CAZyme Information: MGYG000003237_01996

Basic Information

• Species: Victivallis sp002998355
• Lineage: Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; Victivallaceae; Victivallis; Victivallis sp002998355
• CAZyme ID: MGYG000003237_01996
• CAZy Family: GH39
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1002	MGYG000003237_57|CGC1	110991.28	7.7075

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003237	4618450	MAG	United States	North America

• Gene Location: Start: 26783; End: 29791 Strand: -

Full Sequence      

MFKRFLLSTVLFLAACAGAVPLGDFSSTAPWTVNDSEKRNQCMTLQTLPESGEKGVKLSW
DGYAFPYAELHLRTPLPLPADFRRGNVSLRLRLPARAPVRSISLRLVDATGEIFQYQLRC
LPPAEPKILTVDYPVNLMENKNSSWGGNNDKKFDLPVALKGFTIDFERESGAGEALFLGA
EAIPENTVPSAADNIRLEIETGNPVHVLTPGKADQLRLVLRNAGDARFRGKAEAVFEDFF
GRTFSEKLPSVELAAGETMTCPVRTPLPAPGHWDVRLRLFPEDGGEVTKKRSFASFKPAG
PTPGKAEGFLWGISSHPQLHPAPVQKLEALAAALVGAKVVREDVYWHRVQPARGQWDFRS
FDQTVAIFAEQGIELQAILCYCAPWAARDPGAKRPEKAEPEPEAWKTFCREMAKRYRGRV
RFWEVWNEPDVTPFSGFSSASYAKMMLNAYKAVKTGNPDARVLTGGFATLANHPMLREPG
YQENALRLGKGGYDIHAYHEHGDFHPHFVRMVEERFLPMRKRAGVTEPWWANETALTSSG
GNEKPQAMALYKKLIYAWSRGAVGYNWYDLRNDGDDPNHGEHNYGMMTRDFYPKPVYTVY
NTLTTLFGGKKFVRQLNAGEGEWLFLFRDGEEMALAAWSENGGILPVIVRTDAASAEAVD
LMNNPRPVEIHDGRILLETGSLPVTLRLRGATRAEFAGNPVRLESADLALPGKPYRFAAG
LTNPFDKPVEFVLEFRAPAGFRPEKTERRLTVPAGKTAAPVCELRADENFRPVFGTPVTL
TADYRLSGGAVKGSVSMPVRVAQVIPQGATTGRPPDFTLEHRRQVRELFTGDPTRGHLLW
KGPRDLSGRVSLGTEGANLLLQVRVTDNIHHQPERGANAWMGDNIQFALELPGRKGGWEL
GLTRLADGSPEVWCWSAPDGFDPAAAARGIVLATSREESETVYCAKIPFETLGLTPELLK
EGFRFNLLINDNDGGGRQGWISIAPGIGERKDPSQFPFVIFN

Enzyme Prediction     

No EC number prediction in MGYG000003237_01996.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH39	352	640	1.4e-27	0.728538283062645

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd09621	CBM9_like_5	2.33e-77	815	1001	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	2.86e-13	839	986	29	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	3.72e-06	840	982	12	157	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	1.56e-05	845	996	30	176	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	2.48e-04	403	509	125	237	Glycosyl hydrolases family 39.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AVM47149.1	1.00e-232	54	1001	212	1306
AVM46276.1	4.32e-214	67	1001	56	1136
AHF94342.1	1.64e-197	14	1002	42	1033
AVM44759.1	6.30e-187	171	1002	138	965
AHF90198.1	7.25e-187	33	1002	35	1006

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5JVK_A	1.01e-21	334	683	127	493	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 LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.001892	0.410107	0.585481	0.001397	0.000639	0.000468

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003237_01996.