CAZyme Information: VBB77115.1

Basic Information

• Species: Podospora comata
• Lineage: Ascomycota; Sordariomycetes; ; Podosporaceae; Podospora; Podospora comata
• CAZyme ID: VBB77115.1
• CAZy Family: CE8
• CAZyme Description: Putative Glycoside Hydrolase Family 15

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
679		73892.90	6.4174

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PcomataTmat	13100	N/A	2652	10448

• Gene Location: location=LR026966:1659980-1662072(+)

Full Sequence      

MALFAVPNIIQDLIPAAASESINPWTWNLNLNASGLYEYLPTMHALSKFALLGACAVQSV
MGLPESVERREANLLKRNVDDWINRETPIAWEKLLCNIGPDGCAVRNQGVPAGVVVASPS
RSDPDYFYTWTRDAALVYKGLADAFRRNYTEDLHTQLKNFVSSQAKLQGVGNPAGGLNDG
QGLGEPKFMVDLKEFTGEWGRPQRDGPPLRAIALIRYAKWLVENGHKAVANAQVWPTIEN
DLKYSAQYWNQTGFDLWEEVPGSSFFTIASTHRALVEGAQLGAVLGKPTRAYTAVAPQVL
CFQQSFWNAREGFVVSNINGGEWRRGRDANSILTSIHNFDPSAGCDANTFQPCSDRALSN
HKVVVDSFRSIYNINRGIAQNKAVAVGRYSEDVFYNGNPWFLATFAAAEQLYDALLVWKA
QGSIAITQTSLPFFRDHVSGATVGTHAAGSATYNQIVSAITAYADGFIEVASKYAHSNGA
LNEQIDRNTGQPIAAPDLTWSYSAFLTATARRDGYIPTGWGAGQATALPAGQCQKFEVAG
NYNLPPTPVFPSNLTPAANAPVEQITAVPTGCTNPEKVFVTFNERASTSWGQVIKVVGNV
PELGSWDVNKAVPLSASKYTSGDPLWSITLPIQAGSSVQYKYIRITNGVAGVSWEGGDNR
AFSVPGATCDIQNRWDNWR

Enzyme Prediction     

EC	3.2.1.3:94	3.2.1.3:71

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH15	108	509	5.3e-71	0.9529085872576177
CBM20	578	666	1.1e-26	0.9333333333333333

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395586	Glyco_hydro_15	1.71e-131	88	508	1	415	Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99886	CBM20_glucoamylase	3.55e-40	572	675	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	2.37e-31	578	665	1	86	Starch binding domain.
119437	CBM20	1.22e-26	580	675	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	3.00e-26	578	679	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
VBB77115.1|CBM20|GH15	0.0	1	679	1	679
CDP27005.1|CBM20|GH15	0.0	1	679	1	679
CAP70412.1|GH15	1.00e-294	1	395	1	395
AEO61583.1|CBM20|GH15|3.2.1.3	2.44e-284	43	679	1	628
ACC34981.1|CBM20|GH15|3.2.1.3	3.53e-273	79	679	3	604

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VN4_A	1.27e-243	78	679	1	598	Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
6FRV_A	2.47e-199	79	675	3	615	Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
6FHV_A	9.88e-188	78	672	7	585	Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]
1AGM_A	2.62e-179	79	552	3	467	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	2.71e-179	79	552	3	467	GLUCOAMYLASE-471 COMPLEXED WITH ACARBOSE [Aspergillus awamori]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P14804|AMYG_NEUCR	1.94e-251	43	679	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|P36914|AMYG_ASPOR	1.35e-207	79	679	30	612	Glucoamylase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=glaA PE=2 SV=2
sp|P22832|AMYG_ASPUS	8.50e-200	76	675	24	638	Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1
sp|P69327|AMYG_ASPAW	1.00e-198	58	675	4	639	Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1
sp|P69328|AMYG_ASPNG	1.00e-198	58	675	4	639	Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999732	0.000312

TMHMM  Annotations     

There is no transmembrane helices in VBB77115.1.