CAZyme Information: EXJ71522.1

Basic Information

• Species: Cladophialophora psammophila
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Cladophialophora; Cladophialophora psammophila
• CAZyme ID: EXJ71522.1
• CAZy Family: GH47
• CAZyme Description: Glucoamylase [Source:UniProtKB/TrEMBL;Acc:W9WTJ0]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
618		67461.18	6.4870

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CpsammophilaCBS110553	13421	1182543	0	13421

• Gene Location: location=AMGX01000007:865111-867150(-)

Full Sequence      

MLCSSQLLVGLLTLVAPSPALEKRQAPLSTFIPQEQAVSIQGVLANIGGLNSTWVPGASP
GVVVASPSTVNPNYFYTWTRDSALTYRMLIEELVFGNLTLRKTIEDYTTAQAILQTVTNP
SGSLWPAGDGLGEAKFYTNLTRFDGTWGRPQRDGPALRAIAFMDLAPVLFKLNETALYKQ
IYWPLVLNDLRYLGQYWNQTGYDLWEEVHGSSFFTIANQHRALVQGALLARQLNTTCSPC
AQAPQVLCFLQNYFWNATGGYLTADVNVNNVVRSGINSDPILASISVFDANATCNASDFQ
PCNSKMLATHKVLVDSFRNLYPINKNAPPPHAVLIGRYPEDTYYGGNPWPLCTLGAAEML
YDAVHQIRTAGQLTVDNYSLPFFTDLFPTISIGHYTGNVMNQILTNMTTYADGFVSAVQQ
HLPSNGSISEQFDRTTGFSTSASKLTWSFASFVTMSRRRAGQFPVSWGASRPLANTNLTR
GQCRGTSFNATGNYSPALAAGAPNVTKDCESEVIFSVNATTSFGQNIFILGNVTKLGGAL
NNADDIILPLNPGNYTSTSPEWYVDLWLKAGQFVAYQYVLQNGAQWMFEDHPVRTLQVGA
CGSGRVARANDVAAFPSS

Enzyme Prediction     

EC	3.2.1.3:94

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH15	57	455	4.1e-72	0.9473684210526315

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395586	Glyco_hydro_15	5.12e-114	37	457	1	417	Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99886	CBM20_glucoamylase	6.07e-16	513	609	9	104	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.
395557	CBM_20	1.66e-12	513	604	3	91	Starch binding domain.
119437	CBM20	2.09e-11	513	606	2	92	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.
99883	CBM20_alpha_amylase	5.42e-11	511	603	1	87	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAA47945.1|CBM20|GH15|3.2.1.3	2.82e-189	9	606	12	600
CAA48243.1|CBM20|GH15|3.2.1.3	2.82e-189	9	606	12	600
CAY05396.1|CBM20|GH15|3.2.1.3	2.82e-189	9	606	12	600
APA13257.1|CBM20|GH15	5.65e-189	28	609	32	604
ATZ55778.1|CBM20|GH15	4.61e-185	28	612	32	604

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FHW_A	9.73e-191	9	606	12	600	Chain A, Glucoamylase P [Amorphotheca resinae],6FHW_B Chain B, Glucoamylase P [Amorphotheca resinae]
6FHV_A	8.90e-156	28	615	8	594	Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]
6FRV_A	7.13e-155	26	603	1	606	Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
2VN4_A	1.06e-152	31	601	5	587	Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
3EQA_A	5.37e-147	26	505	1	469	Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q03045|AMYG_AMORE	5.01e-190	9	606	12	600	Glucoamylase P OS=Amorphotheca resinae OX=5101 GN=GAMP PE=1 SV=1
sp|P69328|AMYG_ASPNG	2.75e-154	24	603	23	630	Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1
sp|P69327|AMYG_ASPAW	2.75e-154	24	603	23	630	Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1
sp|P22832|AMYG_ASPUS	3.76e-154	24	602	23	628	Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1
sp|P23176|AMYG_ASPKA	1.69e-152	24	602	23	628	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
0.000278	0.999663	CS pos: 24-25. Pr: 0.9670

TMHMM  Annotations     

There is no transmembrane helices in EXJ71522.1.