CAZyme Information: MGYG000002455_00942

Basic Information

• Species: Bacteroides cellulosilyticus
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides cellulosilyticus
• CAZyme ID: MGYG000002455_00942
• CAZy Family: GH27
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
894	MGYG000002455_3|CGC6	101850.83	6.0973

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002455	6974062	Isolate	United States	North America

• Gene Location: Start: 273171; End: 275855 Strand: -

Full Sequence      

MNKRITLFLITLLTVCGVQSQNNNQNRNADFHKWAETPPMGWNSWDCFGANVTEAEVKAN
ADYMAEHLKDYGWEYIVVDIRWFVENQTTGYYNFKDPKYVLDEYGRYMPAVNRFPSAGNG
NGFKPLADYVHSKGLKFGIHLMRGVPTLAVEKKLPVKDAGGVTAADIYSTDWKCPWLGDN
YTIVADRPGAQEYYNSIFDLYASWGVDFVKIDDLSRPYHQAEIEMIRKAIDRTGRPIVLS
MSPGETDVNKADHAVGHANMWRTVDDFWDNWPHLYHQFEVCPKWAPYIGRGAWPDADMLP
LGHIDLRGNARMSKFTRDEQYMVMTLFAMFKSPLMFGGHLPDNDKFTNSLITNEEVLYVH
RNSVNNKQWYNKDGVIAWTADDPRNGDKYLALFYVDQKEPRESHPANRKVTVDLKELGFG
GAAKVRDIWRNQDIGNFSGTEFSPVINYHGAGLYRISKKLKVQTNNPIIQTKYTADPAPM
VHNDTVFLYSSHDDDNAKGFVMREWLLYTSTDMVNWTDHGVVASLKDFKWVPYDNGAWAP
QCIERNGKFYMYCPMPGGIGIGVLVADSPYGPFIDPIGKPLVKNSYADIDPTVLIDDDGQ
AYMYWGNPDLYYVKLNEDMISCDGEVVHEQMTHEAFGERKGNQKRPTLYEEGPWAYKRKN
KYYMAFASTCCPEGMGYSMSDSPTGPWVYKGMIMEGDRRSNGNHPGIIDYKGNTYVFGFN
YDIHFSKISQHYERRSICVEKLTFNPDGTIQQLPFWTAKGVDPVGKLDPYRRVEAETIAW
SEGLKTEKSEAGMYVTAIHDGDYIRVRNVDFKKGAKSFEAVAASSSSGGQIEIRLDDKEG
TLIGTCVIGNTGGPESWKTFQAQVDKVKGVHDVYFIFRGGEDELFNFDCWKFIR

Enzyme Prediction     

EC	3.2.1.88

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH43	466	750	5.9e-112	0.9964028776978417
GH27	196	434	2.5e-60	0.9475982532751092
CBM6	773	892	1.7e-33	0.8623188405797102

