | 522 | 764 | 0 |
GR088431 | 219 | 546 | 764 | 0 |
FE480380 | 213 | 552 | 764 | 0 |
CO128344 | 217 | 548 | 764 | 0 |
EL452695 | 273 | 457 | 728 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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