CAZyme Information: SPBR_00343-t41_1-p1

Basic Information

• Species: Sporothrix brasiliensis
• Lineage: Ascomycota; Sordariomycetes; ; Ophiostomataceae; Sporothrix; Sporothrix brasiliensis
• CAZyme ID: SPBR_00343-t41_1-p1
• CAZy Family: AA1
• CAZyme Description: glucoamylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
630		67466.21	4.6658

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Sbrasiliensis5110	9231	1398154	140	9091

• Gene Location: location=AWTV01000008:225348-227372(+)

Full Sequence      

MVSSYVSVLLGGLAAAGQARAGSVDSFVAHEQTVALQGVLNNIGADGSLVPGAAAGLVVA
SPSKTNPNYFYTWTRDSALTLRMLVDELIFGNTKVQGVIEDYVKAQAVLQTVSNPSGTLL
PYGLGLGEPKFNVDGTRFNGAWGRPQRDGPALRAITLIDYCNWLLDRGEHKQVSEVIWPV
IANDISYVGQYWNTSGYDLWEEVYGSSFFTTQNHYKSLVAARQLADKIGATCTGCIEAPN
VLCFLQTFWNGDFLTANINVDSGRSGIDANTMLGAISVFDVAADCSHPSLQPCHSRSLAS
FKVFVDTFRNGSLYAVNEGVPSSAGVALGRYPEDVYFNGNPWYLITQGAAEFLYDAVAQW
TRQGAIAVDATSEAFFRDLYPAARAGETYRRNAKDTTKGKGAPPRAAFQAIVHAATAYAD
SFVAVAEKYTPRDGSLSEQFDKSTGQPLSAIDLTWSYAAFVTMARRRAGHYPKYSWTQSA
PAAVPSVCLASSTNGVYAPATAAGAPNVTASCTSGVLFVVNASTYYGENVYLVGNTTDLG
AWDLANAQPLSANNYTSERPEWFAEVQMTAGEYVSYVFVREEDCGQASIYETVNRTLLVP
ACDENATPNSPPLLTTDNAWTGPTGSSGGC

Enzyme Prediction     

EC	3.2.1.3:94	3.2.1.3:71

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH15	40	464	1e-71	0.9833795013850416
CBM20	516	603	1.9e-18	0.9333333333333333

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395586	Glyco_hydro_15	1.04e-117	34	465	2	417	Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99886	CBM20_glucoamylase	2.83e-30	516	610	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	3.96e-18	516	602	3	88	Starch binding domain.
119437	CBM20	1.10e-15	516	602	2	87	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	8.13e-15	514	601	1	84	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	2.22e-269	13	630	20	616
CAA48243.1|CBM20|GH15|3.2.1.3	2.22e-269	13	630	20	616
CAY05396.1|CBM20|GH15|3.2.1.3	2.22e-269	13	630	20	616
UQC75847.1|CBM20|GH15	5.42e-264	12	624	12	608
APA13257.1|CBM20|GH15	4.97e-261	23	630	31	616

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FHW_A	7.68e-271	13	630	20	616	Chain A, Glucoamylase P [Amorphotheca resinae],6FHW_B Chain B, Glucoamylase P [Amorphotheca resinae]
6FHV_A	3.71e-180	20	600	4	579	Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]
6FRV_A	3.97e-177	23	602	2	604	Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
2VN4_A	5.69e-167	23	601	1	584	Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
3EQA_A	4.74e-162	23	508	2	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	3.95e-270	13	630	20	616	Glucoamylase P OS=Amorphotheca resinae OX=5101 GN=GAMP PE=1 SV=1
sp|P22832|AMYG_ASPUS	3.80e-177	4	605	2	630	Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1
sp|P69328|AMYG_ASPNG	1.57e-176	4	602	2	628	Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1
sp|P69327|AMYG_ASPAW	1.57e-176	4	602	2	628	Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1
sp|P23176|AMYG_ASPKA	1.26e-172	4	605	2	630	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
0.000288	0.999705	CS pos: 21-22. Pr: 0.9708

TMHMM  Annotations     

There is no transmembrane helices in SPBR_00343-t41_1-p1.