CAZyme Information: MGYG000003138_00906

Basic Information

• Species: Streptococcus pseudopneumoniae_O
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; Streptococcus; Streptococcus pseudopneumoniae_O
• CAZyme ID: MGYG000003138_00906
• CAZy Family: GH85
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1690	MGYG000003138_7|CGC1	186701.17	4.8932

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003138	1796209	MAG	United States	North America

• Gene Location: Start: 18109; End: 23181 Strand: +

Full Sequence      

MKNPFFERRCRYSIRKLSVGACSLMIGAVLFAGPALAEETAVPENSGAHTELVSGESEHP
TNEADKQHEGEHARENKPEKAEGVATASETASPASNEAATTETAEAVSAAKPEEKASEVA
AETPSAEAKPKSDKETEAKPEGTSQGDESKPAAEANKTEKEVQPDVPKNTEKTLKPKEIK
FNSWEDLLKWEPGAREDDPINRSSVELAKRHRGQLVNEKASRRAKVQALANTNSKAKDHA
SVGGEEFKAYAFDYWQYLDSMVFWEGLVPTPDVIDAGHRNGVPVYGTLFFNWSNSIADQE
KFVAALKQDEDGTFPIARKLVDLAKYYGFDGYFINQETTGDLVTPLGEKMRQFMLYTKEY
AAKVNHPIKYAWYDAMTYKYGRYHEDGLGDYNYQFMQKEGDKVPADQFFANFNWNKEKND
HSVEMAKWLERSQYDVFAGLELQQGGSYKTKVKWDALLDEKGKLRLSLGLFAPDTITSLG
KTGEDYHKNEDIFFTGYQGDPTAQKPADKEWYGIANLVADRTPAVGRTFTTSFNTGHGRK
WFVDGKVSKDSEWNYRSVSGILPTWRWWQTSTGEKLRAEYDFTDAYNGGNSLKFSGNIAG
KTDQDVNLYSTKLEVTEKTKLRVAHKGGKGSKVYMAFSTTPDYKFDDADAWKELTLSDNW
TNEEFDLSSLAGKTIYAVKLFFEHEGAVKDYQFNLGQLTISDNHQAPQAPTGLSVVKQSL
KNAQEAEAVVQFAGNQDADFYEVYEKDGDNWRLLTGSSASTIYLPKVSRSANATGTTQEL
KVVAVGKNGLRSEAATTSFNWGMTVQDTTLPRPLAENIVPGATVIGSTFPNTEGGEGIEG
MLNGTITSLSDKWSSGQLSGSVDIRLTQPRTVVRWVMDHAGAGGESVNDGLMNTKDFDLY
YKDTDGEWKLAKEVRGNKAHVTDITLDKPITAQDWRLHVITSDNGTPWKAIRIYNWKMYE
ALDTESQNIPMAKVAARSLGNHQVQLGFSDVPAGATITVYDKADSQTPIATLKTETGGDL
ATAPLGFDKQPTLLYYRTQLPGKEISNTLAVAIPQDERKIAAVSLEKGPKKTVYKEGEKL
DLRGGTLRVQYEGGQVDELINLTHSGVTVSGYDAHQKGEQNLTLQYLGLPVSGDLKVQVT
GQDEGKPKEVAGLYITKKPKTDYLVGDQLEHSEGRFGVLYDDETEETHSFTDEGVEITGY
DAQKTGRQTLTLHYKGHTAEFDVLVSPKAAVNDEYLKQEITAAQGRQSTLAYTFSSEDKQ
AVLVEKLNAAKAVAENHDASQEEVNKALNELKQAGADLDGNQRYQTAREELEGLLESVRE
KDPKAELIEQAETLLASEMPTPRAFADMKEKLNKKLAPAEESHHVGSMDPSEVAPTVEVL
PELVVETETTAYERQERPSANLLKGQRQLVQKGEEGQIRRLVEVDSQGNRTLRATEVLKE
ATPEIVEVGTKVFSSNQPAEGVKDLVLETPKLEIEEDTVAFKHQERPNPNLLVGQRQLVQ
AGVEGQIRRFVELDAQGNRIIRTTEVLKEAVPEITEVGTKVLSSNQPAEGVKDLVLEIPK
LEIEEDTVAFERQERPSASLLKGQHQLVQSGVKGQVRRFVEVDAQGNRTLRTTEVLKEAL
PEIVEVGTKEEQDSQKTGQALLATPTNEKVGKELPNTGVTRDASLVALGLLGVMSGYGLL
AGKKRENESI

Enzyme Prediction     

EC	3.2.1.96

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH85	233	542	4.9e-110	0.9904761904761905

