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CAZyme Information: MGYG000000057_00330

You are here: Home > Sequence: MGYG000000057_00330

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Bacteroides sp002491635
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp002491635
CAZyme ID MGYG000000057_00330
CAZy Family GH43
CAZyme Description Extracellular exo-alpha-(1->5)-L-arabinofuranosidase ArbA
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
338 MGYG000000057_2|CGC3 37720.09 4.8889
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000057 4370351 Isolate United Kingdom Europe
Gene Location Start: 120342;  End: 121358  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000057_00330.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH43 39 322 2.6e-115 0.9966555183946488

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd18616 GH43_ABN-like 4.52e-163 41 317 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 1.10e-83 39 322 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 3.35e-83 50 318 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 2.17e-69 49 317 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.
cd08999 GH43_ABN-like 2.84e-61 41 323 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      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QQA29976.1 1.61e-247 1 338 1 335
QUT61486.1 1.61e-247 1 338 1 335
BBK86520.1 2.01e-247 1 338 7 341
QBJ18534.1 4.44e-247 1 338 1 334
QUT37325.1 9.30e-247 1 338 1 335

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1UV4_A 2.92e-38 45 323 9 292
NativeBacillus subtilis Arabinanase Arb43A [Bacillus subtilis]
1GYD_B 1.33e-37 50 326 6 303
Structureof Cellvibrio cellulosa alpha-L-arabinanase [Cellvibrio japonicus]
6B7K_A 3.71e-37 48 323 21 300
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]
1GYH_A 2.07e-36 50 326 9 306
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 1.44e-35 50 326 7 304
Structureof Cellvibrio cellulosa alpha-L-arabinanase complexed with Arabinohexaose [Cellvibrio japonicus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P94522 3.19e-37 45 323 39 322
Extracellular endo-alpha-(1->5)-L-arabinanase 1 OS=Bacillus subtilis (strain 168) OX=224308 GN=abnA PE=1 SV=3
P95470 1.45e-36 50 326 38 335
Extracellular exo-alpha-(1->5)-L-arabinofuranosidase ArbA OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=arbA PE=1 SV=1
B3EYM8 4.18e-34 50 322 27 311
Intracellular endo-alpha-(1->5)-L-arabinanase OS=Geobacillus stearothermophilus OX=1422 GN=abnB PE=1 SV=1
Q93HT9 5.58e-34 50 322 27 311
Intracellular endo-alpha-(1->5)-L-arabinanase OS=Geobacillus thermodenitrificans OX=33940 GN=abn-ts PE=1 SV=1
B8NDL1 2.45e-32 47 324 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

SignalP and Lipop Annotations help

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 1.000048 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000057_00330.