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CAZyme Information: AGR57_11409T0-p1

You are here: Home > Sequence: AGR57_11409T0-p1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Phanerochaete chrysosporium
Lineage Basidiomycota; Agaricomycetes; ; Phanerochaetaceae; Phanerochaete; Phanerochaete chrysosporium
CAZyme ID AGR57_11409T0-p1
CAZy Family AA3
CAZyme Description Glycoside Hydrolase Family 13 / Carbohydrate-Binding Module Family 20 protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
581 61110.83 5.3489
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PchrysosporiumRP-78 13602 273507 0 13602
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC - 3.2.1.1:7 3.2.1.116:1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 59 334 2.4e-97 0.9962825278810409
CBM20 487 574 3.3e-30 0.9777777777777777

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
200456 AmyAc_bac_euk_AmyA 2.71e-149 33 390 1 329
Alpha amylase catalytic domain found in bacterial and eukaryotic Alpha amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes AmyA proteins from bacteria, fungi, mammals, insects, mollusks, and nematodes. 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.
200454 AmyAc_bac1_AmyA 6.44e-44 35 394 3 349
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes Firmicutes, Proteobacteria, Actinobacteria, and Cyanobacteria. 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.
99883 CBM20_alpha_amylase 7.52e-44 487 581 1 95
Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in several bacterial and fungal alpha-amylases including the maltopentaose-forming amylases (G5-amylases). Most alpha-amylases have, in addition to the C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13, which hydrolyzes internal alpha-1,4-glucosidic bonds in starch and related saccharides, yielding maltotriose and maltose. Two types of soluble substrates are used by alpha-amylases including long substrates (e.g. amylose) and short substrates (e.g. maltodextrins or maltooligosaccharides). The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.
395557 CBM_20 1.99e-38 487 578 1 95
Starch binding domain.
99886 CBM20_glucoamylase 3.36e-37 482 580 2 106
Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Glucoamylases are inverting, exo-acting starch hydrolases that hydrolyze starch and related polysaccharides by releasing the nonreducing end glucose. They are mainly active on alpha-1,4-glycosidic bonds but also have some activity towards 1,6-glycosidic bonds occurring in natural oligosaccharides. The ability of glucoamylases to cleave 1-6-glycosidic binds is called "debranching activity" and is of importance in industrial applications, where complete degradation of starch to glucose is needed. Most glucoamylases are multidomain proteins containing an N-terminal catalytic domain, a C-terminal CBM20 domain, and a highly O-glycosylated linker region that connects the two. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
4.39e-288 27 581 37 589
1.55e-258 12 581 4 574
1.27e-257 12 581 4 574
2.95e-256 6 581 4 574
3.38e-249 6 581 4 569

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.72e-105 34 480 3 446
CRYSTAL STRUCTURE ANALYSIS OF THE TERNARY COMPLEX BETWEEN PSYCHROPHILIC ALPHA AMYLASE FROM PSEUDOALTEROMONAS HALOPLANCTIS IN COMPLEX WITH A HEPTA-SACCHARIDE AND A TRIS MOLECULE [Pseudoalteromonas haloplanktis],1G9H_A TERNARY COMPLEX BETWEEN PSYCHROPHILIC ALPHA-AMYLASE, COMII (PSEUDO TRI-SACCHARIDE FROM BAYER) AND TRIS (2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL) [Pseudoalteromonas haloplanktis],1L0P_A Crystal Structure Analysis Of The Complex Between Psychrophilic Alpha Amylase From Pseudoalteromonas Haloplanctis And Nitrate [Pseudoalteromonas haloplanktis]
2.00e-105 34 480 3 446
Chain A, ALPHA-AMYLASE [Pseudoalteromonas haloplanktis]
2.00e-105 34 480 3 446
Chain A, ALPHA-AMYLASE [Pseudoalteromonas haloplanktis]
2.00e-105 34 480 3 446
ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS [Pseudoalteromonas haloplanktis],1AQM_A ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS COMPLEXED WITH TRIS [Pseudoalteromonas haloplanktis],1B0I_A ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS [Pseudoalteromonas haloplanktis]
9.59e-105 34 480 3 446
Chain A, alpha-amylase [Pseudoalteromonas haloplanktis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6.55e-160 6 581 3 565
Alpha-amylase OS=Streptomyces limosus OX=1947 GN=aml PE=3 SV=1
7.43e-159 6 581 3 565
Alpha-amylase OS=Streptomyces griseus OX=1911 GN=amy PE=3 SV=1
7.45e-157 9 581 5 568
Alpha-amylase OS=Streptomyces violaceus OX=1936 GN=aml PE=2 SV=1
3.19e-136 13 549 21 570
Alpha-amylase OS=Thermomonospora curvata OX=2020 GN=tam PE=1 SV=1
1.88e-134 9 476 5 454
Alpha-amylase OS=Streptomyces thermoviolaceus OX=1952 GN=amy PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000926 0.999047 CS pos: 27-28. Pr: 0.6446

TMHMM  Annotations      help

There is no transmembrane helices in AGR57_11409T0-p1.