CAZyme Information: MGYG000002832_00514

Basic Information

• Species: Prevotella sp900548195
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900548195
• CAZyme ID: MGYG000002832_00514
• CAZy Family: GH115
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
847	MGYG000002832_19|CGC1	96567.07	8.673

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002832	2701309	MAG	United Republic of Tanzania	Africa

• Gene Location: Start: 17510; End: 20053 Strand: +

Full Sequence      

MKKVITTLSLILIWITVVQAQSFCIAEKGNTASIIIDKNDWKGVIRAANDLGDDVRKVCG
KNAVVKHEKNANNGNIIVGTIGKSHIIDTLVKQEKLDVSKVKGQWESFIIDIVDGNLVVA
GSDKRGTIYGIYEISQRIGVSPWYWWADVPVKHQDNIYWNDGRFIQPSPKVKYRGIFIND
EWPSFGEWATTHFGGVNSKMYAKMFELILRLKANYLWPAMWASAFNEDDPLTPQVADDYG
IVMGTSHHEPMMRAHREYVNRKNAIGPWDYASNKKRIDQFFLEGMQRNKAFDNLVTIGMR
GDGDVAMGKGDDEDNMKTLKNVIKGQRQIIKKVYGKEDAVPQLWAIFTEVQRYYDAGFTV
PDDVTLLLCDNNWGYIRRIGRDFERKRKGGLGLYYHIDMNGGPWNDRWVNTTTIPKLREQ
LNLAYKTGIDRIWIINVGDLKPKEVPIDFIMHYAWNPDGVKAGDEQAWLENFTASAFGKE
YAKESADLIAKYSKYNLWRKAEAEVPGIFNKQEMEKTDSLWLSLTAHAEILRSKIPVQAQ
DAFYQLVYYPVVASAGVHMIYNAATRGNSNLIEQLMARDKQLSDFYHQMADGKWNKMMQD
KHIGYTNWYMPKENTNPMLLSRQVVREGYKEKAPIDDPQRGFLDFNVAYALKDQPTTKEY
SIPAYRFDRITKGKNATWMFLPDLGRGKGCMGSNNVLAQNSGATLEYDIDLTSDGTVAIG
ILPTQDVNPSRGLRIGIQIDDQPMQTIDARRGLVDTFSEYNPQNISRSKVLKALPPSSKL
ALSGFWQGRQLPRRSEVFDNIRWLDASFPSISTGRHTLKIIMIDPEIVVEQIVVNPDNNH
YSYFGNQ

Enzyme Prediction     

EC	3.2.1.131

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH115	21	832	7.8e-236	0.9971305595408895

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam15979	Glyco_hydro_115	0.0	168	502	2	333	Glycosyl hydrolase family 115. Glyco_hydro_115 is a family of glycoside hydrolases likely to have the activity of xylan a-1,2-glucuronidase, EC:3.2.1.131, or a-(4-O-methyl)-glucuronidase EC:3.2.1.-.
pfam17829	GH115_C	1.71e-28	661	845	10	169	Gylcosyl hydrolase family 115 C-terminal domain. This domain is found at the C-terminus of glycosyl hydrolase family 115 proteins. This domain has a beta-sandwich fold.
pfam03648	Glyco_hydro_67N	1.55e-06	47	133	36	119	Glycosyl hydrolase family 67 N-terminus. Alpha-glucuronidases, components of an ensemble of enzymes central to the recycling of photosynthetic biomass, remove the alpha-1,2 linked 4-O-methyl glucuronic acid from xylans. This family represents the N-terminal region of alpha-glucuronidase. The N-terminal domain forms a two-layer sandwich, each layer being formed by a beta sheet of five strands. A further two helices form part of the interface with the central, catalytic, module (pfam07488).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
EEC55419.1	0.0	32	845	53	987
QRQ50360.1	0.0	32	845	28	962
QUT25621.1	0.0	19	845	40	1003
QRQ59056.1	0.0	19	845	11	974
SCV06546.1	0.0	19	845	40	1003

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4ZMH_A	2.30e-178	25	660	16	668	Crystalstructure of a five-domain GH115 alpha-Glucuronidase from the Marine Bacterium Saccharophagus degradans 2-40T [Saccharophagus degradans 2-40],4ZMH_B Crystal structure of a five-domain GH115 alpha-Glucuronidase from the Marine Bacterium Saccharophagus degradans 2-40T [Saccharophagus degradans 2-40]
4C90_A	1.50e-165	23	843	44	843	Evidencethat GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus],4C90_B Evidence that GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus],4C91_A Evidence that GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus],4C91_B Evidence that GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus]
7PUG_A	5.22e-162	21	714	15	723	ChainA, xylan alpha-1,2-glucuronidase [uncultured bacterium]
7PXQ_A	2.40e-159	21	714	14	722	ChainA, xylan alpha-1,2-glucuronidase [uncultured bacterium]
6NPS_A	2.95e-124	21	619	9	655	Crystalstructure of GH115 enzyme AxyAgu115A from Amphibacillus xylanus [Amphibacillus xylanus NBRC 15112],6NPS_B Crystal structure of GH115 enzyme AxyAgu115A from Amphibacillus xylanus [Amphibacillus xylanus NBRC 15112]

Swiss-Prot Hits     

has no Swissprot hit.

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
0.000213	0.999182	0.000172	0.000139	0.000133	0.000132

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002832_00514.