CAZyme Information: MGYG000001514_02553

Basic Information

• Species: Paenibacillus_A ihumii
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A ihumii
• CAZyme ID: MGYG000001514_02553
• CAZy Family: GH43
• CAZyme Description: Extracellular endo-alpha-(1->5)-L-arabinanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
467	MGYG000001514_12|CGC18	52239.39	4.4821

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001514	5923787	Isolate	not provided	not provided

• Gene Location: Start: 1086855; End: 1088258 Strand: +

Full Sequence      

MPILMLVGLVGCSGKGTPQPVFPDPPGETAMYDTSVLHDEQKWTVNNAHDPGIIKTEDGY
YVFSTDVKVGGEPKPGVMVRKSADLIHWQWVGYALPGIPEEAGAWSSAVNLWAPDVVKHG
DEYRLYYSASTFGSRQSMIAMATSPSIEGPWTDQGAVLKTRSEDALNAIDPNIVTDTEGR
MWMVYGSFFGGIHIIELDPATGKPREEGFGTRIAARDPVTEDGAVEGPYIIYNEKFKKYY
LFVSYDSLFEDYNVRVARSDSITGPYVDYNGREMTDTEFQPQYEIGNKVLGGYKFGEDEG
WVAPGHNSVLKDGDDYYIVHHARGEVDKHWSYLHIRKILWTEDGWPVVSPERYAGEKEQD
IPEAMVAGEWQRIEIDPLVDGMIESDPLILHSDGKLEGRRGKGAWTFDGRRTLNLTWEEV
PEGEGRKASVQLLPSWDWEKGVQTLVFTGLDERGISIWGKREAPGES

Enzyme Prediction     

EC	3.2.1.99

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH43	47	346	9e-110	0.9967741935483871

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08998	GH43_Arb43a-like	1.68e-131	48	341	1	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.
cd18832	GH43_GsAbnA-like	6.65e-76	49	323	2	314	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.
cd18830	GH43_CjArb43A-like	5.31e-67	48	341	1	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.
cd18616	GH43_ABN-like	1.07e-65	44	340	4	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.
cd18829	GH43_BsArb43A-like	2.94e-61	48	322	1	254	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 includes mostly enzymes annotated as having endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activities, and includes Bacillus subtilis subsp. subtilis str. 168 endo-alpha-1,5-L-arabinanase (AbnA;BSU28810) (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 arabinofuranosidase (ABF; EC 3.2.1.55) 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
AZK49000.1	0.0	1	467	1	467
AIQ73134.1	1.70e-257	15	462	3	450
AWV32481.1	3.97e-256	15	462	3	450
AUS26057.1	7.89e-248	1	461	1	458
AIY11003.1	7.89e-248	1	461	1	458

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KC7_A	1.66e-69	42	461	29	471	CrystalStructure 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]
3LV4_A	6.69e-61	49	459	14	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]
2X8F_A	9.27e-61	47	461	35	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]
4COT_A	9.49e-60	47	461	35	469	Theimportance of the Abn2 calcium cluster in the endo-1,5- arabinanase activity from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168]
2X8S_A	1.36e-59	47	461	35	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A5IKD4	7.85e-70	36	461	17	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
P42293	4.96e-60	47	461	35	469	Extracellular endo-alpha-(1->5)-L-arabinanase 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=abn2 PE=1 SV=2
B3EYM8	5.08e-56	40	349	14	314	Intracellular endo-alpha-(1->5)-L-arabinanase OS=Geobacillus stearothermophilus OX=1422 GN=abnB PE=1 SV=1
Q93HT9	7.20e-55	40	346	14	311	Intracellular endo-alpha-(1->5)-L-arabinanase OS=Geobacillus thermodenitrificans OX=33940 GN=abn-ts PE=1 SV=1
P94522	8.45e-41	43	346	35	321	Extracellular endo-alpha-(1->5)-L-arabinanase 1 OS=Bacillus subtilis (strain 168) OX=224308 GN=abnA PE=1 SV=3

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	0.000001	1.000090	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001514_02553.