CAZyme Information: MGYG000003680_01723

Basic Information

• Species: Prevotella sp000433175
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp000433175
• CAZyme ID: MGYG000003680_01723
• CAZy Family: GH43
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1377		157222.51	7.5479

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003680	2339843	MAG	Italy	Europe

• Gene Location: Start: 9171; End: 13304 Strand: +

Full Sequence      

MKKLFLSAIIAAATMASSITSAKDVYVSTSFREPANEGLRFIYSYDGLRWDTIQGSFLRP
EVGTQKVMRDPSIVKGPDGTFHLVWTSSWRGDKGFGYASSKDLIHWSKERLINVMDDPTT
VNVWAPELFYDDVKKQYMIVWASCVPGKFPDYEEDHYNNHRLYYVTTKDFKKFSKAKVLI
DPDFSCIDATILKRGDKDYVMVLKDNSRKQRNLKISFAKSPYGPWSKPSEPFTESFTEGP
TTAKAEGWYYVYYDSYQHGIYGAARTKDFVNFQDRTGAVNFPVGHKHGTVFMASEEIVNN
LIKYNRDAVHYTGSVIATPARHDGGLSPVVGVHNIQTMRGSAGWLYNHQPMMAYWNNKFY
MHYLTDPRSEHEAPGRTMLQTSDDGYTWTEPVVLFPEYNVPDGFTKPAWPGVVAKDLKAI
MHQRIGFYVSKSNKLIAMGNYCVAITPKDDPNDGNAIGRVVREIKADGSFGPIYFIYYNH
GFNEKNTDYPYYKRSKDKAFVKACDELLADPMIRMQWVEEADRDDEILPLKTPYKAFSGY
TLPDGRKVGLWKHALTSISSDGGNTWRQPVKRAHGFVNSNAKIWGQRLSDGTYATVYNPA
EYRWPLAISLSNDGLEYTTLNLINGEVTPERHWGLYKSFGPQYTRGILEGNGKPKDGNLW
ITYSNNKEDMWVACVQVPVKLEATEQASGGFGKYKKLADMTDWNIYSPLWAPVKLDGEWL
TLSDKDPYDYARVEKVIPATKELTVEFDVKAMQNDHGQLNIEFLDAKGNMCSRIVLDSTA
TMKVKGGARYGGMMKHYDVGQAYHIKAVLSVDGHVGTYFVNGKKATARMFDTPVEAITRI
VFRTGNLFDKPDIETPADQTVDMPRADEQDPMATFAIANLTTKSSDTDANAAVLKYDNYK
HYADRFNTMEDENIETYIPNSKSSEWMSKNVPLFDCPDKDMEEIYYFRWWSLRKHIKRTP
VGLGMTEFLVQRSYADKYNLIACAVGHHIMETRWLRDTTYLHQILNTWYHGNNGKAMTKM
NKFSSWNPAAVFEAYKVLGDTAFVLGLKPSLEEEYARWKSTNRLANGLYWQGDVQDGMEE
SISGGRRKQYARPTINSYMYGNARALAELNRMAGDASKAKEYDLEADTLKSLIQSKLWNE
KHSFFETVRGDTAAAVREAIGYIPWYFNLPDAKKYDEAWKQLEDEKGFSAPYGLTTAERR
HPEFRSHGVGKCEWDGAIWPFATSQTLTAFANYINEYPEPVLGDSTFFKQMKLYVESQHH
RGRPYIGEYLDEKNGAWLMGDRERSRYYNHSTFADLVITGLVGLRPQADGSIVVNPLVPE
NTWTYFCLDNVNYRGNVLTIIYDKDGQRYHQGKGFRLLVNGKTVCEREDLGKLTYRK

Enzyme Prediction     

No EC number prediction in MGYG000003680_01723.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH143	304	842	2.2e-244	0.9892086330935251
GH142	906	1371	6.2e-211	0.9937369519832986
GH43	66	291	6e-82	0.9912663755458515

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08983	GH43_Bt3655-like	4.38e-74	56	304	7	261	Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 arabinofuranosidase Bt3655. This glycosyl hydrolase family 43 (GH43)-like family includes the characterized arabinofuranosidases (EC 3.2.1.55): Bacteroides thetaiotaomicron VPI-5482 (Bt3655;BT_3655) and Penicillium chrysogenum 31B Abf43B, as well as Bifidobacterium adolescentis ATCC 15703 beta-xylosidase (EC 3.2.1.37) BAD_1527. 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 includes enzymes with beta-xylosidase (EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanases (beta-xylanases) and galactan 1,3-beta-galactosidase (EC 3.2.1.145) 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.
cd08978	GH_F	6.00e-13	69	256	1	191	Glycosyl hydrolase families 43 and 62 form CAZY clan GH-F. This glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) includes family 43 (GH43) and 62 (GH62). GH43 includes enzymes with beta-xylosidase (EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanases (beta-xylanases) and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. GH62 includes enzymes characterized as arabinofuranosidases (alpha-L-arabinofuranosidases; EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose side chains from xylans. 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 of the enzymes in this family display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. GH62 are also predicted to be inverting enzymes. A common structural feature of both, GH43 and GH62 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.
cd08986	GH43-like	3.43e-09	68	227	2	218	Glycosyl hydrolase family 43 protein; uncharacterized. This glycosyl hydrolase family 43 (GH43)-like subfamily includes uncharacterized enzymes similar to those with beta-1,4-xylosidase (xylan 1,4-beta-xylosidase; EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanase and galactan 1,3-beta-galactosidase (EC 3.2.1.145) 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. Many of the enzymes in this family 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.
pfam13088	BNR_2	1.30e-07	540	614	168	247	BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases.
pfam04616	Glyco_hydro_43	1.11e-06	70	253	12	191	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
QUT77852.1	0.0	306	1373	21	1100
ALJ45260.1	0.0	304	1373	21	1099
QRQ56889.1	0.0	304	1373	21	1099
SCV09596.1	0.0	304	1373	21	1099
QRN01961.1	0.0	304	1373	21	1099

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5MQR_A	0.0	306	1373	25	1101	SialidaseBT_1020 [Bacteroides thetaiotaomicron]
5MQS_A	0.0	306	1373	25	1101	SialidaseBT_1020 [Bacteroides thetaiotaomicron]
6M5A_A	1.14e-24	924	1375	303	811	Crystalstructure of GH121 beta-L-arabinobiosidase HypBA2 from Bifidobacterium longum [Bifidobacterium longum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
E8MGH9	1.08e-23	924	1375	334	842	Beta-L-arabinobiosidase OS=Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b) OX=565042 GN=hypBA2 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
0.000367	0.998897	0.000199	0.000202	0.000171	0.000151

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003680_01723.