CAZyme Information: MGYG000002621_00486

Basic Information

• Species: Bacteroides ndongoniae
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides ndongoniae
• CAZyme ID: MGYG000002621_00486
• CAZy Family: GH43
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
935	MGYG000002621_3|CGC4	106034.69	5.3108

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002621	3633256	MAG	China	Asia

• Gene Location: Start: 190660; End: 193467 Strand: -

Full Sequence      

MNAKKILLMCLVGMCAVFSAYAQRTFVYEGNPLITDKFTADPAPLVHDGKLYLYVGHDEY
YDGQDTASGGKEFNITEWLCYSTEDMKTWTDHGSVLRPTDFKWAVGEAWASQVVEKDGKF
YYYTTVQGGGKYTGKAVGVAVADTPVGPFVDAIGKPLVSDDMTSNGARGWWNDIDPTVLI
EKNGQTWLCWGNGTCFMAKLKPNMIELDGEIKVIDLPKYVEGPWLHERNGIYYLTYASMG
KGRENISYATSKSMEGPWEYQGELTGMAENSFTIHPGIAEFKDKWYLFYHNAVLTIDGHK
GAIGRRSVCVDELFYNEDGTMKYVEQTRSISSPNGKIQLKYTTSAENHFSFDVNYMDAKG
QHEILSIPVIGMYTQDGGGRGLILKSVSQPRLVKEDYTMLTGKRKHCFNEGFEYVYLFTD
SLHRELRLNFRLYNDGIAFRYELPKLNQTVLSEELTTYRITEGTKRWMQKYNSGYEDFFP
MTTIGENSNHHWGYPALIQTADDVWTLISEAGIDRQNSASSLKNEQLVTDYKVCPAENTK
PITGNWTSPWRVMIIGSLADVVESTLVTDVSAPCILEDTDWIHPGNVSWIYWAYNHGSKD
FQIVKKYIDMAAKLKWPYVLIDWEWDVMENGGTIQDALKYAEQRGVRTLLWYNSSTAWIN
NGAAGPLFKLNSPENREKEFAWLEENKVAGVKIDFFAGDTEETMAYCLDLLESAAKHHLL
VNFHGATIPRGWQRTYPNLMSVEAVYGAEWYNNAPVLTNKAASHNTTLPFTRNVVGPMDY
TPCTFSDSQHPHITTHAHELALMVVFESALQHWADRPESYLIQPESVKNFMGQLPTVWDD
THLISGYPGEYVVMARQKGDAWYIAGLNGTDQEKMLDLDWKFLKNGKYQITLFQDSGNKE
QQWKVSSEVKDLSQLPNQMNSLARGGFVAVIKPTN

Enzyme Prediction     

EC	3.2.1.22

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH97	325	931	3.2e-174	0.9809825673534073
GH43	31	321	5.6e-109	0.9964028776978417

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18618	GH43_Xsa43E-like	4.84e-138	38	322	1	274	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.
cd08990	GH43_AXH_like	2.22e-104	40	322	1	268	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.
pfam10566	Glyco_hydro_97	1.36e-86	578	835	1	278	Glycoside hydrolase 97. This domain is the catalytic region of the bacterial glycosyl-hydrolase family 97. This central part of the GH97 family protein sequences represents a typical and complete (beta/alpha)8-barrel or catalytic TIM-barrel type domain. The N- and C-terminal parts of the sequences, mainly consisting of beta-strands, form two additional non-catalytic domains. In all known glycosidases with the (beta-alpha)8-barrel fold, the amino acid residues at the active site are located on the C-termini of the beta-strands.
cd09003	GH43_XynD-like	7.31e-82	31	324	1	315	Glycosyl hydrolase family 43 protein such as Bacillus subtilis arabinoxylan arabinofuranohydrolase (XynD;BsAXH-m23;BSU18160). This glycosyl hydrolase family 43 (GH43) subgroup includes characterized Bacillus subtilis arabinoxylan arabinofuranohydrolase (AXH), Caldicellulosiruptor sp. Tok7B.1 beta-1,4-xylanase (EC 3.2.1.8) / alpha-L-arabinosidase (EC 3.2.1.55) XynA, Caldicellulosiruptor sp. Rt69B.1 xylanase C (EC 3.2.1.8) XynC, and Caldicellulosiruptor saccharolyticus beta-xylosidase (EC 3.2.1.37)/ alpha-L-arabinofuranosidase (EC 3.2.1.55) XynF. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. It belongs to the GH43_AXH-like subgroup which includes enzymes that have been annotated as having beta-xylosidase, alpha-L-arabinofuranosidase and arabinoxylan alpha-L-1,3-arabinofuranohydrolase, xylanase (endo-alpha-L-arabinanase) as well as 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. Bacillus subtilis AXH (BsAXH-m2,3) has been shown to cleave arabinose units from O-2- or O-3-mono-substituted xylose residues and superposition of its structure with known structures of the GH43 exo-acting enzymes, beta-xylosidase and alpha-L-arabinanase, each in complex with their substrate, reveals a different orientation of the sugar backbone. 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.
cd09004	GH43_bXyl-like	1.42e-73	40	324	1	266	Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (BT3675;BT_3675) and (BT3662;BT_3662); includes mostly xylanases. This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have been annotated as xylan-digesting beta-xylosidase (EC 3.2.1.37) and xylanase (endo-alpha-L-arabinanase, EC 3.2.1.8) activities, as well the Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (EC 3.2.1.55) (BT3675;BT_3675) and (BT3662;BT_3662). 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. 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNL40595.1	7.62e-234	332	932	27	630
QVJ82067.1	3.47e-229	332	932	25	619
ADE81739.1	2.11e-228	332	932	24	618
ALJ60079.1	9.28e-227	332	932	28	630
QUT88912.1	1.05e-225	332	932	28	630

