CAZyme Information: MGYG000000720_02884

Basic Information

• Lineage: Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; Victivallaceae; Victivallis
• CAZyme ID: MGYG000000720_02884
• CAZy Family: GH39
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1137		126700.76	7.4135

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000720	3759035	MAG	Kazakhstan	Asia

• Gene Location: Start: 1627; End: 5040 Strand: -

Full Sequence      

MRKPYTFFTGLTLALASALSGAQEMDNSFLRAGGSYLYKGEARGQSLEFTTAPDGKPATR
LGWDFSRFKFAEVNLRKPLQITSFQELELALDYSSSGRRQLDSCGFRIADASGEVFQWSC
PAGDDLPGWKTIRCRLTPRNFNSCWGGDGNKTIDFPARLIGFGAGFCRESSGPVWFGALR
FRFPEEKKKIPVLEYSWNFDEKAEFWKSWGAGRLEKQTVSADRNGEIFLNERMFAIRPAE
ECRELRLSCTLQNGNATVAVRVRDGAGKSQLLTALPLVSGRNRLSFPLAGLASPVRIEQL
RIDNRGGSLRIELETLELWTEKETAAALSAAVDTGHPLHLLLPGKSRTAVLVLTNRAERP
LTLKGKFTLSDYFGECARFERDIALPAGKSMRIPVDTTPFPRDGIYYVDYRFVNPDENSS
EGVSGRISFARMTPAGPTPGRAQGFLFGICTHTERWGIRDRELEVLACALAGAKVIRSSP
GWEIVQPKKGAWDYTLYDRMVEQYAASGMELQAGFGLCNQWGKAADAKMRDGSPDRLNNG
RSMPDLELWRLYVRNTVSRYRGKIRFWEVWNEPDLTHFANFGVEDYARLLAASAEEIRRA
DPEARVMNGGFAGLTAPAQVEYQRRFLELARGTFDVHAFHQHGEFGVFRQVIDELFLPQR
RETGTAVPWFANETAMHSLGGREQLQAESLFKKLIFARARGAIGYTWYDLRNDGFSVTDA
EHNYGMVTNDFYPKAVYPAFAALVNLYRDADFDRELPLGTGEFAFLFRKKGELILGAWRE
VSADDATGGLYAGTTDGTRVRRVDIMGNSTDVPLENGRFLFQPGRIPESLVVEGGSRLAF
HPVLNIATIGPVAEGRPATLEFELPDDSIPMLKCELAAEKPFQIREKKFLLKAVPGSRTK
IRKTLTVGSGLGTEMRQLPLRIAIPGGGEAEILIPVYPARKLSRALSPENPDFVLNRRGQ
VVSVYDKVPGHSIWEGPEDLSARISCGIEQDELVVRAEVTDDIHRQNDSGSEIWRGDSLQ
LFFQLPGQKGEWELGNALTSAGGEHWVWRAPEGFTAAAARSAIRSKAGRVGSVTTCEIHI
PFKAIGLTPQMLREGFRFNLLVNDSDVPGDEREGWIRLAPGVGDERNTLRYPVVFFE

Enzyme Prediction     

No EC number prediction in MGYG000000720_02884.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH39	488	784	1.2e-27	0.7378190255220418

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd09621	CBM9_like_5	7.81e-57	951	1136	1	188	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	4.79e-11	974	1121	30	175	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	1.48e-09	965	1112	3	154	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.
pfam06452	CBM9_1	4.07e-05	959	1116	3	160	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.
pfam01229	Glyco_hydro_39	5.62e-05	547	645	129	232	Glycosyl hydrolases family 39.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AVM47149.1	7.69e-199	61	1137	216	1307
AVM46276.1	2.21e-188	70	1137	56	1137
AVM44759.1	5.82e-154	227	1137	60	965
AHF90198.1	3.27e-134	37	1136	35	1005
AHF94342.1	1.28e-129	294	1137	182	1033

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5JVK_A	1.25e-17	448	833	107	499	Structuralinsights into a family 39 glycoside hydrolase from the gut symbiont Bacteroides cellulosilyticus WH2. [Bacteroides cellulosilyticus],5JVK_B Structural insights into a family 39 glycoside hydrolase from the gut symbiont Bacteroides cellulosilyticus WH2. [Bacteroides cellulosilyticus],5JVK_C Structural insights into a family 39 glycoside hydrolase from the gut symbiont Bacteroides cellulosilyticus WH2. [Bacteroides cellulosilyticus]

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
0.012663	0.981565	0.001694	0.001786	0.000961	0.001293

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000720_02884.