CAZyme Information: PABG_03168-t30_1-p1

Basic Information

• Species: Paracoccidioides brasiliensis
• Lineage: Ascomycota; Eurotiomycetes; ; NA; Paracoccidioides; Paracoccidioides brasiliensis
• CAZyme ID: PABG_03168-t30_1-p1
• CAZy Family: GH18
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
648		70303.61	6.6821

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PbrasiliensisPb03	8548	482561	121	8427

• Gene Location: location=KN305534:1566070-1568273(+)

Full Sequence      

MLAFFHCAVWVLSLFRVVQAQSQNPLGLKATGSLDAWIAKESPYALQALLANIGADGAKA
KGAAAGIVIASPSKSDPDYFFTWTRDAALVFKGLVDAFISGNTGLQPKLHEFINSQARLQ
TVSNPSGGLSSGGPGEPKFHVDMSPFNGDWGRPQRDGPALRATAMISYARWLVANGYSDT
AKSIVWPVVQNDLSYVSQFWSFSGYDLWEEINSVSFFTTAVQHRALVEGARLARQLGLTC
PNCESQAPQILCSLQNYWTGSYINSNTGGGRSGKDTNSILASIHTFDPEAACDDTTFQPC
SAKSLANHKVVTDAFRSIYALNSGIPAGSAVSVGRYPEDLYYGGNPWYLSTFAAAEQLYD
AIYQWQKIGSISITNVSLPFFRDVYGSAMIGTYSSSSSAFKSIIEAVRNYADGFLAIAQK
YTPESGALAEQFSRDTGTPLSAGDLTWSYASFLTAIARRSSIVPDPWGETEANGIPKTCQ
ATSAIGPYITATNTNWPSNLTPIKRTATPTSTSTASTTSSFPCVTPGSVNVTFNQIATTL
FGQTILLVGSIPELGSWAPGSAIALSADQYTDANHLWYKTITLSAGQKFEYKYIRKETGG
DIVWEGGSNRLYTVPRGCNIYTARREDNWRSQWAFYTEETQTWHARKD

Enzyme Prediction     

EC	3.2.1.3:94	1.14.99.55:4

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH15	49	456	6.3e-77	0.9861495844875346
CBM20	529	618	3.2e-27	0.9555555555555556

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395586	Glyco_hydro_15	2.71e-124	45	456	3	416	Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99886	CBM20_glucoamylase	1.05e-44	523	618	1	96	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	2.05e-34	529	623	1	94	Starch binding domain.
99883	CBM20_alpha_amylase	1.85e-28	529	630	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.
119437	CBM20	1.89e-26	531	629	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
QSS67842.1|CBM20|GH15	0.0	23	630	35	646
QSS49369.1|CBM20|GH15	0.0	23	630	35	646
QSS60609.1|CBM20|GH15	4.71e-288	23	630	78	617
EDP53734.1|CBM20|GH15	9.05e-287	8	630	7	631
CAC28076.1|CBM20|GH15|3.2.1.3	3.75e-285	20	629	18	617

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FRV_A	3.50e-242	33	630	2	616	Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
2VN4_A	1.37e-232	33	631	1	599	Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
6FHV_A	1.30e-216	32	620	6	584	Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]
1AGM_A	2.84e-214	33	498	2	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	2.95e-214	33	498	2	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|P0DN29|AMYG_ARTBC	1.82e-264	46	630	39	610	Glucoamylase ARB_02327-1 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_02327-1 PE=1 SV=1
sp|P36914|AMYG_ASPOR	4.53e-263	24	630	21	612	Glucoamylase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=glaA PE=2 SV=2
sp|P22832|AMYG_ASPUS	1.41e-246	11	630	6	639	Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1
sp|P23176|AMYG_ASPKA	1.32e-244	11	630	6	639	Glucoamylase I OS=Aspergillus kawachii OX=1069201 GN=gaI PE=1 SV=1
sp|P69327|AMYG_ASPAW	1.04e-241	11	630	6	640	Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000282	0.999719	CS pos: 20-21. Pr: 0.9819

TMHMM  Annotations     

There is no transmembrane helices in PABG_03168-t30_1-p1.