CAZyme Information: MGYG000002092_00238

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella
• CAZyme ID: MGYG000002092_00238
• CAZy Family: GH43
• CAZyme Description: Extracellular exo-alpha-(1->5)-L-arabinofuranosidase ArbA

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
341	MGYG000002092_15|CGC1	38340.79	6.4088

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002092	1925182	MAG	Mongolia	Asia

• Gene Location: Start: 3627; End: 4652 Strand: -

Full Sequence      

MYTHTIIVSAMLAMSTAASAQQQATTPHTQTATKATYTNPVTRTSLPDPTVERADDGYFY
LYATENIRNLPICRSRDLVDWTFVGTAFTDETRPQWNAKGNLWAPDINRIGGKYVLYYSK
STWGGEWDCGVGVATAERPEGPFTDRGPLFISREIGVQNSIDPFFITDHGRNYLFWGSFR
GIYGIELTADGTAVKPGAEKQQVAGTFMEGTYIHRRGKYYYLFGSTGSCCEGEKSTYRVT
VARSRHLFGPYTDRQGRPVMDNNFEVVVHRNDSVIGPGHNAEIVTDDHGDDWMLMHGFMS
SDPDSGRVTWLCQIKWRDGWPYVDGDSPAIEAPRPYFKPQK

Enzyme Prediction     

No EC number prediction in MGYG000002092_00238.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH43	37	321	7.2e-108	0.9966555183946488

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18616	GH43_ABN-like	1.06e-146	39	316	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.
pfam04616	Glyco_hydro_43	2.31e-74	37	321	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.
cd08998	GH43_Arb43a-like	7.36e-72	48	296	3	258	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	5.65e-69	47	302	1	264	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.
cd08999	GH43_ABN-like	1.72e-62	39	322	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
QQA08888.1	1.26e-150	36	337	25	325
AAO78006.1	1.26e-150	36	337	25	325
QCQ40040.1	1.26e-150	37	338	23	323
QMW85328.1	1.26e-150	36	337	25	325
ANQ62620.1	1.26e-150	37	338	23	323

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1GYD_B	2.15e-35	48	324	6	302	Structureof Cellvibrio cellulosa alpha-L-arabinanase [Cellvibrio japonicus]
1GYH_A	3.29e-34	48	324	9	305	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	1.17e-33	48	324	7	303	Structureof Cellvibrio cellulosa alpha-L-arabinanase complexed with Arabinohexaose [Cellvibrio japonicus]
4KCB_A	1.10e-32	42	324	128	441	CrystalStructure of Exo-1,5-alpha-L-arabinanase from Bovine Ruminal Metagenomic Library [uncultured bacterium],4KCB_B Crystal Structure of Exo-1,5-alpha-L-arabinanase from Bovine Ruminal Metagenomic Library [uncultured bacterium]
3CU9_A	8.58e-31	48	323	26	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
P95470	4.44e-34	48	324	38	334	Extracellular exo-alpha-(1->5)-L-arabinofuranosidase ArbA OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=arbA PE=1 SV=1
B8NDL1	5.15e-31	45	323	31	319	Probable arabinan endo-1,5-alpha-L-arabinosidase A OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=abnA PE=3 SV=1
Q2U8C6	5.15e-31	45	323	31	319	Probable arabinan endo-1,5-alpha-L-arabinosidase A OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=abnA PE=3 SV=1
B3EYM8	4.79e-30	48	323	27	313	Intracellular endo-alpha-(1->5)-L-arabinanase OS=Geobacillus stearothermophilus OX=1422 GN=abnB PE=1 SV=1
A2QT85	7.48e-30	51	323	38	321	Probable arabinan endo-1,5-alpha-L-arabinosidase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=abnA 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
0.000620	0.998431	0.000224	0.000270	0.000217	0.000199

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002092_00238.