CAZyme Information: MGYG000001376_01387

Basic Information

• Species: Dysgonomonas gadei
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae; Dysgonomonas; Dysgonomonas gadei
• CAZyme ID: MGYG000001376_01387
• CAZy Family: GH43
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
629	MGYG000001376_2|CGC12	70017.98	4.8769

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001376	5166013	Isolate	not provided	not provided

• Gene Location: Start: 689537; End: 691426 Strand: -

Full Sequence      

MKHYKWFSLLVICSLLFGACSDDDKDFGELGVIIETPVVSEITYSSAQLQATLSSAKDVI
LSKRGFCYSTKANPDIYDATVVATGNESFTATLTGLQGNTTYYVRAFVSIYNGGVAYSSE
IEVSTGEGTLDEQLAQYKAPAYADNYASIAAWDNRSQWNLANVHDPSVVLAKDGYYYMYQ
TDASYGNAHAGHGHFHARRSKDLVYWEYLGGTMKELPEWVIPKLNEIRKEMGLGETTSTG
ESEFGYWAPGVHKVNDNLYRMYYSIICPGLLNGEGTWGERAFIGMMENTDPANNDGWIDK
GYVVTNASDKGLNFNVQANDWANCYYKWNAIDPSYIVTPEGTHWLIYGSWHSGIVAMELN
AADGMPKQSLGVPWADTSAPAGYGQLIFTRQAGNRWQASEGPEIVYNPETGYYYLFVAYD
ALGVPYNTRVARSKSITGPYLGIDGTNVTAGGDMLPVVTHPYKFANSNGWVGISHCAVFN
DGNGNWYYSSQGRLPESVDNYIMMGHVRSIRWTKDGWPLVMPERYGAVPQVAITEEELVG
NWEHIDLSYSYGKQKESSVMTLTAEHTVSEGTWKDASWSYDAGKQVLTVNGVELYLQREV
DWEANPRTHTIVYAAYGGNFKTYWGKKTK

Enzyme Prediction     

EC	3.2.1.99

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH43	162	518	1.8e-87	0.9967741935483871

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08998	GH43_Arb43a-like	4.89e-80	163	513	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.
cd18616	GH43_ABN-like	9.00e-39	165	487	10	262	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.
cd18832	GH43_GsAbnA-like	1.88e-35	163	487	1	308	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	4.15e-34	163	513	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.
pfam04616	Glyco_hydro_43	1.95e-27	164	518	11	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QDO70915.1	0.0	1	629	1	630
QUT46357.1	0.0	1	629	1	630
QRQ48079.1	0.0	1	629	1	630
ALA73257.1	0.0	15	629	15	627
AII66060.1	0.0	15	629	15	627

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KC7_A	5.32e-34	161	625	31	469	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]
5HO9_A	2.89e-31	157	627	47	546	Structureof truncated AbnA (domains 1-3), a GH43 arabinanase from Geobacilllus stearothermophilus, in complex with arabinooctaose [Geobacillus stearothermophilus],5HO9_B Structure of truncated AbnA (domains 1-3), a GH43 arabinanase from Geobacilllus stearothermophilus, in complex with arabinooctaose [Geobacillus stearothermophilus]
5HO0_A	5.37e-31	157	627	47	546	Crystalstructure of AbnA (closed conformation), a GH43 extracellular arabinanase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5HO2_A Crystal structure of AbnA (open conformation), a GH43 extracellular arabinanase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5HOF_A Crystal structure of AbnA, a GH43 extracellular arabinanase from Geobacillus stearothermophilus, in complex with arabinopentaose [Geobacillus stearothermophilus],5HP6_A Structure of AbnA, a GH43 extracellular arabinanase from Geobacillus stearothermophilus (a new conformational state) [Geobacillus stearothermophilus]
2X8F_A	1.96e-29	162	627	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]
2X8T_A	8.83e-29	162	627	35	469	CrystalStructure of the Abn2 H318A mutant [Bacillus subtilis],2X8T_B Crystal Structure of the Abn2 H318A mutant [Bacillus subtilis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A5IKD4	8.23e-34	153	625	20	466	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	1.06e-28	162	627	35	469	Extracellular endo-alpha-(1->5)-L-arabinanase 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=abn2 PE=1 SV=2
Q93HT9	7.48e-27	158	518	17	311	Intracellular endo-alpha-(1->5)-L-arabinanase OS=Geobacillus thermodenitrificans OX=33940 GN=abn-ts PE=1 SV=1
B3EYM8	3.58e-26	158	518	17	311	Intracellular endo-alpha-(1->5)-L-arabinanase OS=Geobacillus stearothermophilus OX=1422 GN=abnB PE=1 SV=1
P95470	2.20e-18	162	520	35	333	Extracellular exo-alpha-(1->5)-L-arabinofuranosidase ArbA OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=arbA PE=1 SV=1

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	0.000016	1.000034	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001376_01387.