CAZyme Information: KAG2009998.1

Basic Information

• Species: Coprinopsis cinerea
• Lineage: Basidiomycota; Agaricomycetes; ; Psathyrellaceae; Coprinopsis; Coprinopsis cinerea
• CAZyme ID: KAG2009998.1
• CAZy Family: GH11
• CAZyme Description: glucoamylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
575		63290.36	6.5035

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Ccinerea326	15250	N/A	238	15012

• Gene Location: location=JAAGWA010000007:1230639-1232763(-)

Full Sequence      

MRLFLTTALGLFSTFAGVNAQADPAADAYLARQVPISRAGVVANIGPDGARSSGARAGVV
IASPSTYDPDYLYTWTRDSALVFKGITERYIRGEDDSLRRRIDDFVAAQTILQGVTNPSG
SPTTGGLGEPKFHIDLTAFTDGWGRPQHDGPPLRAIALINYANHLVDTNNATWAAQRVWP
VIKNDLDYTAKYWNYTGFDLWEEVSGRSFFTSAVQLRALKEGVTLANRLQQNSAPYAEQV
ERVHCFLQSYWNPQQGYITANVGHRSGKDANTILASIHTFDPDAGCDATTFQPCSDKALS
NLKVVVDSFRNEYSINRGIPANQAVAVGRYHEDIYYGGQPWYLTTHAPAEQLYDALIVWD
RQESLEVTDISLAFFRQFDGSVQPGTYAKGSATYTALTNAVRRFADGFFLVNAKYTPADG
SLAEQYHRDHGYPLSAKHLTWSYASLLTAYAARSGQTPTRSWGAKDLVVPGQCVGNIGPT
AAITFRVHAETVWGENIFITGNIDALSGWSPDNAIPLAPTNYPTWTATIQIPVDTNFEYK
YIRKNGNAVVWESDPNRRNSSPSSGSKTINDSWKN

Enzyme Prediction     

EC	3.2.1.3:94	3.2.1.1:7	3.2.1.116:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH15	42	449	4.1e-74	0.9806094182825484
CBM20	483	567	2.4e-28	0.9555555555555556

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395586	Glyco_hydro_15	4.36e-125	35	449	1	415	Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99883	CBM20_alpha_amylase	1.14e-48	481	574	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	2.89e-32	482	571	2	95	Starch binding domain.
99886	CBM20_glucoamylase	5.72e-29	480	573	6	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	1.14e-27	483	573	2	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
CAS91480.1|CBM20|GH15	7.95e-244	5	574	6	579
AOC97459.1|CBM20|GH15	1.26e-242	27	574	24	578
BAU78332.1|CBM20|GH15	1.07e-237	26	574	22	573
BAE47183.1|CBM20|GH15|3.2.1.3	1.61e-231	1	573	1	569
CDJ79833.1|CBM20|GH15	7.26e-231	27	574	26	583

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VN4_A	6.02e-192	27	556	3	577	Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
6FRV_A	2.82e-173	27	574	4	616	Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
6FHV_A	3.86e-165	40	557	22	574	Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]
1GAI_A	1.04e-160	27	501	4	472	GLUCOAMYLASE-471 COMPLEXED WITH D-GLUCO-DIHYDROACARBOSE [Aspergillus awamori]
1AGM_A	1.95e-160	27	493	4	465	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|D8Q9M3|AMYG_SCHCM	7.10e-232	1	574	1	576	Glucoamylase ARB_02327-1 OS=Schizophyllum commune (strain H4-8 / FGSC 9210) OX=578458 GN=SCHCODRAFT_57589 PE=1 SV=1
sp|P14804|AMYG_NEUCR	7.12e-181	27	574	38	626	Glucoamylase OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=gla-1 PE=1 SV=3
sp|P36914|AMYG_ASPOR	4.70e-178	27	563	31	598	Glucoamylase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=glaA PE=2 SV=2
sp|P22832|AMYG_ASPUS	6.69e-174	27	574	28	639	Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1
sp|P23176|AMYG_ASPKA	1.90e-173	27	574	28	639	Glucoamylase I OS=Aspergillus kawachii OX=1069201 GN=gaI PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000471	0.999501	CS pos: 22-23. Pr: 0.8802

TMHMM  Annotations     

There is no transmembrane helices in KAG2009998.1.