CAZyme Information: MGYG000001542_04799

Basic Information

• Species: Paenibacillus_A sp900069005
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A sp900069005
• CAZyme ID: MGYG000001542_04799
• CAZy Family: GH85
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1660	MGYG000001542_44|CGC11	181147.37	4.4554

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001542	5846629	Isolate	not provided	not provided

• Gene Location: Start: 567218; End: 572200 Strand: -

Full Sequence      

MIKLARRKSFKRITVTALIFGVVVAGFPHAAFAGDTWPFEGDSAHGKNQPSVHGYTSSHI
MNWSPETDPDAEMLRSYVPLQKRIAPFSATQANPELGSEAQMITVAGDYGNAFIENAAYT
NKFAQYHFNFWQYTDYYSYWHGTATAYTPPEYYDETAQSDWQQKWFEFGILNIPNPTYTD
AAHKNGVLSLAGIFFSNNDRGQQTYKQMIVKDEHGNFPVAEKLIEMANYFGFDGYFMNQE
EQSPNVAVADIPDYIAFLKVLQKGGLYVQWYDSLNTATGSNTFARTFNDNNISFLYDKND
GEPVSQSYFFDYGMGSSQITGAKNYLNQLNQSNGTDIDLYDVGFAGLEAGRDRFKSVQGS
ALKSKLDSKGQPQLSLATLGADFVHAGLDEDMNLSYPVKHRAENEYQWMTKVREQLWWSG
PNIDPQNTTVSATNTVNDVYADNRYWPGIASVISERSVIAGTNFYTNFNTGHGLSYYVNG
SVSNDDEWSNMSLQDIPVTWQWWQDTVGSKLTVDFDYGAKYNTSTSRYNYSKIGGFNGGS
SLVVSGDLDAENFLHLYKTDLDVIANSMASLTYNKPAADDDSSMALGLLFADNPDVVVKV
PVPESGNQTDGWVTKDINLSSYAGKRIAAFGLVFDPGQSATIADYQMNVGQIRITDGSAA
KLSAPGGLTITQAFADSNEMNLKWEMDSNYNQVKQYNVYVNDVFVGGKYDKVFYIKNLPA
KSGVVKVVPVGTDGLEGEAATVSFDLTASVSDITADSRESGEFIVSWENAAPAFGEITVK
VRSLNWITTEEPVSEQMIVPAGSTSASFTDMPINGDDYLVTVIPAGADPVSISGNFIDKV
AEPYAEAWSWEGNKLNLPMPTARDWRYMYVYEDNVLKSFPTTYSVGNKDRIIRGRSTKAS
LSFTSNAQLVHVVMEDYAGNKSEPVYLKNYQISFDTDGGEPALNQISAAHGSKIGEPTGI
AKAGYVLEGWYNGGKKWNFAEDVVTGDLTLKAHWVLEAPSFTVDLQPSKTVNEGDEVNLS
VVAKGNIESLTWQTMPAGGDSWNSTTVTEDVYSFTAQAEDNGTRFRVVLRGIEGTEPREV
TSTELTLTVAPAGVDIDEPEIHRVDVSSNPAVMGSQVTFSVDARANGTLGYQWYKDNTAI
ENAVSATYEIGRVTANDAGKYKVVVTNTIEFHGQAYTAAKESEEIDFEVSRDLAEWKQLN
ALLTEIDVLKNNDIYTAQSIAALKASTAYKEAKLLNADADPDVIKEAYAALLQAKNDILV
RVASGGGPGNGGNGNDNGSGSSSGSGQTPDITPAPKPEDPNTLVITAHELSKSAENGRVA
ISVEAGVTNIELPVNAGELLGQNALQLQTDKVTLEIQSELLHQLQAAVDKDQLKDSKIRV
TIAPKSLSEAGIHSSTGISLQGGAVELELSIITGTGDAHHLSGFAPQVKIAFPMNKILNA
DLLGIYKIAADGTPTYMGGWRNGQMMEIEIGTAGTYAILEYNVSFSDVPANHWAADAIKK
LAAKHLIQGVSENEYQPNREITRAEFVKIMANALQLDAQAVLTFTDVAQDAWYREDLAKM
VEAGLITGRSESSFAPNAKISRQEMATILMRAYTLEHGSAAIEYTVSFKDEAHIAAWALD
NIKAAASLGLIHGRTGERFAPEDLATRAEAAQIMANYLSQ

Enzyme Prediction     

No EC number prediction in MGYG000001542_04799.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH85	113	477	5.6e-67	0.9777777777777777

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG4724	COG4724	7.82e-84	47	656	26	551	Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism].
pfam03644	Glyco_hydro_85	3.44e-57	120	473	2	291	Glycosyl hydrolase family 85. Family of endo-beta-N-acetylglucosaminidases. These enzymes work on a broad spectrum of substrates.
cd06547	GH85_ENGase	1.91e-56	104	506	1	337	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.
NF033190	inl_like_NEAT_1	3.94e-17	1483	1660	580	754	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.
pfam09479	Flg_new	2.99e-12	930	993	1	65	Listeria-Bacteroides repeat domain (List_Bact_rpt). This model describes a conserved core region of about 43 residues, which occurs in at least two families of tandem repeats. These include 78-residue repeats which occur from 2 to 15 times in some proteins of Bacteroides forsythus ATCC 43037, and 70-residue repeats found in families of internalins of Listeria species. Single copies are found in proteins of Fibrobacter succinogenes, Geobacter sulfurreducens, and a few other bacteria.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AWV31864.1	0.0	7	1658	65	1741
ASA25869.1	0.0	1	1658	1	1596
QUL53214.1	0.0	1	1658	1	1677
AZN42923.1	0.0	7	1042	7	1048
CQR56044.1	0.0	8	928	8	928

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2W91_A	3.09e-53	60	752	20	640	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	7.87e-52	60	752	171	791	Crystalstructure of Spr0440 glycoside hydrolase domain, Endo-D from Streptococcus pneumoniae R6 [Streptococcus pneumoniae R6]
3FHA_A	1.58e-46	51	699	2	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	2.12e-46	51	699	2	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]
2VTF_A	4.10e-46	51	699	7	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P38536	7.34e-27	1367	1660	1568	1857	Amylopullulanase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyB PE=3 SV=2
P38535	1.35e-25	1478	1660	901	1083	Exoglucanase XynX OS=Acetivibrio thermocellus OX=1515 GN=xynX PE=3 SV=1
C6CRV0	3.27e-22	1319	1654	1121	1455	Endo-1,4-beta-xylanase A OS=Paenibacillus sp. (strain JDR-2) OX=324057 GN=xynA1 PE=1 SV=1
Q9ZES5	1.61e-20	1484	1655	33	202	S-layer protein OS=Bacillus thuringiensis subsp. finitimus OX=29337 GN=ctc PE=1 SV=1
P49051	1.09e-19	1484	1655	33	201	S-layer protein sap OS=Bacillus anthracis OX=1392 GN=sap 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
0.000377	0.998789	0.000252	0.000219	0.000174	0.000151

TMHMM  Annotations     

start	end
13	32