y
Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 165275 |
Family | GH13 |
Protein Properties | Length: 889 Molecular Weight: 99074 Isoelectric Point: 5.0036 |
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 | 286 | 693 | 3.5e-28 |
FSEMESAGVRHLRSLAEAGLTHVHLLPSFDFGSVNEVKEKWKTLDYDRLEGLPPDSEEQQEAVVAIQNEDGFNWGYDPVNWGVPDGSYSTDPNGPCRTFE FRSMVQSINRLGLRVVLDVVYNHLHGNGPSDHLSVLDKVVPGYYLRRNKDGVIENSTCMNNTASEFYMVDRLIVDDLLMWATQYKVDGFRFDLMGHIMKR TMMRAKTAVQSLTEEKDGVDGSKIYLYGEGWDFGEVYGNGRGVNATQLNLPGSQIGSFNDRMRDSAIGGSPFGDPLEQGIFTGLSLQPNSLPQGDEENMA KNLARGKDRIILGLAGNLRDYVFVDFEGREVKGCEVLTHDGKPVAYAASPTEIINYVSAHDNETLFDIIMMKVAESVSLEDRCRVNHLASSIVALSQAIP FFHAGEDM |
Full Sequence |
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Protein Sequence Length: 889 Download |
MLLFFLFFQG NLNLARAFWV NKDLLAWNVD AQDGSFFLHA SQHAQLQLTG RGIEGADTII 60 QLEVDTHDLP AEVLERLPHI SGYHALRLPR DADWKKLIKC QLAVGASNAY GAPIDASGVQ 120 LPSVLDDVLR YDGPLGVTFS ETECTFSIWA PTAQNVRLFL YTEPSGGEPE AVIQLDEKHN 180 VWTASGPKDW VGKYYLYEVT VFHPSTLQVE ICLANDPYSR GLSANGERSL VIDLSDHNPE 240 NWDRLSSEKP MLHCFNDMAI YELHIRDFSA RDQTVPENLR GTFLAFSEME SAGVRHLRSL 300 AEAGLTHVHL LPSFDFGSVN EVKEKWKTLD YDRLEGLPPD SEEQQEAVVA IQNEDGFNWG 360 YDPVNWGVPD GSYSTDPNGP CRTFEFRSMV QSINRLGLRV VLDVVYNHLH GNGPSDHLSV 420 LDKVVPGYYL RRNKDGVIEN STCMNNTASE FYMVDRLIVD DLLMWATQYK VDGFRFDLMG 480 HIMKRTMMRA KTAVQSLTEE KDGVDGSKIY LYGEGWDFGE VYGNGRGVNA TQLNLPGSQI 540 GSFNDRMRDS AIGGSPFGDP LEQGIFTGLS LQPNSLPQGD EENMAKNLAR GKDRIILGLA 600 GNLRDYVFVD FEGREVKGCE VLTHDGKPVA YAASPTEIIN YVSAHDNETL FDIIMMKVAE 660 SVSLEDRCRV NHLASSIVAL SQAIPFFHAG EDMLRSKSLD RDSYNSGDWF NRLDFSYETN 720 NWGVGLPPKS KNGEKWPIMR KLLGNESLRP SKDHILAAVA NFQDLLKIRF SSPLFRLKTV 780 NAIQARLQFH NTGPAAIPGI IVMSIHDGDE GEPGLLQIDS IFRIIVVVIN ARPDEGILKV 840 GLLRGFKLEL HPVQAASQDE LVKASSCDNG TFAIPKRTTA VFVEKRCC* 900 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG1523 | PulA | 3.0e-87 | 131 | 882 | 797 | + Type II secretory pathway, pullulanase PulA and related glycosidases [Carbohydrate transport and metabolism] | ||
TIGR02104 | pulA_typeI | 2.0e-143 | 126 | 835 | 723 | + 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 | 2.0e-169 | 256 | 721 | 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 | 9 | 886 | 882 | + alpha-amylase/limit dextrinase | ||
TIGR02103 | pullul_strch | 0 | 12 | 886 | 912 | + 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 - 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 | 15 | 887 | 6 | 884 | A Chain A, Crystal Structure Of Human Muscle Glycogen Phosphorylase A With Amp And Glucose |
PDB | 2y5e_A | 0 | 15 | 887 | 6 | 884 | A Chain A, Crystal Structure Of Human Muscle Glycogen Phosphorylase A With Amp And Glucose |
PDB | 2y4s_A | 0 | 15 | 887 | 6 | 884 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
PDB | 2fhf_A | 0 | 14 | 882 | 176 | 1066 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
PDB | 2fhc_A | 0 | 14 | 882 | 176 | 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 |