CAZyme Information: MGYG000000098_03390

Basic Information

• Species: Bacteroides bouchesdurhonensis
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides bouchesdurhonensis
• CAZyme ID: MGYG000000098_03390
• CAZy Family: GH43
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
624		70795.83	4.696

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000098	4868436	Isolate	Canada	North America

• Gene Location: Start: 25796; End: 27670 Strand: +

Full Sequence      

MKCRTMKKVLTKSLCMLAVFLLATACGKEDDTSQTDDNDNGDSKTSYVYLKKYGLEIIKV
SIQKEEYVYSLSILKGGDNTAFEGDVKISTWTEEELTAYNKNKGTSYVSIASDLYSVTPE
RQTFTKEQKSLNFDVKLIPEKLLKVIGENTKAEYVIPLRLESEDVEVKANRQDLLLYISL
EAPMLKFAFYEKTVFVQEESTSFNVGTVLNYKIDGKVSGSQWDFTSELVVPENAAELVTT
YNQSNKTDYELLPSEAYDLTEKVHYNINDTKAETTVVIDRDKMEVKYYLLPLKLSTPSSN
VVMCDNGILYCLVSRSYNNPIIAFSAPDPTVIHTDDGYFYLYGTEDTRNMPIYRSKDMVS
WEYMGTAFTNETRPTWEGEHSLWAPEIRHFDGRYVLYYSWAKWGDEWNSNVGVAVSDSPT
GPFIDKGCVIDAQDMGVQNSIDQFFYEDGGKKYMFWGSFRGIYVTELTDDGLRVKMNADG
TPVLKKRICGNYFEATNIYKKGEYYYLFASIGSCCEGAKSSYTTVVGRSKNVLGPYLNKT
GGDMLYDKYEVVLKGNSVWAGPGHNSIIQVDDDGVEWLIYHGYKKSEADNGRVVLLDRLH
WTDDGWPYVKDLAPSVSSLIPVFR

Enzyme Prediction     

No EC number prediction in MGYG000000098_03390.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH43	317	607	7.9e-104	0.9966555183946488

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18616	GH43_ABN-like	6.99e-143	319	601	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	1.27e-78	328	602	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	1.08e-73	327	601	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	4.28e-70	317	607	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.
cd08999	GH43_ABN-like	3.46e-61	319	608	1	284	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUR45032.1	1.03e-223	9	624	21	626
QUT26765.1	1.33e-222	16	624	1	599
QQR19270.1	1.67e-217	16	624	20	627
ANU59122.1	1.73e-217	16	624	21	628
QUT73032.1	1.34e-216	16	624	30	637

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1GYD_B	1.45e-44	328	617	6	311	Structureof Cellvibrio cellulosa alpha-L-arabinanase [Cellvibrio japonicus]
1GYH_A	1.50e-43	328	617	9	314	Structureof D158A Cellvibrio cellulosa alpha-L-arabinanase mutant [Cellvibrio japonicus],1GYH_B Structure of D158A Cellvibrio cellulosa alpha-L-arabinanase mutant [Cellvibrio japonicus],1GYH_C Structure of D158A Cellvibrio cellulosa alpha-L-arabinanase mutant [Cellvibrio japonicus],1GYH_D Structure of D158A Cellvibrio cellulosa alpha-L-arabinanase mutant [Cellvibrio japonicus],1GYH_E Structure of D158A Cellvibrio cellulosa alpha-L-arabinanase mutant [Cellvibrio japonicus],1GYH_F Structure of D158A Cellvibrio cellulosa alpha-L-arabinanase mutant [Cellvibrio japonicus]
1GYE_B	2.66e-43	328	617	7	312	Structureof Cellvibrio cellulosa alpha-L-arabinanase complexed with Arabinohexaose [Cellvibrio japonicus]
3CU9_A	1.09e-35	318	610	25	313	Highresolution crystal structure of 1,5-alpha-L-arabinanase from Geobacillus Stearothermophilus [Geobacillus stearothermophilus]
3D60_A	2.05e-35	320	610	27	313	ChainA, Intracellular arabinanase [Geobacillus stearothermophilus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P95470	3.33e-43	328	617	38	343	Extracellular exo-alpha-(1->5)-L-arabinofuranosidase ArbA OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=arbA PE=1 SV=1
B3EYM8	6.11e-35	318	610	26	314	Intracellular endo-alpha-(1->5)-L-arabinanase OS=Geobacillus stearothermophilus OX=1422 GN=abnB PE=1 SV=1
Q93HT9	2.06e-34	318	609	26	313	Intracellular endo-alpha-(1->5)-L-arabinanase OS=Geobacillus thermodenitrificans OX=33940 GN=abn-ts PE=1 SV=1
P94522	1.69e-33	328	607	44	321	Extracellular endo-alpha-(1->5)-L-arabinanase 1 OS=Bacillus subtilis (strain 168) OX=224308 GN=abnA PE=1 SV=3
A5AAG2	5.49e-20	326	609	28	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 LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000000	0.000007	1.000023	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000098_03390.