CAZyme Information: MGYG000004164_01716

Basic Information

• Species: UMGS1494 sp900552305
• Lineage: Bacteria; Firmicutes_A; Clostridia; Monoglobales; Monoglobaceae; UMGS1494; UMGS1494 sp900552305
• CAZyme ID: MGYG000004164_01716
• CAZy Family: GH10
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
880	MGYG000004164_114|CGC1	98236.9	4.6831

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004164	2287505	MAG	United Kingdom	Europe

• Gene Location: Start: 2961; End: 5603 Strand: +

Full Sequence      

MRLRLVSIFLCLSMFLSAVPAYAAEGGSGKKAAAEYGIIKDEFEDLSRIKAHTGAVAAVT
LEGAEYDGDTSGLSMGGAAKGTEILYEAPFEIGSYTLWLKGDTGEYTPDFKIYLSSDGKN
FTWDKNAEHRNEGKLRIYTNPEVFEENRFLKIVYNGEKAPQDLYLLKTEIREEGFVQFSG
RRIPRTEPSEFDYSSIPSLREAYKDYFRIGAALEYRDIAAEPNLLATQYEVIGSEGQTHF
NGLQQSEGNFTWYWADRIFDWGAEQGMMGRLHALMYYINLPDWVKVQPGGGTVTKELFLK
RYERHVKTVVSHYKGRVKYYDVVNELIDAGQYRPYMFEYKIFGGNEDEFEDFIANLFLWA
YEADPDAKLVFLDGGLLAKQKRNRHWFELFGPNILPRILEKGVPKENIILGEQGHWGIND
FVTEEQSGGTGNSLEGILNDVRELGLHVVFTEMDMGVTSDMYISDQTGQKTNLSRAENQE
LAAKKWGLIFDVLRENADIVDLVTFWGATDNTNVRTQTTGTCGTFFDYNFEPYPAFYRVL
DFDKKLPRWTTDDITEINYGNGWTRRGAQAAYGTPVIDGKVDDVWKKTEKIELDRQTVGS
ADKGATGTLRVLWDEENIYGLFEVNDEDINTDNPNTWFKDCVEIFIGENNSQTGAYSSGD
CQIRVTANGLKAGKGYGDWTTDWYDSAAVSDKKGYTVEIAYHMHTRKNAVGDTIGLDAVI
VDHEDGNGTRRSMRKFCDTLKQTSETPQCWGTCQLVEKVGSTVNKNSKGTGASGNAEKKR
TLKNGEVEFSVGVTAADGTEYVSLKELAAQLGGTVRYDRVTDTVSLTVGTKTAGLCIGSQ
TAEIGGTAVGMGHAVTIADGRTAVPLKELLKAMDMNFSIE

Enzyme Prediction     

EC	3.2.1.8	3.2.1.-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH10	198	541	6.1e-55	0.9933993399339934
CBM9	577	755	3.1e-35	0.9945054945054945

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00331	Glyco_hydro_10	2.00e-52	199	541	1	310	Glycosyl hydrolase family 10.
smart00633	Glyco_10	4.56e-47	243	539	6	263	Glycosyl hydrolase family 10.
COG3693	XynA	3.93e-43	210	547	39	345	Endo-1,4-beta-xylanase, GH35 family [Carbohydrate transport and metabolism].
cd00005	CBM9_like_1	4.19e-43	568	756	2	185	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	5.70e-30	577	756	1	182	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
AGC67677.1	2.28e-55	184	758	344	891
ANW98094.1	2.28e-55	184	758	344	891
CAD48314.1	2.28e-55	184	758	344	891
ANX00638.1	2.28e-55	184	758	344	891
AGI38724.1	2.28e-55	184	758	344	891

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1N82_A	7.36e-42	194	540	3	329	Thehigh-resolution crystal structure of IXT6, a thermophilic, intracellular xylanase from G. stearothermophilus [Geobacillus stearothermophilus],1N82_B The high-resolution crystal structure of IXT6, a thermophilic, intracellular xylanase from G. stearothermophilus [Geobacillus stearothermophilus],3MUA_A Enzyme-Substrate interactions of IXT6, the intracellular xylanase of G. stearothermophilus. [Geobacillus stearothermophilus],3MUA_B Enzyme-Substrate interactions of IXT6, the intracellular xylanase of G. stearothermophilus. [Geobacillus stearothermophilus]
2Q8X_A	7.36e-42	194	540	3	329	Thehigh-resolution crystal structure of ixt6, a thermophilic, intracellular xylanase from G. stearothermophilus [unidentified],2Q8X_B The high-resolution crystal structure of ixt6, a thermophilic, intracellular xylanase from G. stearothermophilus [unidentified],3MSD_A Enzyme-Substrate interactions of IXT6, the intracellular xylanase of G. stearothermophilus. [Geobacillus stearothermophilus],3MSD_B Enzyme-Substrate interactions of IXT6, the intracellular xylanase of G. stearothermophilus. [Geobacillus stearothermophilus],3MSG_A Enzyme-Substrate interactions of IXT6, the intracellular xylanase of G. stearothermophilus. [Geobacillus stearothermophilus],3MSG_B Enzyme-Substrate interactions of IXT6, the intracellular xylanase of G. stearothermophilus. [Geobacillus stearothermophilus]
3MUI_A	4.66e-41	194	540	3	329	Enzyme-Substrateinteractions of IXT6, the intracellular xylanase of G. stearothermophilus. [Geobacillus stearothermophilus],3MUI_B Enzyme-Substrate interactions of IXT6, the intracellular xylanase of G. stearothermophilus. [Geobacillus stearothermophilus]
3MS8_A	4.66e-41	194	540	3	329	Enzyme-Substrateinteractions of IXT6, the intracellular xylanase of G. stearothermophilus. [Geobacillus stearothermophilus],3MS8_B Enzyme-Substrate interactions of IXT6, the intracellular xylanase of G. stearothermophilus. [Geobacillus stearothermophilus]
3EMC_A	3.36e-37	194	543	2	331	Crystalstructure of XynB, an intracellular xylanase from Paenibacillus barcinonensis [Paenibacillus barcinonensis],3EMQ_A Crystal structure of xilanase XynB from Paenibacillus barcelonensis complexed with an inhibitor [Paenibacillus barcinonensis],3EMZ_A Crystal structure of xylanase XynB from Paenibacillus barcinonensis complexed with a conduramine derivative [Paenibacillus barcinonensis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
C6CRV0	3.70e-47	93	763	375	1064	Endo-1,4-beta-xylanase A OS=Paenibacillus sp. (strain JDR-2) OX=324057 GN=xynA1 PE=1 SV=1
P36917	3.60e-46	53	728	214	826	Endo-1,4-beta-xylanase A OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=xynA PE=1 SV=1
P38535	5.51e-45	194	729	205	679	Exoglucanase XynX OS=Acetivibrio thermocellus OX=1515 GN=xynX PE=3 SV=1
Q60042	9.16e-45	196	757	363	1055	Endo-1,4-beta-xylanase A OS=Thermotoga neapolitana OX=2337 GN=xynA PE=1 SV=1
Q60037	5.05e-44	196	757	367	1059	Endo-1,4-beta-xylanase A OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=xynA 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
0.000221	0.999113	0.000185	0.000165	0.000159	0.000145

TMHMM  Annotations     

start	end
5	24