CAZyme Information: AGR57_8534T0-p1

Basic Information

• Species: Phanerochaete chrysosporium
• Lineage: Basidiomycota; Agaricomycetes; ; Phanerochaetaceae; Phanerochaete; Phanerochaete chrysosporium
• CAZyme ID: AGR57_8534T0-p1
• CAZy Family: GT2
• CAZyme Description: Glycoside Hydrolase Family 15 / Carbohydrate-Binding Module Family 20 protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
572		60800.51	5.0385

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PchrysosporiumRP-78	13602	273507	0	13602

• Gene Location: location=PchrRP-78_SC008:978890-980936(+)

Full Sequence      

MRFFALASLASLLTSALGQSSVDSYVASESPIAKAGLLANIGPNGAKSSGAKAGVVIASP
STTNPDYLYTWVRDSSLVFKVIVDQYAAGQDTSTRSLIDAFVSAEATLQQVTNPSGSVTT
GGLGEPKFNIDETAFTGSWGRPQRDGPALRSTAIINYANWLIANGNSSWVTSKLWPIIKL
DLDYVANNWNQSTFDLWEEVDSSSFFTTAVQHRALREGAALASKIGQTSVVSGYTTQAAN
LLCFLQSYWNPSAGYITANTGGGRSGKDANTVLASIHTFDPAAGCDANTFQPCSDKALSN
LKVYVDSFRSIYGVNSGIASNAAVATGRYPEDVYYNGNPWYLATFAVAEQLYDALIVWNK
QGSLTVTSTSLPFFKQFLSSVTAGTYASSTSTFKTLTSAVKTFADGFIAINAKYTPSNGG
LSEQFDKNSGVPTSAVDLTWSYASALTVFAARNGFASPSWGAQGLTVPTTCSASSGPTVA
VTFNVQATTVWGENIYLTGSVTALENWSPDNALLLSSANYPTWSITVNLPANTVVQYKYI
RKNNGAVTWESDPNNQITTPASGTFTVNDTWR

Enzyme Prediction     

EC	3.2.1.3:94	3.2.1.3:71

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH15	42	447	8.8e-76	0.9667590027700831
CBM20	479	564	3.3e-31	0.9666666666666667

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395586	Glyco_hydro_15	7.62e-141	31	449	1	416	Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99883	CBM20_alpha_amylase	3.73e-46	479	572	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.
395557	CBM_20	1.04e-35	479	569	1	95	Starch binding domain.
99886	CBM20_glucoamylase	1.73e-32	478	571	6	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.
119437	CBM20	3.82e-27	481	571	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
CAS91480.1|CBM20|GH15	0.0	1	572	1	579
BAU78332.1|CBM20|GH15	3.74e-311	19	572	18	573
BAM72726.1|CBM20|GH15	1.86e-301	12	572	11	580
AOC97459.1|CBM20|GH15	5.74e-300	12	572	12	578
BAL43555.1|CBM20|GH15|3.2.1.3	1.25e-298	18	572	19	576

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VN4_A	1.41e-212	21	572	1	598	Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
6FRV_A	2.12e-198	21	572	2	616	Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
1AGM_A	5.12e-183	21	475	2	452	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	5.30e-183	21	475	2	452	GLUCOAMYLASE-471 COMPLEXED WITH ACARBOSE [Aspergillus awamori]
1GAI_A	5.49e-183	21	475	2	452	GLUCOAMYLASE-471 COMPLEXED WITH D-GLUCO-DIHYDROACARBOSE [Aspergillus awamori]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|D8Q9M3|AMYG_SCHCM	1.16e-275	20	572	23	576	Glucoamylase ARB_02327-1 OS=Schizophyllum commune (strain H4-8 / FGSC 9210) OX=578458 GN=SCHCODRAFT_57589 PE=1 SV=1
sp|P22832|AMYG_ASPUS	8.47e-203	1	572	1	639	Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1
sp|P14804|AMYG_NEUCR	4.42e-202	21	572	36	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	7.83e-202	22	572	30	612	Glucoamylase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=glaA PE=2 SV=2
sp|P23176|AMYG_ASPKA	1.27e-199	1	572	1	639	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
0.000306	0.999664	CS pos: 18-19. Pr: 0.9793

TMHMM  Annotations     

There is no transmembrane helices in AGR57_8534T0-p1.