CAZyme Information: MGYG000000409_01456

Basic Information

• Species: QALS01 sp003150575
• Lineage: Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; Borkfalkiaceae; QALS01; QALS01 sp003150575
• CAZyme ID: MGYG000000409_01456
• CAZy Family: GH43
• CAZyme Description: Extracellular exo-alpha-(1->5)-L-arabinofuranosidase ArbA

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
359	MGYG000000409_8|CGC2	39021.66	5.0577

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000409	2691378	MAG	Sweden	Europe

• Gene Location: Start: 147254; End: 148333 Strand: +

Full Sequence      

MKKTFLAQVLCVFCTAVFCLAGCSAGGKPSSSDSETSSAEPEPVYVTNPLTQYDTADPHI
LRWEDSLYLYSTGGRVSRSDDGTTWQEIGKVGISPQWGTSGAGFWAPDIVRIGDKLLLYY
SLSTWGDTNPGIGVASADHPEGPWTDHGKLFNSKEIGVANSIDPCVFIGQDEKVYMIWGS
FYGCFGVELTEDGLGLKNGLEYARENKVLVSGAAGAAWDGSMFEGSYVIYKDGWYYYFGS
SGTCCEELRSTYHVRVGRSKNPLGPYVDSRGRALAGSGNVGDPILSGAGNFVGPGHNSIL
IDDLGYYYMVYHVWVNDNGTGKGRYLAMSRLEWDEDGWCSVKGNAPSKRVIAPYIKKSK

Enzyme Prediction     

No EC number prediction in MGYG000000409_01456.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH43	47	338	7.6e-82	0.9899665551839465

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18616	GH43_ABN-like	1.58e-112	48	333	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	8.19e-77	57	334	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	2.39e-55	56	320	1	266	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	7.70e-55	47	338	2	280	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	2.21e-52	48	338	1	282	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
QWB96294.1	7.92e-127	47	347	102	404
QWB96639.1	1.50e-93	85	356	10	288
QDO68166.1	1.87e-75	1	355	1	334
CBK67138.1	2.41e-75	31	359	22	354
QUT31494.1	2.41e-75	31	359	22	354

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6B7K_A	1.25e-34	57	338	23	298	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]
1GYD_B	8.90e-34	52	341	1	301	Structureof Cellvibrio cellulosa alpha-L-arabinanase [Cellvibrio japonicus]
1GYH_A	1.33e-32	52	341	4	304	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]
1WL7_A	1.65e-31	57	338	26	309	Structureof the thermostable arabinanase [Geobacillus thermodenitrificans]
1GYE_B	1.75e-31	52	341	2	302	Structureof Cellvibrio cellulosa alpha-L-arabinanase complexed with Arabinohexaose [Cellvibrio japonicus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P95470	1.28e-33	52	341	33	333	Extracellular exo-alpha-(1->5)-L-arabinofuranosidase ArbA OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=arbA PE=1 SV=1
Q93HT9	9.22e-31	57	338	27	310	Intracellular endo-alpha-(1->5)-L-arabinanase OS=Geobacillus thermodenitrificans OX=33940 GN=abn-ts PE=1 SV=1
B3EYM8	4.97e-30	57	338	27	310	Intracellular endo-alpha-(1->5)-L-arabinanase OS=Geobacillus stearothermophilus OX=1422 GN=abnB PE=1 SV=1
P94522	7.96e-29	57	340	44	322	Extracellular endo-alpha-(1->5)-L-arabinanase 1 OS=Bacillus subtilis (strain 168) OX=224308 GN=abnA PE=1 SV=3
A1DHW8	9.63e-29	41	336	43	359	Probable arabinan endo-1,5-alpha-L-arabinosidase B OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=abnB PE=3 SV=2

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	0.000000	1.000069	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000409_01456.