CAZyme Information: MGYG000002256_02370

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; UBA3282
• CAZyme ID: MGYG000002256_02370
• CAZy Family: GH43
• CAZyme Description: Extracellular endo-alpha-(1->5)-L-arabinanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
286		31880.23	4.1379

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002256	2755304	MAG	Peru	South America

• Gene Location: Start: 2912; End: 3772 Strand: -

Full Sequence      

MVYGSWSGGIFLLELDPETGEVIHPQDDQAGRVDAYFGKKLMGGNHTSIEGPYIMYDEES
GYYYLFVSYGGLAREGGYQIRVFRSETIDGDYVDMNGEFPLDTQNYGQAPYGLKLSGNYN
LPSLEVAYMATGHNSAFVDDNGKKYIVNHTRFDNATEDHEPRVHQFLVNEEGWPCMLPYA
TSGETVSASGYDAQEVTGKYYLINQGTGIDAEIAQPVMIYLLEDGSVRGENVDGVWEKKE
DSYFMNITLGEKKYSGVFCQMKDEAGTDVMTFSAVGSNESIWGVKY

Enzyme Prediction     

No EC number prediction in MGYG000002256_02370.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH43	1	174	1.2e-63	0.532258064516129

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18832	GH43_GsAbnA-like	3.53e-86	1	169	160	332	Glycosyl hydrolase family 43 protein such as Geobacillus stearothermophilus endo-alpha-1,5-L-arabinanase AbnA. 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. It includes Geobacillus stearothermophilus T-6 NCIMB 40222 AbnA, Bacillus subtilis subsp. subtilis str. 168 (Abn2;YxiA;J3A;BSU39330) (Arb43B), and Thermotoga petrophila RKU-1 (AbnA;TpABN;Tpet_0637). 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. Many of these enzymes 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.
COG3507	XynB2	2.20e-42	1	286	160	448	Beta-xylosidase [Carbohydrate transport and metabolism].
cd08998	GH43_Arb43a-like	3.26e-30	1	155	132	264	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.
pfam16369	GH43_C	3.08e-28	178	283	1	106	C-terminal of Glycosyl hydrolases family 43. This is the C-terminal of Glycosyl hydrolases family 43. It is around 100 residues in length from various Bacteroides species. The function of this family is unknown.
cd08988	GH43_ABN	1.43e-27	1	166	133	275	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBL14030.1	2.21e-150	1	286	232	515
CBL08764.1	6.29e-150	1	286	232	515
VCV23479.1	6.29e-150	1	286	232	515
CBK74092.1	1.06e-146	1	286	1	284
AEN95753.1	4.01e-143	1	286	241	524

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2X8F_A	2.22e-71	1	285	184	469	Nativestructure 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]
2X8S_A	2.22e-71	1	285	184	469	CrystalStructure 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]
4COT_A	2.39e-70	1	285	184	469	Theimportance of the Abn2 calcium cluster in the endo-1,5- arabinanase activity from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168]
2X8T_A	7.02e-70	1	285	184	469	CrystalStructure of the Abn2 H318A mutant [Bacillus subtilis],2X8T_B Crystal Structure of the Abn2 H318A mutant [Bacillus subtilis]
3LV4_A	9.28e-63	2	283	162	440	Crystalstructure of the glycoside hydrolase, family 43 YxiA protein from Bacillus licheniformis. Northeast Structural Genomics Consortium Target BiR14. [Bacillus licheniformis DSM 13 = ATCC 14580],3LV4_B Crystal structure of the glycoside hydrolase, family 43 YxiA protein from Bacillus licheniformis. Northeast Structural Genomics Consortium Target BiR14. [Bacillus licheniformis DSM 13 = ATCC 14580]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P42293	1.19e-70	1	285	184	469	Extracellular endo-alpha-(1->5)-L-arabinanase 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=abn2 PE=1 SV=2
A5IKD4	3.95e-61	1	285	183	468	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

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.999933	0.000104	0.000001	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002256_02370.