CAZyme Information: MGYG000002603_01328

Basic Information

• Species: Prevotella sp900767615
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900767615
• CAZyme ID: MGYG000002603_01328
• CAZy Family: GH5
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
592		64132.4	4.7177

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002603	2739364	MAG	China	Asia

• Gene Location: Start: 45911; End: 47689 Strand: -

Full Sequence      

MAFAMVSFSACSKEDTIGGGEGLSKDFVVSRSDMEFTKNGGETDLYVKAAQVPTVSTEAT
WLAVTPVAGSSSITHHFLIKAEANTANDDRSATITVAAGSDTKTITVSQNSTEGLLITSG
KTMNVGAAGGQVTVTLKANASYSQVISNEWVSEITSRANMVEYTRNYSVAANISNARSAT
ISYTMVVNDSTSITEAVTINQEQGTTTGDMSKTAMDIAALMYPGWNLGNTMEAGNAANNW
KNTGIGSETSWQSAKTTQQFIDLVKASGFKSVRIPCSWVMGHITDAEACTIDADWLARVH
EVVDYCIKNDLYVIINQHWDGGWIEHDGLTAATDVGATKAKLTKIWTQIANSFKDYDERL
IFAGMNEPGVGGGDANALLGTADLANRIAEYEQTFIEAVRATGGNNAKRVLVVQGPNTNI
DNTVVHNYMDKIHDSATDRLMVEVHFYDPYQFTDLSEDKDWGKYYLYWGKNNKGGDADRT
ADAKYNEDYVEAQMEKMKTHFFDKGYPVLIGEFGANQRLAIGKDALHDASVKDYYKAVVT
SAINNGCVPVAWDTNGGLPSMTIFNRANTTVSNANILESIQEAVKTASWPAK

Enzyme Prediction     

No EC number prediction in MGYG000002603_01328.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	247	555	1e-94	0.9927536231884058

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00150	Cellulase	3.21e-50	242	556	10	270	Cellulase (glycosyl hydrolase family 5).
COG2730	BglC	5.02e-25	221	516	51	324	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
cd14948	BACON	5.88e-15	27	109	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	8.32e-09	54	109	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	1.49e-05	116	202	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	9.47e-161	1	587	42	605
QUT65987.1	5.14e-121	34	590	49	592
QUU01445.1	5.14e-121	34	590	49	592
BBK86684.1	5.14e-121	34	590	49	592
QUT37093.1	1.02e-120	34	590	49	592

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4W8A_A	7.58e-101	212	590	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	4.53e-80	210	582	41	391	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	3.48e-79	210	582	41	391	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	6.34e-62	214	585	35	395	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	5.50e-58	212	573	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	6.02e-58	211	585	37	400	Endoglucanase A OS=Paenibacillus barcinonensis OX=198119 GN=celA PE=1 SV=1
A7LXT7	1.67e-52	207	584	143	501	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	1.18e-51	207	570	35	360	Endoglucanase B OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=engB PE=3 SV=1
P28623	2.70e-49	207	584	36	372	Endoglucanase D OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=engD PE=1 SV=2
P23660	1.92e-48	214	585	27	364	Endoglucanase A OS=Ruminococcus albus OX=1264 GN=celA PE=1 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
0.014389	0.029714	0.955772	0.000041	0.000051	0.000047

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002603_01328.