CAZyme Information: MGYG000003326_00157

Basic Information

• Species: Blautia sp900541955
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia; Blautia sp900541955
• CAZyme ID: MGYG000003326_00157
• CAZy Family: GH85
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2144	MGYG000003326_2|CGC5	236858.52	4.4654

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003326	2715873	MAG	United States	North America

• Gene Location: Start: 72945; End: 79379 Strand: +

Full Sequence      

MKKKSLKKTVAVMLSGVCLASGVAVPADTVQASAGLGYWPENLPIPNQYYYQKESLQPYG
TCLQIGELKNWSPDNDPDARYNRSSIPLRQRYMGPSVNPLASRDAKVMPLAMSNARASEA
ESQGGEGDFVYAFNNFQYIDTYNFWGGSSAEGPICIPSPEHIDSAHRNGVQATGTIFIPW
GDEEYGGRFVRELVAQDEQGNYPCADKLIEVAQYYGFDGYIFNAESGTGVSGFKEFLAYM
QEKAPENFRISWYNGSGTLGADSIDAWMQDEDKRITDEWWLDMSGNGNVDSTIDATYEAD
RDKWDIHSTWEYIPMQDGAKGGDYHTRLDKDGKLKISLGILAPTSTLTQSKNSDDFMNVQ
DQKLWVGPDFDPSSTNRPDDEFCGFANLVADQTPVLGTDFVTHFNPGNGYKFYENGAVIG
MESGWHNRSLTEVLPTWRWIVDAEDGAKKVEPKIDYEDAYWGGASMKISGGLSAGKANHI
KLYSTQLDITDSSTFELVYKTKKNSDVKLSVGLCFGDTYEDKNFQFYPVEIQGDGSWKEA
SIPLADESGQRVSAISLKLESAGGVDDYSMNIGKMGIVTDKSQPEAPGEITLDDVIYPTD
LSAEARIYWDKGEHSFIDIIHRVRPDGQEEFVGATPSDAFYIPKFRKLEGEKEATFKITS
ISENGIEGDSREIKIAWPKEVPDGFGPSAELGENLALRAPAVCDVPCAADGPVDKINDGV
IPSSKWCGTANSGSAYLDLGKEVDISRWIVYHANCRGAGEGVNYNTVDFELLYAPDDGKP
VLDPTDKTAAERVKKLNYKEADKVTGNKQNVTDRNLDGPIKARYIKLHITDSDNSPWSAI
RIYEMELYGEKGEGSVAVPTAPLERNVTVYNEKGNQDKVIIDNVGMPYAEGSYPNGTVNE
KTGVVSLYDSMDAKEPIAQVRAQQPDNVYKQYAVGIAQFDNLKLKPEGGRLWYSVQDAST
GETVTTQRSSVAYPPEDGKKIPEAQAKLYGEAAGVNLSGAYGALEISGLPKEATVKVYDS
KDALKPILHSAPAGEDKKILLESVPLKEEGGTVYYTIHAPGYSDTERLELAYGEVGALPA
YQGTLAEMVNMYERGFFEEEYLDSTWGAFASARTKAAGLLEGNPTKAEADAVRMELKQAE
CGLLKKADKSRIQEVCADYEANKGHYSKESWEKFQPVFEEVKAFAQAEDETDKMTIQTQR
VKLDKAARQLVEIVPINSSVIPDEALLKAIKEQTGFESVDQLSTYEGTLDLTNLPVKDLT
GLEKMEKLKGLILDGTKVKEVNAKNLPKTLETLSMKNCGDLETIDLRNSGMDKLKQADIT
GCEKLVLVYMNTGNLEKLEVSENGKYANIYALDISGNKLDLSEKTPEGKLAAKVEENLKK
NPPEKLEKYTNVTQGRNVTADVMQGRHEKPEVMVDGKKDQNADIYYLDTNGKAVINLGEA
KDISKVGATFQKDNFPAEYKWEYSEDGKDYKELAVVKKNEKYQTENTLKTPVKAQYLRFT
VLNKGKGEAVVVELEGFEKKTIASGVTSGNQKPEAVVDYKTIPAELSLKQGSEAVDMLDY
MKNCYKEVKTVRGTKIAELTDAKWLAKDYDIEAAAKMPEGMKVVITKEDGSACQNPFVPE
NTGNYTAEYRVGEGKALASVKVKVTADKSYLEELAASCEGKKETDYTPATWAVFQEKLAK
AKELLENEFAGQDEIDAAEQELSEALTGLRVKPIKTVLHVFIELAEKELENAADKAPETM
DALNTALTEAKTVFENPNATQEEVDAAGDKLLEALNRIRPMADKEKLLNLIARVESMETS
GYTDASVKTLEEKLAESKTVAEDDNAFEEDVELAYNNLLQAVAHLEVKVHTAELEYVIAK
AEDILAKKDKYIAATLEGLSEETKKAKEVLEKADATQEEVNQAAADLAWKVGNARLKAEK
QALLDMLEEAEKMDVALYTEESARTFTGALLKARQAAEDEYATQAEVDAAISELDDAMTN
LVKAEPEQPETKPEEEQKPEQKPESEPEEEQNQDKGTEEGQQEEAKEEKPETPSHQAPSK
KPVSSTRDYAVRSRRQHSDNTASQSSKEEQTEERKETKEETLLAKGDGEENSNKETEDTA
DSEKAEKDKTVQKEEKASYGWILAGVLILAAAGGLWYWKKKQKK

