CAZyme Information: MGYG000002293_00314

Basic Information

• Species: Prevotella sp900557255
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900557255
• CAZyme ID: MGYG000002293_00314
• CAZy Family: GH5
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
604		65415.13	4.8496

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002293	3611909	Isolate	China	Asia

• Gene Location: Start: 120380; End: 122194 Strand: -

Full Sequence      

MKKITILSFLIMAFAMVSFSACSNEDTIEGGEGLSTDFVVSRSDMAFTKNGGETDLYVKA
AQVPTVSTEAAWLAVTPVAGSSSITHHFLIKAEANTANDDRSATITVAAGSDTKTITVSQ
NSTEGLLITSSKNVNVGAAGGQVTVTLKANASYSQVISNDWVSEITSRANMVEYTRNYSV
AANISNARSATISYTMVVNDSTSITEAVTINQEQGTTTGDMSKTAMDIAALMYPGWNLGN
TMEAGNSANNWKNAGIGSETLWQSAKTTQQLIDLVKASGFKSVRIPCSWVMGHITDAEAC
TIDADWLARVHEVVDYCIKNDLYVIINQHWDGGWIEHDGLTAATDVDATKAKLTKIWTQI
ANSFKNYDERLIFAGMNEPGVGAGDANALLGTADLANRIAEYEQTFIEAVRATGGNNAKR
VLVVQGPNTNIDNTVAHNYMAKLHDSATDRLMIEVHFYDPYQFTDMSEDKDWGKYYLYWG
KNNTNGSEADRTADAKYNEDYVEAQMKKMKTNFFDKGYPVLIGEFGANQRLAIGKDAVHD
ASVKDYYKAVVTSAINNGCVPMAWDTNGNYPSMTIFNRAGASVSNANMLESIKAAVAAAK
WPAK

Enzyme Prediction     

No EC number prediction in MGYG000002293_00314.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	258	567	1.1e-94	0.9891304347826086

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00150	Cellulase	3.67e-50	253	569	10	271	Cellulase (glycosyl hydrolase family 5).
COG2730	BglC	1.13e-23	232	528	51	324	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
cd14948	BACON	1.07e-14	38	120	2	82	Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes.
pfam13004	BACON	9.65e-09	65	120	4	60	Putative binding domain, N-terminal. The BACON (Bacteroidetes-Associated Carbohydrate-binding Often N-terminal) domain is an all-beta domain found in diverse architectures, principally in combination with carbohydrate-active enzymes and proteases. These architectures suggest a carbohydrate-binding function which is also supported by the nature of BACON's few conserved amino-acids. The phyletic distribution of BACON and other data tentatively suggest that it may frequently function to bind mucin. Further work with the characterized structure of a member of glycoside hydrolase family 5 enzyme, Structure 3ZMR, has found no evidence for carbohydrate-binding for this domain.
cd14948	BACON	1.76e-06	127	213	2	83	Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
VEH16026.1	2.51e-161	1	600	31	606
QUT37093.1	6.05e-123	20	602	25	592
QUT65987.1	1.20e-122	20	602	25	592
QUU01445.1	1.20e-122	20	602	25	592
BBK86684.1	1.20e-122	20	602	25	592

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4W8A_A	9.20e-99	223	602	1	377	Crystalstructure of XEG5B, a GH5 xyloglucan-specific beta-1,4-glucanase from ruminal metagenomic library, in the native form [uncultured bacterium],4W8B_A Crystal structure of XEG5B, a GH5 xyloglucan-specific beta-1,4-glucanase from ruminal metagenomic library, in complex with XXLG [uncultured bacterium]
5OYC_A	1.38e-77	221	592	41	389	GH5endo-xyloglucanase from Cellvibrio japonicus [Cellvibrio japonicus Ueda107],5OYC_B GH5 endo-xyloglucanase from Cellvibrio japonicus [Cellvibrio japonicus Ueda107],5OYD_A GH5 endo-xyloglucanase from Cellvibrio japonicus [Cellvibrio japonicus Ueda107],5OYD_B GH5 endo-xyloglucanase from Cellvibrio japonicus [Cellvibrio japonicus Ueda107],5OYE_A GH5 endo-xyloglucanase from Cellvibrio japonicus [Cellvibrio japonicus Ueda107],5OYE_B GH5 endo-xyloglucanase from Cellvibrio japonicus [Cellvibrio japonicus Ueda107]
6HA9_A	1.06e-76	221	592	41	389	Structureof an endo-Xyloglucanase from Cellvibrio japonicus complexed with XXXG(2F)-beta-DNP [Cellvibrio japonicus Ueda107],6HA9_B Structure of an endo-Xyloglucanase from Cellvibrio japonicus complexed with XXXG(2F)-beta-DNP [Cellvibrio japonicus Ueda107],6HAA_A Structure of a covalent complex of endo-Xyloglucanase from Cellvibrio japonicus after reacting with XXXG(2F)-beta-DNP [Cellvibrio japonicus Ueda107],6HAA_B Structure of a covalent complex of endo-Xyloglucanase from Cellvibrio japonicus after reacting with XXXG(2F)-beta-DNP [Cellvibrio japonicus Ueda107]
2JEP_A	1.13e-61	225	592	35	390	Nativefamily 5 xyloglucanase from Paenibacillus pabuli [Paenibacillus pabuli],2JEP_B Native family 5 xyloglucanase from Paenibacillus pabuli [Paenibacillus pabuli],2JEQ_A Family 5 xyloglucanase from Paenibacillus pabuli in complex with ligand [Paenibacillus pabuli]
6WQY_A	2.67e-55	223	585	22	369	ChainA, Cellulase [Phocaeicola salanitronis DSM 18170]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O08342	1.50e-56	222	592	37	395	Endoglucanase A OS=Paenibacillus barcinonensis OX=198119 GN=celA PE=1 SV=1
A7LXT7	2.78e-51	132	565	50	473	Xyloglucan-specific endo-beta-1,4-glucanase BoGH5A OS=Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153) OX=411476 GN=BACOVA_02653 PE=1 SV=1
P28621	3.58e-48	218	578	35	356	Endoglucanase B OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=engB PE=3 SV=1
P23660	4.37e-47	225	572	27	335	Endoglucanase A OS=Ruminococcus albus OX=1264 GN=celA PE=1 SV=1
P28623	2.79e-46	218	578	36	354	Endoglucanase D OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=engD PE=1 SV=2

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
0.000000	0.000002	1.000057	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002293_00314.