CAZyme Information: MGYG000002414_00810

Basic Information

• Species: Paenibacillus odorifer
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus odorifer
• CAZyme ID: MGYG000002414_00810
• CAZy Family: GH85
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1684	MGYG000002414_1|CGC16	181288.79	4.4777

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002414	6802552	Isolate	South Korea	Asia

• Gene Location: Start: 921554; End: 926608 Strand: +

Full Sequence      

MNLHTGKKARRKLTSAVLAAALLVSGLPLTAYAGDTWPFTGDSAPGANQPNVHGYTSSHI
ANWSPATDPDAELLRSRVPLQKRNAPFAATQANPALSADTQMINVAGDYGNAFIENAPYT
NKFAQYHFNFWQYIDYYSYWHGTATAYTPPEYYDELAQKDWQQKWFEFGMLNIPNPTYTD
AAHKNGVLSLAGIFFSNNDRGQQTYKQMIVKDENGNFPVADKLIEMAGYFGFDGYFVNQE
EMNPNVATQDIPDYIAFMKVLQEGGLYVQWYDSLNTNTGANTFARTINDTNISFLVDKST
KEPVSNSFFFDYGAGNTQITNAANYLSNLNASLGTSYNLFEVGFAGLEAGRDRFKSVNGT
ALMSKLDSNGLPRLSLATLGADFVHAGLDEDMNLSYPVSHRSENGYQWMTKLREQLWWSG
PNVDPKNTIKSATNTVSDVYADNRYWPGISSVIAERSVIKDKNFYTNFNTGQGLSYSVNG
EVSNPDEWSNMSLQDIPVTWQWWQDTAGNKLTVDFDYGPEYNLAGTNRYNYEQIGAYNGG
SSLVVNGNLNAKNFLRLYKTELEVNGNSKLSISFNKPSATDASAMAVGLILADDPNTVVE
VAVPNSGQHSEGWVTKELDLSAYAGHNIAALGLVFDPGQGTASTYQMNVGQLRVYDGSAV
KPAAPAELAVAEAFTDTGEMVVKWKLDPDYTKIKQYNVYVNDVFMGGKYDEVFYLKHLPV
KSGTLKVVAVGADGVEGEAASLAFDLDAAVSGVKVDSSADGELTVNWTNSTQASGDITVR
VQSLNWITTSEPVSQQVVAPAGASTALFTGMPVNGDDYIVTVTAGNTDPVSVSGRFIDTV
AEPYAEEWSWTDGKLNLPMPNTRDWRYMYVYEDGNPKSFATTYSSGNKPMIIRGRTTKAS
LSFTSTAKVVHVVMEDYAGNRSKPVYVKGSYPVLFDANGGEPANTVAEAVYGTLLLEPTG
IAREGYDLEGWYVGEGEGARRWNFAEDLITGELNLQAKWALQAPKVQIVGEGSFRENTSA
TLTAVATGAGQLTYAWYADTGSGYGDALGMSASYTIPALTTVMDGDKYKVIVTNESGGSS
EAEYTLNVTPAEAPWEVPDFITDLPSALDVIMGEEVKLFVQIRGDVESIRWETKAATAEE
WTVVESVTSAVYAFTASEADSGTQFRVVLIGKEGTEPSTRTGNELTVTVHPAPDAPVITS
NSVDKNPAVVGDKVSFAVVASAVYGELSYQWLKDGQAIEGAVERDYTIASAKETDSGEYT
AVVTNTKILNGHPYTAVQKSGTIDFKVHNTPVSTPQPTLAPETGTGTGGTTPAATATPLP
SPTSTTLTVPASALSTSTENGKVTVNVPAGVTAIELPVNAGELLGIHQLELAASGTTLGI
APELLVQLKALLNEAQASGGKIQAKLSPETLNMSTLKAERGVVLRGTGMTFDLSIIAGNG
TSSRLPSFSKPVTLQWSATNTDYNTNLLGLYAIAEGGSLTYLGGVYANGFLQGEFSGTGR
LAVLEYNKSFADVPSTHWAADTIRQLAAKHLVQGSSENGFEPARSITRAEFVKLLAGVLG
LQDQAELKFSDVPSGVWYEQDLARLVRAGIVGGRTAEHFDPSANISRQEIVTMLMRAYVL
EHGTLQSSAPATFTDSNEVAAWAADSVNAASSLGLLNGRTDGNFVPGGLATRAEAAQFIL
NYIR

Enzyme Prediction     

No EC number prediction in MGYG000002414_00810.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH85	113	476	1.1e-66	0.9746031746031746

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG4724	COG4724	1.81e-85	47	656	26	551	Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism].
cd06547	GH85_ENGase	1.40e-56	105	508	2	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.
pfam03644	Glyco_hydro_85	6.16e-56	120	473	2	291	Glycosyl hydrolase family 85. Family of endo-beta-N-acetylglucosaminidases. These enzymes work on a broad spectrum of substrates.
NF033190	inl_like_NEAT_1	2.22e-16	1510	1684	582	753	NEAT domain-containing leucine-rich repeat protein. Members of this family have an N-terminal NEAT (near transporter) domain often associated with iron transport, followed by a leucine-rich repeat region with significant sequence similarity to the internalins of Listeria monocytogenes. However, since Bacillus cereus (from which this protein was described, in PMID:16978259) is not considered an intracellular pathogen, and the function may be iron transport rather than internalization, applying the name "internalin" to this family probably would be misleading.
pfam00395	SLH	2.27e-07	1633	1675	1	42	S-layer homology domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AWV31864.1	0.0	1	1684	59	1742
ASA25869.1	0.0	5	1684	5	1597
QUL53214.1	0.0	11	1684	11	1678
AIQ69045.1	0.0	1	931	1	931
QQZ59873.1	0.0	1	931	1	931

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2W91_A	2.35e-53	60	745	20	633	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	6.09e-52	60	745	171	784	Crystalstructure of Spr0440 glycoside hydrolase domain, Endo-D from Streptococcus pneumoniae R6 [Streptococcus pneumoniae R6]
2VTF_A	1.01e-45	53	699	9	568	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	1.70e-45	53	699	4	563	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]
3FHQ_A	2.27e-45	53	699	4	563	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P38536	1.30e-28	1338	1679	1499	1851	Amylopullulanase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyB PE=3 SV=2
P38535	7.03e-25	1486	1679	889	1077	Exoglucanase XynX OS=Acetivibrio thermocellus OX=1515 GN=xynX PE=3 SV=1
Q9ZES5	2.16e-20	1508	1679	32	201	S-layer protein OS=Bacillus thuringiensis subsp. finitimus OX=29337 GN=ctc PE=1 SV=1
P49051	3.31e-19	1508	1679	32	200	S-layer protein sap OS=Bacillus anthracis OX=1392 GN=sap PE=1 SV=1
P19424	9.96e-18	1510	1679	41	210	Endoglucanase OS=Bacillus sp. (strain KSM-635) OX=1415 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
0.000273	0.999004	0.000199	0.000208	0.000160	0.000136

TMHMM  Annotations     

start	end
13	32