CAZyme Information: KDQ28034.1

Basic Information

• Species: Pleurotus ostreatus
• Lineage: Basidiomycota; Agaricomycetes; ; Pleurotaceae; Pleurotus; Pleurotus ostreatus
• CAZyme ID: KDQ28034.1
• CAZy Family: GH18
• CAZyme Description: glycoside hydrolase family 15 protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
578	KL198008|CGC3	61395.43	5.0672

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PostreatusPC15	12460	1137138	164	12296

• Gene Location: location=KL198008:2170159-2172303(-)

Full Sequence      

MRFLSLLSAIWTVGFAFAQSNADAFIAKEGPIAKAGLLANIGPSGAKSQGAQAGVVIASP
SATDPPYLFTWTRDSALVFQAIIEQVISGTDASLRPHIDNYVRSQTILQQVSNPSGTVSS
GGLGEPKFNIDLTAFTGAWGRPQRDGPALRSIALINWANHLLATNNASYVTNSLWPIIKL
DLDYVANSWNLTGFDLWEEVNSASFFTTAVQHRSLRQGAALAKAIGQTGVVAGYTTQADN
SLCFLQSYWNPSGNFATANTGGGRSGKDSNTVLTSIHTFDAEAGCDAATFQPCSDKALAN
LFVYVNAFRSIYTVNSGIPANQAVATGRYPEDVYFGGNPWYLSTLAVAEQLYDALIVWNK
QGSLTVTAVSQPFFASLSPGVAVGTYAASTSTFTTLTAAVRTFADGFVAKVAQFTPSSGA
LAEQYDRNDGHPLSAVDLTWSYASALTAFAAREGKTPVSWGASGLTVPTTCERNTSPGGG
GGPSVSVTFNVQATTVFGENIFLTGSVEALQNWSPDNAIALNSDNYPIWSVTVSVPANTR
IEYKFIRKFNGAVTWESDPNRVINTPAPGSFIENDTWR

Enzyme Prediction     

EC	3.2.1.3:94	3.2.1.3:71

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH15	41	448	1.4e-73	0.9722991689750693
CBM20	485	569	3.7e-30	0.9555555555555556

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395586	Glyco_hydro_15	1.28e-136	31	449	1	416	Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99883	CBM20_alpha_amylase	7.99e-41	488	578	4	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	7.93e-32	488	575	4	95	Starch binding domain.
99886	CBM20_glucoamylase	2.05e-29	488	577	10	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.
119437	CBM20	3.01e-28	488	577	3	96	The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding 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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAL43555.1|CBM20|GH15|3.2.1.3	8.22e-301	3	578	7	576
BAW34499.1|CBM20|GH15	8.22e-301	3	578	7	576
CAS91480.1|CBM20|GH15	1.44e-297	1	578	1	579
AOC97459.1|CBM20|GH15	3.71e-288	1	578	1	578
BAU78332.1|CBM20|GH15	2.39e-285	17	578	16	573

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VN4_A	6.06e-203	21	578	1	598	Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
6FRV_A	4.62e-186	23	578	4	616	Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
6FHV_A	1.90e-174	21	578	7	593	Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]
1AGM_A	8.51e-168	23	478	4	455	Refined structure for the complex of acarbose with glucoamylase from Aspergillus awamori var. x100 to 2.4 angstroms resolution [Aspergillus awamori],1DOG_A REFINED STRUCTURE FOR THE COMPLEX OF 1-DEOXYNOJIRIMYCIN WITH GLUCOAMYLASE FROM (ASPERGILLUS AWAMORI) VAR. X100 TO 2.4 ANGSTROMS RESOLUTION [Aspergillus awamori],1GLM_A REFINED CRYSTAL STRUCTURES OF GLUCOAMYLASE FROM ASPERGILLUS AWAMORI VAR. X100 [Aspergillus awamori],3GLY_A REFINED CRYSTAL STRUCTURES OF GLUCOAMYLASE FROM ASPERGILLUS AWAMORI VAR. X100 [Aspergillus awamori]
1GAH_A	8.81e-168	23	478	4	455	GLUCOAMYLASE-471 COMPLEXED WITH ACARBOSE [Aspergillus awamori]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|D8Q9M3|AMYG_SCHCM	2.49e-269	20	578	23	576	Glucoamylase ARB_02327-1 OS=Schizophyllum commune (strain H4-8 / FGSC 9210) OX=578458 GN=SCHCODRAFT_57589 PE=1 SV=1
sp|P36914|AMYG_ASPOR	3.36e-197	1	578	8	612	Glucoamylase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=glaA PE=2 SV=2
sp|P23176|AMYG_ASPKA	2.75e-187	19	578	24	639	Glucoamylase I OS=Aspergillus kawachii OX=1069201 GN=gaI PE=1 SV=1
sp|P22832|AMYG_ASPUS	1.57e-186	19	578	24	639	Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1
sp|P69327|AMYG_ASPAW	2.61e-185	19	578	24	640	Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000416	0.999556	CS pos: 18-19. Pr: 0.9759

TMHMM  Annotations     

There is no transmembrane helices in KDQ28034.1.