Enzyme Prediction     

No EC number prediction in MGYG000003326_00157.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH85	112	413	2.2e-53	0.9968253968253968

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG4724	COG4724	4.82e-119	67	577	38	549	Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism].
pfam03644	Glyco_hydro_85	1.18e-68	124	409	1	291	Glycosyl hydrolase family 85. Family of endo-beta-N-acetylglucosaminidases. These enzymes work on a broad spectrum of substrates.
cd06547	GH85_ENGase	1.79e-68	107	445	1	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.
pfam00754	F5_F8_type_C	7.42e-11	706	847	7	127	F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.
NF033930	pneumo_PspA	8.95e-11	1643	2042	79	426	pneumococcal surface protein A. The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ASM70437.1	0.0	1	1644	1	1644
AMN35046.1	1.85e-188	46	1078	36	1034
AXH51875.1	2.56e-188	46	1078	36	1034
SQI03683.1	2.56e-188	46	1078	36	1034
AMN32287.1	2.56e-188	46	1078	36	1034

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3GDB_A	1.47e-103	67	842	170	937	Crystalstructure of Spr0440 glycoside hydrolase domain, Endo-D from Streptococcus pneumoniae R6 [Streptococcus pneumoniae R6]
2W91_A	2.55e-86	67	695	19	651	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]
3FHQ_A	3.72e-79	67	675	15	616	ChainA, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae],3FHQ_B Chain B, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae],3FHQ_D Chain D, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae],3FHQ_F Chain F, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae]
3FHA_A	5.04e-79	67	675	15	616	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]
2VTF_A	1.91e-78	67	675	20	621	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A1L251	6.13e-21	40	599	45	603	Cytosolic endo-beta-N-acetylglucosaminidase OS=Danio rerio OX=7955 GN=engase PE=2 SV=1
Q8NFI3	5.91e-20	36	517	63	517	Cytosolic endo-beta-N-acetylglucosaminidase OS=Homo sapiens OX=9606 GN=ENGASE PE=1 SV=1
Q8BX80	1.40e-17	44	517	61	509	Cytosolic endo-beta-N-acetylglucosaminidase OS=Mus musculus OX=10090 GN=Engase PE=1 SV=1
P0C7A1	2.59e-13	50	497	72	487	Cytosolic endo-beta-N-acetylglucosaminidase OS=Gallus gallus OX=9031 GN=ENGASE PE=1 SV=1
E8MGH9	1.07e-06	1647	1841	1667	1871	Beta-L-arabinobiosidase OS=Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b) OX=565042 GN=hypBA2 PE=1 SV=1

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
0.000279	0.999013	0.000191	0.000190	0.000161	0.000134

TMHMM  Annotations     

start	end
2119	2138