CAZyme Information: MGYG000001451_03105

Basic Information

• Species: Paenibacillus_A antibioticophila
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A antibioticophila
• CAZyme ID: MGYG000001451_03105
• CAZy Family: GH85
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1759	MGYG000001451_2|CGC4	191021.23	4.3167

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001451	5573040	Isolate	not provided	not provided

• Gene Location: Start: 277530; End: 282809 Strand: -

Full Sequence      

MNFGNKKKIKIASTILTFALVLTSFPLYVQAGDTWPFTGESAHGENQPSVHGYTSGHVLN
WSPESDPGAELLRSRVPLQQRIDPLAATQSNPDLDPNIKMTNVSGDYGNAFIENAPYTNK
FAQYHFGFWQYVDYWSPWHGTATAYTPPEYYDDLAQKDWQQKWFEFGMLNIPNPTYTDAA
HKNGVMSLAGIFFSNNDRGQQTYKQMIVKDDDGNYPVAEKLIEMAEYFGYDGYFINQEEV
GPNVTVADIPDYIGFMKALQKGGLYIQWYDSLNTATGSNTFARTINDNNISFLYDKNAGE
QVSQSFFFDYGMGSSLITSAKAYLNNLNQQYGTDFDLFDVGFAGLEAGRDRFKSVQGNAL
SNKLSNGLPQVSIATLGADFVHAGLDEDMGLAWPVNHRAENDYQWMTKVREQLWWSGPNI
DPKNTAKSSVNTASDVYADNRYWPGIASVIAERSVIGDSNFYTNFNTGHGLSYYVDGNVS
NDSEWSNMSLQDIPVTWQWWQDTDGNRLTVDFDYGPEYSLASTQRFNYQQIGAYQGGSSL
VINGDLDAENFLRLYKTDISVNPGSKLSITYNKSSQDDGSTLQAGLIFEDDPANVVKVAV
QDSGKETNGWVTAELDLSAYAGKSIAVLGLVFDPGAGVVNDYQMNIGQISISDGSAVVPD
APAGLSISELHPNTKELIVKWNLDNDYSSVKQYNVYVNDVYMGGKYDEVFYVKQLPADSG
VIKVAAVGADGREGPAATLPYDLTSAPSNITVDSREDGVLEVSWINAPGTSGDITVSVTS
RNWITAEQPVNEQTVVPSGSTSAVFNNMPVNGDDYLVTVSSAGGQSVMASGSFIDKIAEP
YAEPWAWNGDTLSLPMPNTRDWRYMYFYEDGELKNFPVTYISGAAGNKDRIIRGRTTKAS
LSFSSTAENIYVVMEDYAGNKSAPVYLRGKERYTVTFDSNGGEHAVPTVESAFGAKISEP
STMMTREGYEFLGWYNGDTKWSFAADSVKQDLTLTAKWKLKDPEVVLIKEGSFREGAAAA
LKAVAAGKGALSYSWAVDEGSGYNGISVTDTVYSIPRVTLDMEGFKYKVIVTNEEGGVGE
AETAITVTPASADPVAPDFERNLDAGKTVKENEEVTLFVSTTGDVEQVVWEAKLKDSDTW
TQVGEGSSAYTFTAQAEHDGALFRVVLQGIAGSNPSTAVSNELLLHVIPLVVNADPVIHT
VTASKNPAEVGDTVTFTVQASGEGVLSYQWFKDGAPIAGATNAEYTIDSAAASDGGAYKV
EVTHTIHLHGRDYIGVKESDEVLFTVETEQSAEWSLLSSLINQIKALKNDVVYTAQSIAE
LKSSSAYLTAVALTADSPADTVRTAYENLVQARSRILKLYVPVSPGTGTNEGAGGDSGGT
KTENGTSPLPPANPSQMIVSGQDLLKASEAGVVAITVKTEVTSIDLPLNAGELLNQNILR
IETDTLTLDIPPEVLKQMKDLLGDSPLSTNKLQLGIQPISLDQAGVTANSEISIKGSTVK
LDLKVVDNQGATVKEITEPTIQPLNIKMPITTGLNADLLGIYLINNDGTLTYLGGARNGN
VMGLEVEQAGTYALLEYKVNFQDVSDTHWAADAIQILAAKHWTQGVPGNKYEPGRTITRA
EFTTLVAKALHLKEQSELKFNDVPSDAWYKDDLAKLVKLGLVSGRSADRFEPDAEISRQE
IVTILMRALELQQDVDAPAPSDSSRFKDDSSIASWARASVHAAAELGLVKGQGDHFAPAQ
SATRAEAAQFAINFLLNSE

Enzyme Prediction     

No EC number prediction in MGYG000001451_03105.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH85	111	474	2.8e-64	0.9777777777777777

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG4724	COG4724	2.41e-88	7	653	2	551	Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism].
pfam03644	Glyco_hydro_85	1.08e-57	118	470	2	291	Glycosyl hydrolase family 85. Family of endo-beta-N-acetylglucosaminidases. These enzymes work on a broad spectrum of substrates.
cd06547	GH85_ENGase	2.52e-55	103	505	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.
NF033190	inl_like_NEAT_1	4.01e-16	1579	1753	580	750	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	2.71e-13	933	997	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	1	1755	61	1741
QUL53214.1	0.0	10	1755	12	1677
ASA25869.1	0.0	10	1755	12	1596
AZN42923.1	0.0	4	998	6	993
AIQ69045.1	0.0	4	929	6	929

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2W91_A	5.70e-54	58	742	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	1.59e-52	58	742	171	784	Crystalstructure of Spr0440 glycoside hydrolase domain, Endo-D from Streptococcus pneumoniae R6 [Streptococcus pneumoniae R6]
2VTF_A	1.84e-46	58	696	21	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	2.30e-46	58	696	16	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	3.08e-46	58	696	16	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
C6CRV0	2.76e-30	1399	1748	1095	1452	Endo-1,4-beta-xylanase A OS=Paenibacillus sp. (strain JDR-2) OX=324057 GN=xynA1 PE=1 SV=1
P38536	8.12e-29	1462	1758	1569	1858	Amylopullulanase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyB PE=3 SV=2
P38535	2.86e-26	1574	1758	901	1084	Exoglucanase XynX OS=Acetivibrio thermocellus OX=1515 GN=xynX PE=3 SV=1
P49051	1.81e-18	1581	1750	34	199	S-layer protein sap OS=Bacillus anthracis OX=1392 GN=sap PE=1 SV=1
P38537	2.73e-17	1589	1731	42	178	Surface-layer 125 kDa protein OS=Lysinibacillus sphaericus OX=1421 PE=3 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
0.000277	0.999027	0.000200	0.000179	0.000157	0.000143

TMHMM  Annotations     

start	end
12	29