dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Aspergillus terreus

Lineage

Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus terreus

CAZyme ID

ATEG_00186-t26_1-p1

CAZy Family

AA11

CAZyme Description

predicted protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
348	CH476594\|CGC7	37919.98	4.6450

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AterreusNIH2624	10551	341663	150	10401

Gene Location

Enzyme Prediction help

EC	3.2.1.55:25	3.2.1.-:1

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH62	33	315	1.2e-115	0.9928057553956835

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
350101	GH62	1.42e-170	34	343	1	304	Glycosyl hydrolase family 62, characterized arabinofuranosidases. The glycosyl hydrolase family 62 (GH62) includes eukaryotic (mostly fungal) and prokaryotic enzymes which are characterized arabinofuranosidases (alpha-L-arabinofuranosidases; EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose side chains from xylans. These enzymes show significantly different substrate preference with rather low specific activity towards natural substrates and differ in catalytic efficiency. They do not act on xylose moieties in xylan that are adorned with an arabinose side chain at both O2 and O3 positions, nor do they display any non-specific arabinofuranosidase activity. The synergistic action in biomass degradation makes GH62 promising candidates for biotechnological improvements of biofuel production and in various biorefinery applications. These enzymes also contain carbohydrate binding modules (CBMs) that bind cellulose or xylan.
281639	Glyco_hydro_62	1.77e-64	34	314	3	271	Glycosyl hydrolase family 62. Family of alpha -L-arabinofuranosidase (EC 3.2.1.55). This enzyme hydrolyzed aryl alpha-L-arabinofuranosides and cleaves arabinosyl side chains from arabinoxylan and arabinan.
350092	GH_F	6.73e-11	60	306	1	242	Glycosyl hydrolase families 43 and 62 form CAZY clan GH-F. This glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) includes family 43 (GH43) and 62 (GH62). GH43 includes enzymes with beta-xylosidase (EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanases (beta-xylanases) and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. GH62 includes enzymes characterized as arabinofuranosidases (alpha-L-arabinofuranosidases; EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose side chains from xylans. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many of the enzymes in this family display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. GH62 are also predicted to be inverting enzymes. A common structural feature of both, GH43 and GH62 enzymes, is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
350153	GH43_GsAbnA-like	6.14e-04	61	140	3	95	Glycosyl hydrolase family 43 protein such as Geobacillus stearothermophilus endo-alpha-1,5-L-arabinanase AbnA. This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes with alpha-L-arabinofuranosidase (ABF; EC 3.2.1.55) and endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activities. It includes Geobacillus stearothermophilus T-6 NCIMB 40222 AbnA, Bacillus subtilis subsp. subtilis str. 168 (Abn2;YxiA;J3A;BSU39330) (Arb43B), and Thermotoga petrophila RKU-1 (AbnA;TpABN;Tpet_0637). These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the ABF enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. Many of these enzymes are different from other arabinases; they are organized into two different domains with a divalent metal cluster close to the catalytic residues to guarantee the correct protonation state of the catalytic residues and consequently the enzyme activity. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
350097	GH43_Bt3655-like	0.005	40	158	125	237	Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 arabinofuranosidase Bt3655. This glycosyl hydrolase family 43 (GH43)-like family includes the characterized arabinofuranosidases (EC 3.2.1.55): Bacteroides thetaiotaomicron VPI-5482 (Bt3655;BT_3655) and Penicillium chrysogenum 31B Abf43B, as well as Bifidobacterium adolescentis ATCC 15703 beta-xylosidase (EC 3.2.1.37) BAD_1527. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 includes enzymes with beta-xylosidase (EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanases (beta-xylanases) and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
1.34e-180	33	348	58	372
1.28e-179	33	348	82	396
2.41e-178	25	348	18	341
1.43e-177	25	348	9	332
2.16e-168	33	346	32	345

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
5.00e-166	34	348	1	316	Chain A, Glycosyl hydrolase family 62 protein [Coprinopsis cinerea okayama7#130],5B6S_B Chain B, Glycosyl hydrolase family 62 protein [Coprinopsis cinerea okayama7#130],5B6T_A Chain A, Glycosyl hydrolase family 62 protein [Coprinopsis cinerea okayama7#130],5B6T_B Chain B, Glycosyl hydrolase family 62 protein [Coprinopsis cinerea okayama7#130]
2.40e-148	24	348	10	337	Chain A, GH62 arabinofuranosidase [Podospora anserina],4N4B_A Chain A, GH62 arabinofuranosidase [Podospora anserina]
7.30e-136	37	343	23	342	Crystal structure of GH62 hydrolase in complex with xylotriose [Mycothermus thermophilus]
1.38e-133	37	343	23	342	Crystal structure of GH62 hydrolase from thermophilic fungus Scytalidium thermophilum [Mycothermus thermophilus]
1.48e-71	34	341	141	434	Crystal Structure of Streptomyces coelicolor alpha-L-arabinofuranosidase [Streptomyces coelicolor A3(2)],3WMZ_A Crystal Structure of Streptomyces coelicolor alpha-L-arabinofuranosidase ethylmercury derivative [Streptomyces coelicolor A3(2)],3WN0_A Crystal Structure of Streptomyces coelicolor alpha-L-arabinofuranosidase in complex with L-arabinose [Streptomyces coelicolor A3(2)],3WN1_A Crystal Structure of Streptomyces coelicolor alpha-L-arabinofuranosidase in complex with xylotriose [Streptomyces coelicolor A3(2)],3WN2_A Crystal Structure of Streptomyces coelicolor alpha-L-arabinofuranosidase in complex with xylohexaose [Streptomyces coelicolor A3(2)]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
3.08e-71	34	341	323	615	Alpha-L-arabinofuranosidase C OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=xynC PE=1 SV=2
3.13e-71	31	341	27	328	Probable alpha-L-arabinofuranosidase axhA OS=Aspergillus tubingensis OX=5068 GN=axhA PE=1 SV=1
1.95e-70	34	341	178	471	Extracellular exo-alpha-L-arabinofuranosidase OS=Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) OX=100226 GN=abfB PE=1 SV=1
1.20e-69	26	341	22	324	Probable alpha-L-arabinofuranosidase axhA-1 OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=axhA-1 PE=3 SV=2
4.23e-69	34	341	178	471	Extracellular exo-alpha-L-arabinofuranosidase OS=Streptomyces lividans OX=1916 GN=abfB PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000272	0.999700	CS pos: 31-32. Pr: 0.4736

TMHMM Annotations help

There is no transmembrane helices in ATEG_00186-t26_1-p1.

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