CAZyme Information: MGYG000004513_03126

Basic Information

• Species: Victivallis sp900550905
• Lineage: Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; Victivallaceae; Victivallis; Victivallis sp900550905
• CAZyme ID: MGYG000004513_03126
• CAZy Family: GH39
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1005		112855.58	9.2078

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004513	4294613	MAG	Israel	Asia

• Gene Location: Start: 1668; End: 4685 Strand: +

Full Sequence      

MVRFFAFFLLIGIIFPASAAEVLQEFLYRPEQDEAEIVFFRRNHTSIRQTSQGEFGRVAG
KRAGWRVNCAAEPESTYFEFCFPGGKKLSDFTVAEVRIQVFLPVNHSVDDLNLRLQDVDG
EVFQFRRKLPAGKSRWTEISYHVETNAPKAESWGGGKKANKKLDAPLRLVGITGDLKRTA
GEIGIGEVVLNVINSNAPVLPEVMTGSGTPIHVLKPGEEEKLALEFRNPRPRMASAVAEW
QLIGVRGETLEKRQQTLRLSPGEVKLRKLPVPKQFGVYRILTEVKDSDPAVKPVKKELRF
AYMKPAGPTPLEKNDGFLFGVCSHPQRHVSADQDLEAMAAAWCGVKALREDIDWARIQPA
RNRWEFQSFDGVVRRFGKVGIEVMPILSYCPAWAAAADWKPKSLSRANATMNRRPDYEYW
RQFLRKVAERYRNAVRFMEVWNEPDLAIFANFSAEEYVKMLESAYAEIKNTAPEIQVLTG
GFSNLPERSSPQLMPAVIRSGKYDVLAFHGHGLFGGYLYQITRICSAYGNRKPWFANETA
LSSMVYGEEVQAQTLFRKLIYSWAKGSIGYNWYDLRNDGFDPANNEHNFGMITADFYPKP
VYVAYNSLANLYRGGTFLKPLSLGNEIHGYLFRGQDGGMLLAAWSDTGDDRILPLAVSGV
TGSAETVDLYGNVRKLPVKNGVAIFEIGQEPATLRVSGQTEEIQVAGALVRPAGKLEIVP
GGHTVFSFEIYNPERRSREYHVQLSLPPGLSQTAAVTPLRLAPGENRKVGFPVRAEESFR
SLPGKTKELTLSLGDRSFRYRIETVTLMPARGYHSEPDFELNSAEQVYSLVPNSPETAHL
FWKGPRDLSAKIWLGRDGNNLLLRAEVVDDRHTQPYSGERVWQGDNIQFAMVLPGQKGNW
EIGLTRTDAKRPEVHVWLAPERFHPAKTASQIVLNTSREEKTGLTRYEARIPFSAIGLTD
AVMRRGFQFNLLVNDNDGAKRESFIAIAPGLGDNKDSSQYPVVRF

Enzyme Prediction     

No EC number prediction in MGYG000004513_03126.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH39	361	645	2.9e-28	0.7238979118329466

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd09621	CBM9_like_5	8.19e-76	817	1005	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	4.80e-16	842	994	30	179	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	4.32e-10	840	986	10	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.
COG1874	GanA	5.66e-05	317	467	16	195	Beta-galactosidase GanA [Carbohydrate transport and metabolism].
pfam06452	CBM9_1	8.10e-05	847	1004	30	180	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
AHF94342.1	1.37e-272	33	1005	56	1032
AHF90198.1	6.88e-245	77	1005	68	1005
AVM47149.1	3.61e-172	172	1005	471	1306
AVM46276.1	1.82e-167	209	1005	336	1136
AVM44759.1	1.23e-147	213	1005	172	964

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5JVK_A	1.58e-19	320	723	107	531	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
0.000694	0.998465	0.000177	0.000225	0.000199	0.000195

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004513_03126.