CAZyme Information: MGYG000001927_00804

Basic Information

• Species: Prevotella sp900547005
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900547005
• CAZyme ID: MGYG000001927_00804
• CAZy Family: GH5
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
592	MGYG000001927_8|CGC1	65058.41	4.557

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001927	2803818	MAG	Denmark	Europe

• Gene Location: Start: 43191; End: 44969 Strand: -

Full Sequence      

MKKIFRIFSLMVVALFATTLVACSDDDEQVTHDWGNAEFLVSKDNLTFSATGGTAEVYVQ
STSVPTVTSGAGWLTIEPRTSDSHKMYVYNITVPQYTETDDRSDVITVSVNGESKTIAIT
QVAHDGLILEKTSFSVGKEETAITVNLKANGAFTVTPGVEWIKETGTRANMADYSRSFTV
AANVGTARTGTISFTLNDITESVTVNQEGSEMGEITAKATELAKLMYPGWNLGNTLEASG
SGVGAETAWQGTKTTQAIIDYVKAQGFKSVRIPCSWYIHSDNGDIDAAWMARVKEVVNYC
IADGLYVVLNDHWDSGWIEVEGFSKSSDRYEPVDEATIAAKSDMLRKLWTQIANEFKDYD
EHLLFAGLNEPFQQYNLFNNRHAELTPILNRYNQVFVDAVRATGGNNAKRTLVVQGPATS
TSSAVDPGIGFTMPTDTETGYLMAEVHYYEPWDFCGQEDNAVWFWGNANHVSGSSHNATW
GEEAHLSSQFGSLKTTFVDKGYPVIIGEYGTQWRSLTANQSEHDASVKHFFYEVNRLAVN
NGIVPFAWDINSLNQRGESGTMTIINRADLSIFCAPAMEGIKEGTAAGKWLQ

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	246	550	3.5e-97	0.9855072463768116

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00150	Cellulase	2.83e-52	237	552	7	270	Cellulase (glycosyl hydrolase family 5).
COG2730	BglC	8.89e-23	220	565	45	372	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
cd14948	BACON	3.78e-14	38	121	1	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.
cd14948	BACON	2.23e-10	127	208	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.
pfam13004	BACON	1.72e-06	63	121	1	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
VEH16026.1	2.46e-177	3	589	29	606
ADB44000.1	9.12e-168	207	590	127	514
SCD22090.1	6.10e-131	2	590	5	564
SCM57160.1	1.22e-130	9	590	12	564
QMI80089.1	6.28e-127	1	590	1	573

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4W8A_A	3.43e-169	219	590	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	1.19e-75	219	587	45	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	9.10e-75	219	587	45	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	2.88e-65	217	584	33	393	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	1.09e-56	221	549	26	346	ChainA, Cellulase [Phocaeicola salanitronis DSM 18170]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O08342	1.45e-61	210	584	33	398	Endoglucanase A OS=Paenibacillus barcinonensis OX=198119 GN=celA PE=1 SV=1
P54937	1.17e-52	219	584	39	377	Endoglucanase A OS=Clostridium longisporum OX=1523 GN=celA PE=1 SV=1
P28621	8.49e-52	221	587	44	376	Endoglucanase B OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=engB PE=3 SV=1
A7LXT7	2.03e-48	144	549	62	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
P16216	3.73e-48	200	582	50	395	Endoglucanase 1 OS=Ruminococcus albus OX=1264 GN=Eg I 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	0.000268	0.999785	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001927_00804.