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18618	GH43_Xsa43E-like	1.64e-134	473	752	1	275	Glycosyl hydrolase family 43, including Butyrivibrio proteoclasticus arabinofuranosidase Xsa43E. This glycosyl hydrolase family 43 (GH43) subgroup belongs to the GH43_AXH-like subgroup which includes enzymes that have been characterized with beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55), alpha-1,2-L-arabinofuranosidase 43A (arabinan-specific; EC 3.2.1.-), endo-alpha-L-arabinanase as well as arabinoxylan arabinofuranohydrolase (AXH) 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. AXHs specifically hydrolyze the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl backbone residues of arabinoxylan. This subgroup includes Cellvibrio japonicus arabinan-specific alpha-1,2-arabinofuranosidase, CjAbf43A, which confers its specificity by a surface cleft that is complementary to the helical backbone of the polysaccharide, and Butyrivibrio proteoclasticus GH43 enzyme Xsa43E, also an arabinofuranosidase, which has been shown to cleave arabinose side chains from short segments of xylan. Several of these enzymes also contain carbohydrate binding modules (CBMs) that bind cellulose or xylan. 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.
cd14792	GH27	6.10e-101	38	361	1	270	glycosyl hydrolase family 27 (GH27). GH27 enzymes occur in eukaryotes, prokaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-N-acetylgalactosaminidase, and 3-alpha-isomalto-dextranase. All GH27 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH27 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.
cd08990	GH43_AXH_like	9.45e-96	475	752	1	269	Glycosyl hydrolase family 43 protein, includes arabinoxylan arabinofuranohydrolase, beta-xylosidase, endo-1,4-beta-xylanase, and alpha-L-arabinofuranosidase. This subgroup includes Bacillus subtilis arabinoxylan arabinofuranohydrolase (XynD;BsAXH-m23;BSU18160), Butyrivibrio proteoclasticus alpha-L-arabinofuranosidase (Xsa43E;bpr_I2319), Clostridium stercorarium alpha-L-arabinofuranosidase XylA, and metagenomic beta-xylosidase (EC 3.2.1.37) / alpha-L-arabinofuranosidase (EC 3.2.1.55) CoXyl43. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. The GH43_AXH-like subgroup includes enzymes that have been characterized with beta-xylosidase, alpha-L-arabinofuranosidase, endo-alpha-L-arabinanase as well as arabinoxylan arabinofuranohydrolase (AXH) 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. AXHs specifically hydrolyze the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl backbone residues of arabinoxylan. Metagenomic beta-xylosidase/alpha-L-arabinofuranosidase CoXyl43 shows synergy with Trichoderma reesei cellulases and promotes plant biomass saccharification by degrading xylo-oligosaccharides, such as xylobiose and xylotriose, into the monosaccharide xylose. Studies show that the hydrolytic activity of CoXyl43 is stimulated in the presence of calcium. Several of these enzymes also contain carbohydrate binding modules (CBMs) that bind cellulose or xylan. 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.
PLN02899	PLN02899	7.70e-83	35	370	28	386	alpha-galactosidase
PLN03231	PLN03231	9.23e-77	38	368	1	354	putative alpha-galactosidase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT88903.1	0.0	1	894	1	894
ALJ60088.1	0.0	1	894	1	894
QDH81067.1	8.58e-209	460	894	20	453
AYM99037.1	3.30e-203	462	892	22	460
APA00964.1	6.81e-202	452	894	10	441

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4NX0_A	1.23e-149	20	435	5	420	Crystalstructure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_B Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_C Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_D Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_E Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_F Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_G Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_H Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus]
4NXK_A	1.93e-148	20	435	5	420	Crystalstructure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_B Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_C Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_D Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_E Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_F Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_G Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_H Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NZF_A Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_B Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_C Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_D Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_E Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_F Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_G Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_H Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus]
3CC1_A	3.66e-125	35	429	9	401	ChainA, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125],3CC1_B Chain B, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125]
4NOV_A	6.58e-84	466	754	46	336	Xsa43E,a GH43 family enzyme from Butyrivibrio proteoclasticus [Butyrivibrio proteoclasticus B316]
3C7E_A	9.44e-70	462	894	10	486	Crystalstructure of a glycoside hydrolase family 43 arabinoxylan arabinofuranohydrolase from Bacillus subtilis. [Bacillus subtilis],3C7F_A Crystal structure of a glycoside hydrolase family 43 arabinoxylan arabinofuranohydrolase from bacillus subtilis in complex with xylotriose. [Bacillus subtilis],3C7H_A Crystal structure of glycoside hydrolase family 43 arabinoxylan arabinofuranohydrolase from Bacillus subtilis in complex with AXOS-4-0.5. [Bacillus subtilis],3C7O_A Crystal structure of a glycoside hydrolase family 43 arabinoxylan arabinofuranohydrolase from Bacillus subtilis in complex with cellotetraose. [Bacillus subtilis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q45071	9.86e-69	462	894	36	512	Arabinoxylan arabinofuranohydrolase OS=Bacillus subtilis (strain 168) OX=224308 GN=xynD PE=1 SV=2
P45796	4.60e-65	465	892	38	507	Arabinoxylan arabinofuranohydrolase OS=Paenibacillus polymyxa OX=1406 GN=xynD PE=1 SV=1
Q8VXZ7	2.19e-35	35	454	70	425	Alpha-galactosidase 3 OS=Arabidopsis thaliana OX=3702 GN=AGAL3 PE=1 SV=1
Q9FXT4	2.79e-35	17	429	43	389	Alpha-galactosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os10g0493600 PE=1 SV=1
P14749	6.16e-35	19	459	37	410	Alpha-galactosidase OS=Cyamopsis tetragonoloba OX=3832 PE=1 SV=1

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
0.000815	0.699435	0.298949	0.000314	0.000253	0.000213

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002455_00942.