CAZyme Information: AEO61583.1

Basic Information

• Species: Thermothelomyces thermophilus
• Lineage: Ascomycota; Sordariomycetes; ; Chaetomiaceae; Thermothelomyces; Thermothelomyces thermophilus
• CAZyme ID: AEO61583.1
• CAZy Family: GT35
• CAZyme Description: glycoside hydrolase family 15 protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
628	CP003008|CGC6	66994.57	4.9417

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TthermophilusATCC42464	9292	573729	195	9097

• Gene Location: location=CP003008:1578424-1580597(+)

Full Sequence      

MHALSSLAVLGAWAVQTVLGRPATLSKRATDSFIETETPIAWEKLRCNIGANGCAASGAA
AGVVIASPSKSDPDYFYTWTRDAGLVLTGIVDALSQNYSAALQTNIQDYIIAQAKLQGVS
NPSGSLSDGTGLGEPKFNVDLTQFTGDWGRPQRDGPPLRAIALIRYAKWLASNGYKDTAN
SVVWPVIKNDLAYAAQYWNETGFDLWEEVPGSSFFTIASTHRALVEGAALAAQLGTECSA
CITVAPQVLCFQQSFWNPSGGYVVSNINGGNNRSGKDLNSVLASIHTFDPAVGCDSVTFQ
PCSDKALSNHKAYVDSFRSVYAINSGIAQGKAVAVGRYSEDVYYNGNPWYLANFAAAEQL
YDAVFVWKKQQSIEVTQLSLPFFKDLLPGISTGTYTPSSSTYQQILDAVSAYADGFIDVA
AKYTPSDGSLAEQYTRDSGQPISAKDLTWSYAAFLSAADRRAGIVPAGWSAEHGKTLPGS
CSAVQVAGTYTQATATSFPPGQTPNPTSDTPAPFPTACADSTQVFVTFRAEVTTQWGQSV
KVVGSSSELGNWDVSKAPRLSASAYTASDPLWAITVPMKAGQSVQYKFVKVNGDGSIQWE
SDPNRQFTVSSSSTASGCAWQTIEATWR

Enzyme Prediction     

EC	3.2.1.3:94	3.2.1.1:13

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH15	53	458	2.4e-74	0.96398891966759
CBM20	524	614	1.6e-28	0.9666666666666667

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395586	Glyco_hydro_15	1.10e-138	39	458	1	416	Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99886	CBM20_glucoamylase	1.09e-42	518	627	1	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.
395557	CBM_20	5.03e-35	524	616	1	92	Starch binding domain.
119437	CBM20	1.93e-30	526	627	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.
99883	CBM20_alpha_amylase	2.29e-27	524	628	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AEO61583.1|CBM20|GH15|3.2.1.3	0.0	1	628	1	628
ACC34981.1|CBM20|GH15|3.2.1.3	7.57e-317	29	628	2	604
AEO71343.1|CBM20|GH15	4.19e-315	1	628	1	657
AAA33386.1|CBM20|GH15|3.2.1.3	1.43e-306	1	628	1	620
CAY05382.1|CBM20|GH15|3.2.1.3	1.43e-306	1	628	1	620

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VN4_A	4.86e-267	29	628	1	598	Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
6FRV_A	3.18e-225	31	628	4	616	Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
6FHV_A	3.48e-201	33	607	11	576	Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]
3EQA_A	6.52e-198	31	499	4	467	Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol [Aspergillus niger]
1AGM_A	9.87e-195	31	499	4	466	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|P14804|AMYG_NEUCR	6.30e-288	1	628	1	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|P69328|AMYG_ASPNG	2.85e-226	20	628	16	640	Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1
sp|P69327|AMYG_ASPAW	2.85e-226	20	628	16	640	Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1
sp|P36914|AMYG_ASPOR	1.01e-224	14	611	19	598	Glucoamylase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=glaA PE=2 SV=2
sp|P22832|AMYG_ASPUS	2.94e-223	20	628	16	639	Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000448	0.999498	CS pos: 28-29. Pr: 0.6245

TMHMM  Annotations     

There is no transmembrane helices in AEO61583.1.