CAZyme Information: MGYG000003943_01708

Basic Information

• Species: NSJ-50 sp014385105
• Lineage: Bacteria; Firmicutes_A; Clostridia; UMGS1810; UMGS1810; NSJ-50; NSJ-50 sp014385105
• CAZyme ID: MGYG000003943_01708
• CAZy Family: GH39
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1402	MGYG000003943_12|CGC1	159426.13	4.6643

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003943	2095283	MAG	United Kingdom	Europe

• Gene Location: Start: 28843; End: 33051 Strand: -

Full Sequence      

MKKLISFITILSVLMTSVVCFPLFAEAVSVPSAKLTDYCTNPDYDNIFTLESDINTDYVL
LDRLSDGFLIMSDKVYDAQKFDEDAAQKFDPSDENNVAYYLNNEFFKTYIPEEMREYIAV
RNWKTEGGNVSGICPNTYFANCRISLLSFEEYNNYYKKFGTVDHDNEIDWWLRTGDGNKK
ENVIAGGGVYTNWGKFVSADASLQCGLRPIFVLTDAFFENVKLNTFKMGKNVKKALLENI
SAQSMQKAGYSPERLRGIGYESINGPDEKVSITIPNEPYYMQDHEYSYFSVNISHSDTTA
RSYTIEYTSGENSKKIDVTVKPYKAYNGKISLKDQKKGVQNLDIKIMRDGELVGYDSARI
CLVDYYKRTPLDKYSRIGIGMPAWHSIETASGAGDAYDSFVKLSYRIAEIGFTKARNSPE
WTWVESERGVYVLDKDRYKYAVAFRENGIEYVPFKINFGNQAVTKRETNNKMAAPNTCDA
IQGFADYATNVKKLYDKIFYPKIAFNTYEVWNEPNLKNYWYPDVNYLEYSQMLNAVTYKI
IRENPDAQVMAGSITSANQRDIFDAMYRNGMTMYSDQIAIHPYSYPNEPDERYVIRTPQY
LEKLEEYGGWLEVAATEIGWPTWQSYNSATYDQQAAYMVKMLVLNDELGFIMTDVFSARN
QGLQKTYIEHGFGIFEYNDRPKPSAASLSFFNNNVNDALYAGEFEISEGVRSFIYKRPGK
SRPFAICWVTDDSKITQYTLKEKQYATDIFGNKLDGKTVTIGRTPIYIFELSDSYYMRMI
AHDILGIYNELTEKLGDKFDFSAVGDLAKEASESNLSYSDTKKYIDKYFDLAEKLTEKAL
NDENLTHENSALIAHIMFKKGESMAASLENMKLDSSAGVLHYEKTKNSAAAKKGDEPEAS
LLFTDAMLRYAYRYTSRIKEIKKMDDFDGKKERMGYYGYLSDKVCALADIMQKYEIPNPS
RVLFTYTQQTRQIMYKGKGYTIKAELENLRNKDFDGTAVLVDENGDAIGEEVAVKAKSGE
CVDVYVEGTAPKLRDAGTYIYNILYKEDGEVVKKQEIEVILKSLIDIDLMASETTLSNLN
SVTVEVKNTFESAVKGKVKLTSPEGWVVESEKEINIPAGETQYIEFKVDSAKKVPFNEYC
FNISVEDEEGSELAHCEKLLDFRIMVYDDKNYNPDTFDGDIAGWEDAYPIYVVSPENPGD
INSWLGCDRSLKMLAKWNENNIYILADVYDVVHNNTYTGSNLWQGDSLQIAFDTFMNGLA
PGTTKGYQSDDYEFGIGLTPNGIENYQYVASDSPIGNIEEHLSAVIRNDKLGITRYLIKI
PNTYTKQLALKAGNKFGFNIAVNDSDVLLREGYSQYTSGICDSKNPSMFKAFSLVTNDSA
QTGETDKIAFYEKVEEFRQGGN

Enzyme Prediction     

No EC number prediction in MGYG000003943_01708.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH39	506	737	1.5e-21	0.5591647331786543

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd09621	CBM9_like_5	3.14e-27	1208	1369	27	183	DOMON-like type 9 carbohydrate binding module. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized heterogeneous subfamily are often located at the C-terminus of longer proteins and may co-occur with various other functional domains such as glycosyl hydrolases. The CBM9 module in these architectures may be involved in binding to carbohydrates.
cd09619	CBM9_like_4	8.08e-12	1174	1346	1	161	DOMON-like type 9 carbohydrate binding module. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized heterogeneous subfamily are often located at the C-terminus of longer proteins and may co-occur with various other domains.
cd00241	DOMON_like	1.08e-11	1208	1354	17	156	Domon-like ligand-binding domains. DOMON-like domains can be found in all three kindgoms of life and are a diverse group of ligand binding domains that have been shown to interact with sugars and hemes. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases.
cd00005	CBM9_like_1	1.56e-10	1172	1346	6	154	DOMON-like type 9 carbohydrate binding module of xylanases. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. The CBM9 domain frequently occurs in tandem repeats; members found in this subfamily typically co-occur with glycosyl hydrolase family 10 domains and are annotated as endo-1,4-beta-xylanases. CBM9 from Thermotoga maritima xylanase 10A is reported to have specificity for polysaccharide reducing ends.
pfam06452	CBM9_1	7.86e-08	1217	1346	39	151	Carbohydrate family 9 binding domain-like. CBM9_1 is a C-terminal domain on bacterial xylanase proteins, and it is tandemly repeated in a number of family-members. The CBM9 module binds to amorphous and crystalline cellulose and a range of soluble di- and monosaccharides as well as to cello- and xylo- oligomers of different degrees of polymerization. Comparison of the glucose and cellobiose complexes during crystallisation reveals surprising differences in binding of these two substrates by CBM9-2. Cellobiose was found to bind in a distinct orientation from glucose, while still maintaining optimal stacking and electrostatic interactions with the reducing end sugar.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUL56627.1	3.72e-156	2	1374	9	1365
AIQ40299.1	9.73e-156	2	1374	9	1365
ACZ43011.1	2.21e-62	411	1375	328	1275
QTH41073.1	6.52e-49	466	1383	706	1643
CQR57727.1	1.29e-45	476	1375	715	1635

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4ZN2_A	1.59e-09	500	734	128	362	Glycosylhydrolase from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1],4ZN2_B Glycosyl hydrolase from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1],4ZN2_C Glycosyl hydrolase from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1],4ZN2_D Glycosyl hydrolase from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1]
5BX9_A	1.59e-09	500	734	128	362	Structureof PslG from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1],5BXA_A Structure of PslG from Pseudomonas aeruginosa in complex with mannose [Pseudomonas aeruginosa PAO1]

Swiss-Prot Hits     

has no Swissprot hit.

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
0.000840	0.645323	0.352770	0.000571	0.000259	0.000202

TMHMM  Annotations     

start	end
7	29