CAZyme Information: MGYG000000029_02684

Basic Information

• Species: Bacteroides finegoldii
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides finegoldii
• CAZyme ID: MGYG000000029_02684
• CAZy Family: GH43
• CAZyme Description: Extracellular endo-alpha-(1->5)-L-arabinanase 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
335		37455.68	9.1597

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000029	4415875	Isolate	United Kingdom	Europe

• Gene Location: Start: 53607; End: 54614 Strand: -

Full Sequence      

MKKYVNLFVFVFMIGACLSQGRAQTKSAVSYKNPVVDIAMPDPTVIKAADGYFYVYATES
TRNVPIMKSKDLVEWTYCNTAFTNKTRPRFEPKAGIWAPDINYINGKYVLYYAMSVWGGE
QTCGIGVATANSPQGPFTDHGKMFRSNEIGVQNSIDPSLLQYEGRNYLVWGSFRGIYVIE
LTADGLSIMPGAKKKRIAGTAFEAVYIHKHDDYYYMFASIGSCCQGVKSTYKVVVGRSKK
VWGPYKDKTGKPMLKNGYSLVIGANDHFVGNGHGSQIIRDDAGQDWLLYHGFSRSTPENG
RILLLDQIKWDQEGWPYVEGGSPSYETQKAPVFNN

Enzyme Prediction     

No EC number prediction in MGYG000000029_02684.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH43	31	316	6.4e-112	0.9966555183946488

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18616	GH43_ABN-like	3.27e-157	33	310	1	291	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.
cd08998	GH43_Arb43a-like	1.40e-87	42	311	3	278	Glycosyl hydrolase family 43 protein such as Bacillus subtilis subsp. subtilis str. 168 endo-alpha-1,5-L-arabinanase Arb43A. This glycosyl hydrolase family 43 (GH43) subgroup belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. 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. 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 such as the Bacillus subtilis arabinanase Abn2, that hydrolyzes sugar beet arabinan (branched), linear alpha-1,5-L-arabinan and pectin, 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.
cd08988	GH43_ABN	7.89e-77	41	310	1	277	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.
pfam04616	Glyco_hydro_43	1.63e-74	31	316	1	281	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.
cd18830	GH43_CjArb43A-like	1.38e-71	42	311	3	291	Glycosyl hydrolase family 43 protein such as Cellvibrio japonicus Ueda107 endo-alpha-1,5-L-arabinanase / exo-alpha-1,5-L-arabinanase 43A (ArbA;CJA_0805) (Arb43A). This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes annotated with alpha-L-arabinofuranosidase (ABF; EC 3.2.1.55) and endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activities, and includes the bifunctional Cellvibrio japonicus Ueda107 endo-alpha-1,5-L-arabinanase / exo-alpha-1,5-L-arabinanase 43A (ArbA;CJA_0805) (Arb43A). 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 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 such as the Bacillus subtilis arabinanase Abn2, that hydrolyzes sugar beet arabinan (branched), linear alpha-1,5-L-arabinan and pectin, 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGT72419.1	1.75e-257	1	335	1	335
QUT79338.1	2.49e-257	1	335	1	335
QDM10261.1	2.49e-257	1	335	1	335
QDH53398.1	7.13e-257	1	335	1	335
ALJ47623.1	7.13e-257	1	335	1	335

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6B7K_A	2.42e-43	42	316	23	299	GH43Endo-Arabinanase from Bacillus licheniformis [Bacillus licheniformis DSM 13 = ATCC 14580],6B7K_B GH43 Endo-Arabinanase from Bacillus licheniformis [Bacillus licheniformis DSM 13 = ATCC 14580],6B7K_C GH43 Endo-Arabinanase from Bacillus licheniformis [Bacillus licheniformis DSM 13 = ATCC 14580],6B7K_D GH43 Endo-Arabinanase from Bacillus licheniformis [Bacillus licheniformis DSM 13 = ATCC 14580]
1UV4_A	1.08e-42	42	316	14	291	NativeBacillus subtilis Arabinanase Arb43A [Bacillus subtilis]
1WL7_A	2.57e-41	37	318	21	312	Structureof the thermostable arabinanase [Geobacillus thermodenitrificans]
1GYD_B	2.76e-41	42	319	6	302	Structureof Cellvibrio cellulosa alpha-L-arabinanase [Cellvibrio japonicus]
3CU9_A	7.42e-41	37	318	21	312	Highresolution crystal structure of 1,5-alpha-L-arabinanase from Geobacillus Stearothermophilus [Geobacillus stearothermophilus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P94522	1.23e-41	42	316	44	321	Extracellular endo-alpha-(1->5)-L-arabinanase 1 OS=Bacillus subtilis (strain 168) OX=224308 GN=abnA PE=1 SV=3
Q93HT9	1.44e-40	37	318	22	313	Intracellular endo-alpha-(1->5)-L-arabinanase OS=Geobacillus thermodenitrificans OX=33940 GN=abn-ts PE=1 SV=1
P95470	3.14e-40	42	319	38	334	Extracellular exo-alpha-(1->5)-L-arabinofuranosidase ArbA OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=arbA PE=1 SV=1
B3EYM8	4.16e-40	37	318	22	313	Intracellular endo-alpha-(1->5)-L-arabinanase OS=Geobacillus stearothermophilus OX=1422 GN=abnB PE=1 SV=1
A5AAG2	4.33e-26	42	318	30	317	Probable arabinan endo-1,5-alpha-L-arabinosidase C OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=abnC PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000741	0.536615	0.461683	0.000367	0.000320	0.000254

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000029_02684.