CAZyme Information: MGYG000001372_01158

Basic Information

• Species: Paraprevotella xylaniphila
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Paraprevotella; Paraprevotella xylaniphila
• CAZyme ID: MGYG000001372_01158
• CAZy Family: GH30
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
966		107583.28	4.7861

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001372	3789432	Isolate	not provided	not provided

• Gene Location: Start: 107362; End: 110262 Strand: -

Full Sequence      

MKRTITLLYATALTGCIPLCAQRTANVNLDSETRYQKIDGFGGCGMNGQWADVYTQEQVD
RLWGPDGMGYNIMRIRINPDESNWKSYVNAVKWAKAHGAIVFASPWTPPFCFKVGAEQTW
GESSNHGHINTDSIDSYARWLERYRQFMEDQGAAIDILSVQNESDYDPEGYEGCLYTVDE
MTRMVTALHQHLSPECKVMAPECFGWDSHKYNQELVKSAAMRNSIDIWGNHIYGVNDMTY
VDYVRSLTKRPMWMTEYIFDEDKVGTWESACDFQEQIDSCMRAGFSAYVYYNMINHMFGD
GKGGGNASELSTFAYVLGHYARYATGMTRIKSSFSDKGKTPVNGSAYVSENGDTLSLFVL
NRSSEPVKLKANLPFESRQVYAVLTNATRNRFVQDVSTQYAGTASPEIDLLGNAFYTLQF
IRTEAETPEPSEPTVMEAYKKTTEVNPLNPYRFCADPTSVEYEGRLYVYGTNDQQEFDAT
GGLTSNTYGKIRSLVMMSTEDLVNWTYHGTIDMTTVCGQWLNASWAPSIVSREEADGKTH
FYLYFSNSGGGVGVITSTSPLGPWTDPLGKNLISGSTPGLGLCSTPFDPGVVIDNDGTGW
LAFGGGNPNAEGTELMPGNARIVRLGKDMISLDSDIMPIPAPYHFEANELNVMGGKLVYS
YCTSWRERTNWPSYGGISEAPSACSICYMTTDTPLAPDSWTYKGEYFANPGTFGYPYGNN
HSHLQKFSNAYYLLYHTQGLEQQMAINGGYRSIAMNRLPVVERSQRINAVTASPTGVMQL
TAKRVDPFILQQAENLCTAAGVSAESYEKTGNTRITIPQSGGWTMVKGVMFGTEGIKKFT
ANLQGEGTLEIRLNDIEAEPVVTLDFSTPEATEVSVDCPTPITGSHDVYFLFTETRGEVK
FDTWQFAGKGSDAITNTEMEDRTPVRYEYYHPNGMRLTEQPATGMYIRKTYYSDGSVKTD
KKLSEH

Enzyme Prediction     

EC	3.2.1.55

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH43	446	760	1.1e-112	0.9742765273311897
GH30	26	374	1.3e-80	0.9824561403508771
CBM6	791	906	7.1e-16	0.8623188405797102

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd09003	GH43_XynD-like	7.76e-162	446	762	1	308	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.
cd08990	GH43_AXH_like	2.50e-48	455	758	1	259	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.
COG5520	XynC	1.04e-42	1	391	5	401	O-Glycosyl hydrolase [Cell wall/membrane/envelope biogenesis].
cd18618	GH43_Xsa43E-like	1.92e-37	453	758	1	265	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.
cd09004	GH43_bXyl-like	2.71e-31	455	758	1	255	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
QMI81061.1	1.08e-149	446	906	47	500
QPH56605.1	1.08e-149	446	906	47	500
QCD39316.1	2.80e-137	442	906	39	497
QCP73007.1	2.80e-137	442	906	39	497
QUT33503.1	5.13e-137	442	906	492	944

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3C7E_A	6.56e-82	446	906	14	484	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]
3C7G_A	6.75e-82	446	906	15	485	Crystalstructure of a glycoside hydrolase family 43 arabinoxylan arabinofuranohydrolase from Bacillus subtilis in complex with xylotetraose. [Bacillus subtilis]
5A8C_A	1.94e-47	447	786	30	322	ChainA, CARBOHYDRATE BINDING FAMILY 6 [Acetivibrio thermocellus],5A8D_A Chain A, CARBOHYDRATE BINDING FAMILY 6 [Acetivibrio thermocellus]
1NOF_A	4.15e-33	27	414	3	368	ChainA, xylanase [Dickeya chrysanthemi],2Y24_A Chain A, XYLANASE [Dickeya chrysanthemi]
4FMV_A	2.37e-32	27	390	7	358	CrystalStructure Analysis of a GH30 Endoxylanase from Clostridium papyrosolvens C71 [Ruminiclostridium papyrosolvens DSM 2782]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P45796	3.36e-84	446	921	39	523	Arabinoxylan arabinofuranohydrolase OS=Paenibacillus polymyxa OX=1406 GN=xynD PE=1 SV=1
Q45071	7.26e-81	446	906	40	510	Arabinoxylan arabinofuranohydrolase OS=Bacillus subtilis (strain 168) OX=224308 GN=xynD PE=1 SV=2
Q45070	3.22e-29	15	367	26	368	Glucuronoxylanase XynC OS=Bacillus subtilis (strain 168) OX=224308 GN=xynC PE=1 SV=1
Q6YK37	2.80e-27	15	351	27	355	Glucuronoxylanase XynC OS=Bacillus subtilis OX=1423 GN=xynC PE=3 SV=2
P49943	1.06e-09	443	736	3	290	Xylosidase/arabinosidase OS=Bacteroides ovatus OX=28116 GN=xsa PE=2 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
0.000075	0.061446	0.938418	0.000024	0.000035	0.000024

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001372_01158.