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG4724	COG4724	0.0	185	704	37	553	Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism].
pfam03644	Glyco_hydro_85	5.55e-104	243	538	1	291	Glycosyl hydrolase family 85. Family of endo-beta-N-acetylglucosaminidases. These enzymes work on a broad spectrum of substrates.
cd06547	GH85_ENGase	1.56e-93	238	573	13	339	Endo-beta-N-acetylglucosaminidase (ENGase) hydrolyzes the N-N'-diacetylchitobiosyl core of N-glycosylproteins. The beta-1,4-glycosyl bond located between two N-acetylglucosamine residues is hydrolyzed such that N-acetylglucosamine 1 remains with the protein and N-acetylglucosamine 2 forms the reducing end of the released glycan. ENGase is a key enzyme in the processing of free oligosaccharides in the cytosol of eukaryotes. Oligosaccharides formed in the lumen of the endoplasmic reticulum are transported into the cytosol where they are catabolized by cytosolic ENGases and other enzymes, possibly to maximize the reutilization of the component sugars. ENGases have an eight-stranded alpha/beta barrel topology and are classified as a family 85 glycosyl hydrolase (GH85) domain. The GH85 ENGases are sequence-similar to the family 18 glycosyl hydrolases, also known as GH18 chitinases. An ENGase-like protein is also found in bacteria and is included in this alignment model.
pfam07523	Big_3	1.20e-10	1159	1225	3	67	Bacterial Ig-like domain (group 3). This family consists of bacterial domains with an Ig-like fold. Members of this family are found in a variety of bacterial surface proteins.
pfam07501	G5	1.22e-10	1382	1451	2	75	G5 domain. This domain is found in a wide range of extracellular proteins. It is found tandemly repeated in up to 8 copies. It is found in the N-terminus of peptidases belonging to the M26 family which cleave human IgA. The domain is also found in proteins involved in metabolism of bacterial cell walls suggesting this domain may have an adhesive function.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQQ35667.1	0.0	1	1690	1	1690
AYF96260.1	0.0	1	1629	1	1629
QKL32516.1	0.0	1	1690	1	1754
ANR74701.1	0.0	1	1687	1	1663
VEF79601.1	0.0	1	1687	1	1574

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2W91_A	0.0	172	820	5	653	Structureof a Streptococcus pneumoniae family 85 glycoside hydrolase, Endo-D. [Streptococcus pneumoniae TIGR4],2W92_A Structure of a Streptococcus pneumoniae family 85 glycoside hydrolase, Endo-D, in complex with NAG-thiazoline. [Streptococcus pneumoniae TIGR4]
3GDB_A	0.0	38	953	22	937	Crystalstructure of Spr0440 glycoside hydrolase domain, Endo-D from Streptococcus pneumoniae R6 [Streptococcus pneumoniae R6]
2XQX_A	2.12e-86	815	960	5	150	Structureof the family 32 carbohydrate-binding module from Streptococcus pneumoniae EndoD [Streptococcus pneumoniae TIGR4],2XQX_B Structure of the family 32 carbohydrate-binding module from Streptococcus pneumoniae EndoD [Streptococcus pneumoniae TIGR4]
2VTF_A	3.01e-86	185	764	19	588	X-raycrystal structure of the Endo-beta-N-acetylglucosaminidase from Arthrobacter protophormiae E173Q mutant reveals a TIM barrel catalytic domain and two ancillary domains [Glutamicibacter protophormiae],2VTF_B X-ray crystal structure of the Endo-beta-N-acetylglucosaminidase from Arthrobacter protophormiae E173Q mutant reveals a TIM barrel catalytic domain and two ancillary domains [Glutamicibacter protophormiae]
3FHA_A	1.66e-85	185	764	14	583	ChainA, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae],3FHA_B Chain B, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae],3FHA_C Chain C, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae],3FHA_D Chain D, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8BX80	6.24e-21	237	640	129	506	Cytosolic endo-beta-N-acetylglucosaminidase OS=Mus musculus OX=10090 GN=Engase PE=1 SV=1
P0C7A1	1.67e-19	173	598	77	463	Cytosolic endo-beta-N-acetylglucosaminidase OS=Gallus gallus OX=9031 GN=ENGASE PE=1 SV=1
Q8NFI3	7.99e-18	173	626	79	500	Cytosolic endo-beta-N-acetylglucosaminidase OS=Homo sapiens OX=9606 GN=ENGASE PE=1 SV=1
P49610	1.39e-16	1470	1687	1064	1312	Beta-N-acetylhexosaminidase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=strH PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000346	0.998645	0.000504	0.000185	0.000164	0.000142

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003138_00906.