CAZyme Information: MGYG000003521_01420

Basic Information

• Species: Parabacteroides sp900770835
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides sp900770835
• CAZyme ID: MGYG000003521_01420
• CAZy Family: GH43
• CAZyme Description: Beta-xylosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
513	MGYG000003521_433|CGC1	57957.16	5.4807

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003521	2802496	MAG	Fiji	Oceania

• Gene Location: Start: 1747; End: 3288 Strand: +

Full Sequence      

MKKCIYILTFAALFAWESKAQKESYFTNPVIHGDVADPSILRDGTTYYATGTSSEWAPYY
PIFRSTDLINWQPIGHVFTEKPAWTKSSFWAPEWFQHKGKTYVYYTARKQADNQSCIGVA
VADSPEGPFIDKGPIVEFGKEAIDAFILEDKGELYISWKAYGLDDRPIELLAARLSDDGL
RIEGEPFSLLRDDERQGMEGQHWFKQGDYYYLLYSIRGCCGPMSDYAVSVARSKRLEGPY
EKYEGNPILHGSESVRSIGHGTLTDTPDGRLYYLCHAYSEGSDFYQGRQPHLQALRIGED
LWPHFVTGEYANLSQPMPFPETAQKPIADFSDDFEGTALRAEWSWNYPYANVKALVGNGL
LRLSGQPISHPEAGAALCLRPTTAHYQMETVVLNQDESWKGIGLYGDDQNWISIGCQAEK
VAIKLRLNGKEQQLLEQHQLGPITHLRMEVTEGIQCRFLISRNGRDWQAIPLSLPAETTQ
ALTRWDRIARPGLYQSGKGEGCFGYVRLTAQSN

Enzyme Prediction     

No EC number prediction in MGYG000003521_01420.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH43	28	303	6.5e-119	0.99644128113879

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08999	GH43_ABN-like	1.69e-90	28	303	1	283	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.
pfam04616	Glyco_hydro_43	5.28e-85	26	303	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.
cd08991	GH43_HoAraf43-like	3.67e-62	36	300	1	275	Glycosyl hydrolase family 43 protein such as Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (HoAraf43;Hore_20580). This glycosyl hydrolase family 43 (GH43) subgroup includes Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (EC 3.2.1.55) (HoAraf43;Hore_20580). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. This GH43_ HoAraf43-like subgroup includes enzymes that have been annotated as having xylan-digesting beta-xylosidase (EC 3.2.1.37) and xylanase (endo-alpha-L-arabinanase, EC 3.2.1.8) activities. 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. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. 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	6.02e-59	28	287	1	277	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.
cd09002	GH43_XYL-like	5.88e-51	26	304	1	270	Glycosyl hydrolase family 43, beta-D-xylosidase (uncharacterized). This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have been annotated as having beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity. They are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. 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. 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
QUT55603.1	1.12e-260	5	497	4	497
QUR47469.1	3.19e-260	5	497	4	497
BBK92213.1	9.13e-260	5	497	4	497
QUT21817.1	1.30e-259	5	497	4	497
QIX64229.1	1.30e-259	5	497	4	497

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MS3_A	4.40e-30	23	467	27	485	Crystalstructure of the GH43 protein BlXynB mutant (K247S) from Bacillus licheniformis [Bacillus licheniformis DSM 13 = ATCC 14580],6MS3_B Crystal structure of the GH43 protein BlXynB mutant (K247S) from Bacillus licheniformis [Bacillus licheniformis DSM 13 = ATCC 14580]
6MS2_A	8.06e-30	23	467	27	485	Crystalstructure of the GH43 BlXynB protein from Bacillus licheniformis [Bacillus licheniformis DSM 13 = ATCC 14580]
1YIF_A	1.16e-28	27	477	4	491	CRYSTALSTRUCTURE OF beta-1,4-xylosidase FROM BACILLUS SUBTILIS, NEW YORK STRUCTURAL GENOMICS CONSORTIUM [Bacillus subtilis],1YIF_B CRYSTAL STRUCTURE OF beta-1,4-xylosidase FROM BACILLUS SUBTILIS, NEW YORK STRUCTURAL GENOMICS CONSORTIUM [Bacillus subtilis],1YIF_C CRYSTAL STRUCTURE OF beta-1,4-xylosidase FROM BACILLUS SUBTILIS, NEW YORK STRUCTURAL GENOMICS CONSORTIUM [Bacillus subtilis],1YIF_D CRYSTAL STRUCTURE OF beta-1,4-xylosidase FROM BACILLUS SUBTILIS, NEW YORK STRUCTURAL GENOMICS CONSORTIUM [Bacillus subtilis]
1GYD_B	1.31e-27	34	286	3	284	Structureof Cellvibrio cellulosa alpha-L-arabinanase [Cellvibrio japonicus]
1YI7_A	2.47e-27	24	414	2	421	Beta-d-xylosidase(selenomethionine) XYND from Clostridium Acetobutylicum [Clostridium acetobutylicum ATCC 824],1YI7_B Beta-d-xylosidase (selenomethionine) XYND from Clostridium Acetobutylicum [Clostridium acetobutylicum ATCC 824],1YI7_C Beta-d-xylosidase (selenomethionine) XYND from Clostridium Acetobutylicum [Clostridium acetobutylicum ATCC 824],1YI7_D Beta-d-xylosidase (selenomethionine) XYND from Clostridium Acetobutylicum [Clostridium acetobutylicum ATCC 824]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P94489	6.38e-28	27	477	4	491	Beta-xylosidase OS=Bacillus subtilis (strain 168) OX=224308 GN=xynB PE=1 SV=2
A7LXT8	2.20e-26	1	451	1	444	Non-reducing end alpha-L-arabinofuranosidase BoGH43A OS=Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153) OX=411476 GN=BACOVA_02654 PE=1 SV=1
P95470	2.35e-26	34	286	35	316	Extracellular exo-alpha-(1->5)-L-arabinofuranosidase ArbA OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=arbA PE=1 SV=1
A9ZND1	1.87e-25	28	385	7	391	Xylan 1,3-beta-xylosidase OS=Vibrio sp. OX=678 GN=xloA PE=1 SV=1
A7LXU0	3.76e-22	18	369	21	373	Non-reducing end alpha-L-arabinofuranosidase BoGH43B OS=Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153) OX=411476 GN=BACOVA_02656 PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000565	0.997332	0.001487	0.000200	0.000207	0.000186

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003521_01420.