CAZyme Information: MGYG000001657_01288

Basic Information

• Species: RC9 sp900760425
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; UBA932; RC9; RC9 sp900760425
• CAZyme ID: MGYG000001657_01288
• CAZy Family: GH18
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
646	MGYG000001657_69|CGC1	70659.6	4.5736

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001657	2980281	MAG	United States	North America

• Gene Location: Start: 7271; End: 9211 Strand: +

Full Sequence      

MIRKSFKFWICSIISVLAVACTETPEDIVNTLTVTPDHALEFQAKDNEAVRLNVETDAAK
WECSTSEKWITVSAGEKSLSVNVEDNPETKVRAGRLTITAGNAEPVSISVSQDAAEEVVP
FLNVTPSEPISFSAEAGEITALTVETNMEEWNYKVPDWLTAEKQEGQLLLTTQANEGTAS
RVGRVDISAEGAKPVRINVSQDAPDLESVKASLSDAQGGQSGELVIANLNTLELPLTVNL
DKSTGNDAQFDIVYDKDYVAAYNLINKTDYQAYPEHLVTIPSEGRVTVAAGEKSASLTVK
INPDDINSLRNDVTYLIPVIVKPIAGTGVTAPMAKARVNYTISRKCKKEVKNVVYIDTKD
TNPLNFLELRLEDGSMMVDAVVLFAANINWDGRNQEVMLNNNGCTQGLLDQTETYIQPLR
KAGIKVLLGLLGNHDGAGIANLSEYGAIEYSKTLANAVKKYKLDGISFDDEYSSYGELSG
EWFEYASGANASRLLYYTKKSMKEIVPWDTYTMVYYYGNISSALPRFNGTAPGEYVDIAV
ADYPVGAATPMTGMTKKQCAGGSVEMNEGRGTSPSSAESIKTKGYGWMMWFSYNPVRKPD
NVKALQTAAKGLYDGMKLMDPQHVYKKATMGTHNNDFDPNPYPFAW

Enzyme Prediction     

EC	3.2.1.96

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06542	GH18_EndoS-like	4.61e-37	378	613	28	255	Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of various asparagine (N)-linked glycans and glycoproteins. The endo-beta-N-acetylglucosaminidases have a glycosyl hydrolase family 18 (GH18) catalytic domain. Some members also have an additional C-terminal glycosyl hydrolase family 20 (GH20) domain while others have an N-terminal domain of unknown function (pfam08522). Members of this family include endo-beta-N-acetylglucosaminidase S (EndoS) from Streptococcus pyogenes, EndoF1, EndoF2, EndoF3, and EndoH from Flavobacterium meningosepticum, and EndoE from Enterococcus faecalis. EndoS is a secreted endoglycosidase from Streptococcus pyogenes that specifically hydrolyzes the glycan on human IgG between two core N-acetylglucosamine residues. EndoE is a secreted endoglycosidase, encoded by the ndoE gene in Enterococcus faecalis, that hydrolyzes the glycan on human RNase B.
pfam08522	DUF1735	3.04e-13	230	326	25	118	Domain of unknown function (DUF1735). This domain of unknown function is found in a number of bacterial proteins including acylhydrolases. The structure of this domain has a beta-sandwich fold.
cd14948	BACON	4.14e-10	31	113	1	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.
cd14948	BACON	7.37e-10	121	202	1	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	1.13e-06	61	112	3	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
BBL11372.1	8.30e-151	19	643	15	648
BBL08580.1	8.30e-151	19	643	15	648
CBK65046.1	2.17e-146	30	643	22	642
QRQ55675.1	8.77e-81	213	627	50	465
QDH54393.1	8.77e-81	213	627	50	465

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6T8I_A	2.31e-69	211	644	23	447	Crystalstructure of wild type EndoBT-3987 from Bacteroides thetaiotamicron VPI-5482 [Bacteroides thetaiotaomicron VPI-5482],6T8K_A Crystal structure of Bacteroides thetaiotamicron EndoBT-3987 in complex with Man9GlcNAc product in P1 [Bacteroides thetaiotaomicron VPI-5482],6T8K_B Crystal structure of Bacteroides thetaiotamicron EndoBT-3987 in complex with Man9GlcNAc product in P1 [Bacteroides thetaiotaomicron VPI-5482],6T8L_A Crystal structure of Bacteroides thetaiotamicron EndoBT-3987 with Man9GlcNAc product in P212121 [Bacteroides thetaiotaomicron VPI-5482],6TCW_A Crystal structure of Bacteroides thetaiotamicron EndoBT-3987 with Man5GlcNAc product [Bacteroides thetaiotaomicron VPI-5482],7NWF_A Chain A, Endo-beta-N-acetylglucosaminidase F1 [Bacteroides thetaiotaomicron VPI-5482]
6TCV_B	4.79e-67	211	644	23	447	Crystalstructure of Bacteroides thetaiotamicron EndoBT-3987 in complex with Man9GlcNAc2Asn substrate [Bacteroides thetaiotaomicron VPI-5482]
3POH_A	5.03e-65	211	644	23	447	Crystalstructure of an endo-beta-N-acetylglucosaminidase (BT_3987) from BACTEROIDES THETAIOTAOMICRON VPI-5482 at 1.55 A resolution [Bacteroides thetaiotaomicron VPI-5482]
2EBN_A	3.93e-48	347	627	7	287	CRYSTALSTRUCTURE OF ENDO-BETA-N-ACETYLGLUCOSAMINIDASE F1, AN ALPHA(SLASH)BETA-BARREL ENZYME ADAPTED FOR A COMPLEX SUBSTRATE [Elizabethkingia meningoseptica]
1EDT_A	5.22e-27	347	594	6	245	ChainA, ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H, ENDO H [Streptomyces plicatus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P36911	2.19e-47	331	627	43	337	Endo-beta-N-acetylglucosaminidase F1 OS=Elizabethkingia meningoseptica OX=238 GN=endOF1 PE=1 SV=1
P04067	6.74e-26	347	594	48	287	Endo-beta-N-acetylglucosaminidase H OS=Streptomyces plicatus OX=1922 PE=1 SV=1
P80036	1.71e-25	352	592	57	289	Endo-beta-N-acetylglucosaminidase OS=Flavobacterium sp. (strain SK1022) OX=148444 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	0.000004	1.000047	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001657_01288.