CAZyme Information: MGYG000004622_01652

Basic Information

• Species: Prevotella sp900316565
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900316565
• CAZyme ID: MGYG000004622_01652
• CAZy Family: GH5
• CAZyme Description: Xyloglucan-specific endo-beta-1,4-glucanase BoGH5A

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
488		53096.5	5.1159

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004622	2570641	MAG	France	Europe

• Gene Location: Start: 11621; End: 13087 Strand: +

Full Sequence      

MNKIKNILILVVAFIATSVFAACNDDDDNVITSHVVFTPETVEFSADGGTQTVTANGNAP
VKTITSDASWLKAEAGSFLPTKLTQPIILTADKNTTSSARTATVTITAGTLTLTIPVSQA
SGNGSTEDRPGSIRGAAMDLAPNMYPGWNLGNTLEAVGGETGWQHTVTTKAVIDYVKAQG
FKSVRIPTAWRIHADATGKIDQAWMTRVKEVVNYCIDDGLYVVLNDHWDNGWIEVDGFSK
SHDSYQPLAEADIAAKADTLKNLWTQIATAFKAYGDHLLFAGLNEPFQEYNLFSTHHAEL
TPILQRYNQAFVDAVRATGGNNAKRTLVVQGPSVNIAATTDAGINFTMPTDQTGGSGRLM
IEVHYYEPWNFCGGNSTKTWGSADEVNYMKDQFSRMKSKFADNGYPVILGEYGVNWQENS
QENNNSIQLFCKSINEYGPANGIIPFVWDTNSPTLPTMTIIDRANLKVFNPYALNGIKAG
VSATTWTK

Enzyme Prediction     

EC	3.2.1.73	3.2.1.78	3.2.1.4	3.2.1.8	3.2.1.151

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	160	451	1.2e-93	0.9891304347826086

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00150	Cellulase	4.17e-48	154	452	10	270	Cellulase (glycosyl hydrolase family 5).
COG2730	BglC	1.56e-18	143	430	50	339	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
cd14948	BACON	3.95e-16	37	120	4	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.
pfam19190	BACON_2	5.06e-10	38	120	5	89	Viral BACON domain. This family represents a distinct class of BACON domains found in crAss-like phages, the most common viral family in the human gut, in which they are found in tail fiber genes. This suggests they may play a role in phage-host interactions.
pfam13004	BACON	4.99e-07	63	120	4	61	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ADB44000.1	3.15e-146	2	486	5	514
VEH16026.1	8.36e-127	35	483	154	604
QSW87076.1	1.71e-87	2	481	3	498
AWK03401.1	4.40e-87	2	481	3	495
QDW19275.1	1.49e-86	2	481	3	502

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4W8A_A	5.29e-137	137	486	3	376	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	9.32e-67	133	483	41	395	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	7.13e-66	133	483	41	395	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	1.07e-58	137	481	35	394	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]
3NDY_A	6.00e-58	137	485	12	345	Thestructure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDY_B The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDY_C The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDY_D The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDZ_A The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans],3NDZ_B The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans],3NDZ_C The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans],3NDZ_D The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P28623	4.76e-57	137	487	43	378	Endoglucanase D OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=engD PE=1 SV=2
O08342	5.25e-56	137	481	40	399	Endoglucanase A OS=Paenibacillus barcinonensis OX=198119 GN=celA PE=1 SV=1
P54937	3.70e-55	127	452	30	345	Endoglucanase A OS=Clostridium longisporum OX=1523 GN=celA PE=1 SV=1
P28621	2.76e-54	137	484	42	377	Endoglucanase B OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=engB PE=3 SV=1
P17901	1.20e-51	138	477	48	396	Endoglucanase A OS=Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10) OX=394503 GN=celCCA 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
0.000000	0.000001	1.000063	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004622_01652.