CAZyme Information: ASPTUDRAFT_40721-t33_1-p1

Basic Information

• Species: Aspergillus tubingensis
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus tubingensis
• CAZyme ID: ASPTUDRAFT_40721-t33_1-p1
• CAZy Family: GH5
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
332		36021.79	4.4508

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AtubingensisCBS134.48	12592	767770	274	12318

• Gene Location: location=KV878198:201962-202960(+)

Full Sequence      

MKFFNAKGSLLSSGIYLIALTPFVNAKCALPSSYSWSSTDALATPKSGWTALKDFTDVVS
DGKHIVYASTTDEAGNYGSMTFGAFSEWSNMASASQTATPFNAVAPTLFYFKPKSIWVLA
YQWGSSTFTYRTSQDPTNVNGWSSEQALFTGKISDSSTNAIDQTVIGDDTNMYLFFAGDN
GKIYRSSMSINDFPGSFGSQYEVILSGARNDLFEAVQVYTVDGGEGDSKYLMIVEAIGST
GHRYFRSFTASSLGGEWTAQAASEDQPFAGKANSGATWTEDISHGDLVRNNPDQTMTVDP
CNLQLLYQGHDPNSSGDYNLLPWKPGVLTLKQ

Enzyme Prediction     

EC	3.2.1.55:25	3.2.1.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH62	28	302	1.2e-130	0.9964028776978417

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
281639	Glyco_hydro_62	5.26e-177	28	302	1	272	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.
350101	GH62	2.02e-146	30	330	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.
350092	GH_F	1.37e-27	53	310	1	251	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAB01408.1|GH62|3.2.1.55	3.50e-245	1	332	1	332
CAA03159.1|GH62	3.50e-245	1	332	1	332
BCR93017.1|GH62	2.64e-240	1	332	1	332
BCS05676.1|GH62	2.64e-240	1	332	1	332
CAA03158.1|GH62|3.2.1.55	4.31e-230	1	332	1	332

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6F1J_A	5.76e-151	17	330	7	324	Structure of a Talaromyces pinophilus GH62 Arabinofuranosidase in complex with AraDNJ at 1.25A resolution [Talaromyces pinophilus],6F1J_B Structure of a Talaromyces pinophilus GH62 Arabinofuranosidase in complex with AraDNJ at 1.25A resolution [Talaromyces pinophilus]
5UBJ_A	1.29e-150	17	331	16	328	Structure of an alpha-L-arabinofuranosidase (GH62) from Aspergillus nidulans [Aspergillus nidulans FGSC A4]
4O8N_A	3.19e-150	26	332	81	384	Crystal structure of SthAraf62A, a GH62 family alpha-L-arabinofuranosidase from Streptomyces thermoviolaceus, in the apoprotein form [Streptomyces thermoviolaceus],4O8O_A Crystal structure of SthAraf62A, a GH62 family alpha-L-arabinofuranosidase from Streptomyces thermoviolaceus, bound to alpha-L-arabinose [Streptomyces thermoviolaceus],4O8P_A Crystal structure of SthAraf62A, a GH62 family alpha-L-arabinofuranosidase from Streptomyces thermoviolaceus, bound to xylotetraose [Streptomyces thermoviolaceus]
3WMY_A	1.42e-149	21	332	132	438	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)]
6CC7_A	3.60e-148	28	332	20	319	Structure of Fungal GH62 from Thielavia terretris [Thermothielavioides terrestris NRRL 8126]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P79021|AXHA_ASPTU	6.21e-246	1	332	1	332	Probable alpha-L-arabinofuranosidase axhA OS=Aspergillus tubingensis OX=5068 GN=axhA PE=1 SV=1
sp|A2QFV9|AXHA_ASPNC	7.66e-231	1	332	1	332	Probable alpha-L-arabinofuranosidase axhA OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=axhA PE=3 SV=1
sp|P79019|AXHA_ASPNG	7.66e-231	1	332	1	332	Alpha-L-arabinofuranosidase axhA OS=Aspergillus niger OX=5061 GN=axhA PE=2 SV=1
sp|Q0C8B3|AXHA_ASPTN	1.04e-169	26	331	24	325	Probable alpha-L-arabinofuranosidase axhA OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=axhA PE=3 SV=1
sp|Q2U7D2|AXHA_ASPOR	1.12e-169	17	331	17	327	Probable alpha-L-arabinofuranosidase axhA OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=axhA PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.036630	0.963330	CS pos: 26-27. Pr: 0.8914

TMHMM  Annotations     

There is no transmembrane helices in ASPTUDRAFT_40721-t33_1-p1.