CAZyme Information: THD00150.1

Basic Information

• Species: Aspergillus tanneri
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus tanneri
• CAZyme ID: THD00150.1
• CAZy Family: GT4
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
310	SOSA01000005|CGC1	33426.75	7.0701

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AtanneriNIH1004	13590	N/A	33	13557

• Gene Location: location=SOSA01000005:114224-115223(-)

Full Sequence      

MSVLLTLLLPTVLAAPWKVLDDNFPDPSVIQTKDGFYAFGTTGNGVHAQIAHSKDFTSWE
KLSHDALPGPFPSWVKSESPSIWAPDVIQRNDGTFVMYFSAIAKDERKHCIGAATSSSVR
GPYKPAPNALACPIDQGGAIDAAGFKDSDGSFYVVYKIDGNSLNTHGGKKHPTPIMLQKL
HSDALTPSGKPVQLLDRDDRDGPLVEAPSLVKHGDTYLLSFSSNMYNTKWYDVSYATAKK
VTGPYTKSTAPLLESGHQSDVGKLVAPGGADFLPDGKRILFHAFNNGENMKKGRGVWAAD
ISIDGGQIHI

Enzyme Prediction     

No EC number prediction in THD00150.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH43	23	298	3.9e-95	0.9924528301886792

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
350113	GH43_ABN-like	2.40e-136	19	306	3	281	Glycosyl hydrolase family 43 protein such as endo-alpha-L-arabinanase. 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. 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. 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.
350105	GH43_HoAraf43-like	6.08e-39	25	310	1	279	Glycosyl hydrolase family 43 protein such as Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (HoAraf43;Hore_20580). This glycosyl hydrolase family 43 (GH43) subgroup includes Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (EC 3.2.1.55) (HoAraf43;Hore_20580). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. This GH43_ HoAraf43-like subgroup includes enzymes that have been annotated as having xylan-digesting beta-xylosidase (EC 3.2.1.37) and xylanase (endo-alpha-L-arabinanase, EC 3.2.1.8) 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.
398349	Glyco_hydro_43	3.87e-30	25	287	11	258	Glycosyl hydrolases family 43. The glycosyl hydrolase family 43 contains members that are arabinanases. Arabinanases hydrolyze the alpha-1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans. The structure of arabinanase Arb43A from Cellvibrio japonicus reveals a five-bladed beta-propeller fold. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
350102	GH43_ABN	4.02e-30	25	289	1	265	Glycosyl hydrolase family 43. 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. 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. 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.
350128	GH43_ABN-like	3.66e-29	19	285	3	269	Glycosyl hydrolase family 43 such as arabinan endo-1 5-alpha-L-arabinosidase. This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes with endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activity. 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. 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QMW38825.1|GH43_30	2.35e-145	3	310	9	321
UCK59362.1|GH43_30	2.35e-145	3	310	9	321
BAE55183.1|GH43_30	3.33e-145	3	310	9	321
QMW26746.1|GH43_30	1.92e-144	3	310	9	321
QRD87096.1|GH43_30	2.21e-144	3	310	13	325

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KC7_A	1.06e-15	17	156	30	188	Crystal Structure of Endo-1,5-alpha-L-arabinanase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],4KC7_B Crystal Structure of Endo-1,5-alpha-L-arabinanase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],4KC7_C Crystal Structure of Endo-1,5-alpha-L-arabinanase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],4KC8_A Crystal Structure of Endo-1,5-alpha-L-arabinanase from Thermotoga petrophila RKU-1 in complex with TRIS [Thermotoga petrophila RKU-1],4KC8_B Crystal Structure of Endo-1,5-alpha-L-arabinanase from Thermotoga petrophila RKU-1 in complex with TRIS [Thermotoga petrophila RKU-1],4KC8_C Crystal Structure of Endo-1,5-alpha-L-arabinanase from Thermotoga petrophila RKU-1 in complex with TRIS [Thermotoga petrophila RKU-1]
4COT_A	6.64e-14	26	254	38	276	The importance of the Abn2 calcium cluster in the endo-1,5- arabinanase activity from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168]
2X8F_A	6.66e-14	26	254	38	276	Native structure of Endo-1,5-alpha-L-arabinanases from Bacillus subtilis [Bacillus subtilis],2X8F_B Native structure of Endo-1,5-alpha-L-arabinanases from Bacillus subtilis [Bacillus subtilis]
2X8T_A	6.67e-14	26	254	38	276	Crystal Structure of the Abn2 H318A mutant [Bacillus subtilis],2X8T_B Crystal Structure of the Abn2 H318A mutant [Bacillus subtilis]
2X8S_A	3.91e-13	26	254	38	276	Crystal Structure of the Abn2 D171A mutant in complex with arabinotriose [Bacillus subtilis],2X8S_B Crystal Structure of the Abn2 D171A mutant in complex with arabinotriose [Bacillus subtilis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A5IKD4|EABN_THEP1	5.40e-15	17	156	27	185	Extracellular endo-alpha-(1->5)-L-arabinanase OS=Thermotoga petrophila (strain ATCC BAA-488 / DSM 13995 / JCM 10881 / RKU-1) OX=390874 GN=Tpet_0637 PE=1 SV=1
sp|P42293|EABN2_BACSU	3.42e-13	26	254	38	276	Extracellular endo-alpha-(1->5)-L-arabinanase 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=abn2 PE=1 SV=2
sp|B8NMD3|ABNC_ASPFN	5.28e-07	26	284	32	289	Probable arabinan endo-1,5-alpha-L-arabinosidase C OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=abnC PE=3 SV=2
sp|Q2U1X8|ABNC_ASPOR	5.28e-07	26	284	32	289	Probable arabinan endo-1,5-alpha-L-arabinosidase C OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=abnC PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000248	0.999705	CS pos: 14-15. Pr: 0.9773

TMHMM  Annotations     

There is no transmembrane helices in THD00150.1.