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3QEE_A	8.80e-90	31	334	4	296	Thestructure and function of an arabinan-specific alpha-1,2-arabinofuranosidase identified from screening the activities of bacterial GH43 glycoside hydrolases [Cellvibrio japonicus Ueda107],3QEE_B The structure and function of an arabinan-specific alpha-1,2-arabinofuranosidase identified from screening the activities of bacterial GH43 glycoside hydrolases [Cellvibrio japonicus Ueda107]
3QEF_A	1.26e-88	31	334	4	296	Thestructure and function of an arabinan-specific alpha-1,2-arabinofuranosidase identified from screening the activities of bacterial GH43 glycoside hydrolases [Cellvibrio japonicus Ueda107],3QEF_B The structure and function of an arabinan-specific alpha-1,2-arabinofuranosidase identified from screening the activities of bacterial GH43 glycoside hydrolases [Cellvibrio japonicus Ueda107]
3QED_A	3.23e-86	31	334	11	303	Thestructure and function of an arabinan-specific alpha-1,2-arabinofuranosidase identified from screening the activities of bacterial GH43 glycoside hydrolases [Cellvibrio japonicus Ueda107],3QED_B The structure and function of an arabinan-specific alpha-1,2-arabinofuranosidase identified from screening the activities of bacterial GH43 glycoside hydrolases [Cellvibrio japonicus Ueda107],3QED_C The structure and function of an arabinan-specific alpha-1,2-arabinofuranosidase identified from screening the activities of bacterial GH43 glycoside hydrolases [Cellvibrio japonicus Ueda107],3QED_D The structure and function of an arabinan-specific alpha-1,2-arabinofuranosidase identified from screening the activities of bacterial GH43 glycoside hydrolases [Cellvibrio japonicus Ueda107]
5XFM_A	2.31e-75	330	930	19	641	Crystalstructure of beta-arabinopyranosidase [Bacteroides thetaiotaomicron],5XFM_B Crystal structure of beta-arabinopyranosidase [Bacteroides thetaiotaomicron],5XFM_C Crystal structure of beta-arabinopyranosidase [Bacteroides thetaiotaomicron],5XFM_D Crystal structure of beta-arabinopyranosidase [Bacteroides thetaiotaomicron]
4NOV_A	8.33e-72	23	334	40	345	Xsa43E,a GH43 family enzyme from Butyrivibrio proteoclasticus [Butyrivibrio proteoclasticus B316]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
D7CFN7	2.75e-82	331	866	44	561	Probable retaining alpha-galactosidase OS=Streptomyces bingchenggensis (strain BCW-1) OX=749414 GN=SBI_01652 PE=3 SV=1
Q8A6L0	4.38e-47	329	898	24	626	Retaining alpha-galactosidase OS=Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50) OX=226186 GN=BT_1871 PE=1 SV=1
Q45071	6.86e-37	6	324	14	365	Arabinoxylan arabinofuranohydrolase OS=Bacillus subtilis (strain 168) OX=224308 GN=xynD PE=1 SV=2
P49943	4.85e-33	29	325	4	321	Xylosidase/arabinosidase OS=Bacteroides ovatus OX=28116 GN=xsa PE=2 SV=1
P45796	5.29e-33	29	325	37	363	Arabinoxylan arabinofuranohydrolase OS=Paenibacillus polymyxa OX=1406 GN=xynD 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
0.000343	0.998586	0.000508	0.000202	0.000175	0.000161

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002621_00486.