CAZyme Information: MGYG000002473_01297

Basic Information

• Species: Victivallis vadensis
• Lineage: Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; Victivallaceae; Victivallis; Victivallis vadensis
• CAZyme ID: MGYG000002473_01297
• CAZy Family: GH167
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1019		113122.99	6.8276

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002473	4576885	Isolate	not provided	not provided

• Gene Location: Start: 18992; End: 22051 Strand: -

Full Sequence      

MVKTLLGAVLLAGTAAGWAGNSPVLQQEGDYFCRATDAPFKFRGELSEWRERGALPLFLA
AEKNRMIPDWEGPLDVDATVYLLHDAQYLYFGALVRDRLPSYQPVPEALYRGDGFQLAFD
PLDDTILPGYDANDIELGFGRLRDGSAAAYCWRGGEALPTGPLADVHLKITPAGEHTLLY
EAAIPWRCLAPFDPRKLEKFGFDVLYNSARDGKRRGWLHWTPGVGEEKLAFLFRNIRLAG
KGEGAAEAAINLDRSQYSSGDPALVSLYLPTEQAGKGQVHFTVRQGEREVWRETVGFDAQ
PGGTVVRWAYQIGRLRGDGLQVDARAVWPGGETALNAELLNLSPESLKQQAQAVAERAFA
FRKRLEAARRAGVAVDYPLTALAVCDVTLKYRRRDLEKPALLKEYALLPKIRRQFRQLDA
MLERAEQELAGLESGALKPRPVPAPPMRNLTIRDGAFYSGDEEVLLIGPLGWWEPFDDLK
SLSELGFNLFSSTLIAQAVTPAPDKVRLDGARRIDRGLREAAKYNLAFDFLISPHPLPQG
WKEKHPEMAQYPSGGWIGSSLYHTATRTMIDAMWKNLLPVVRDNPNLIALDLVNEWSFSD
GVREIHPVMLAKFRAAMRERYGSVAAANRNWGTDCRDFDSLDPMKLKRVSAGFRYDFESF
RNREGLENLRFLRDTARKYAPGTPLHVKSIAVTDLDPGQYLPVGVQREERGEITDFAGSD
CAGIMELDFYRSMVPGKPAADTEFHVSVNTTPHEMAADAWSAMLHGESLREYYAWTGRYS
AELMAAGALLHIPESLEALGRTALDLRRLAPEVVAFQRRIPDAEVALLYSPASMYTVSEY
PARLRRAHAELSHLDLPVRFLSERQLAAGKTGQVKALVIPGAQRLERETAEALAGFAARG
GTILTAPGTRFTDPYGAALPGFPVRESELTATAFDREFDRLGLNRPVRGNLPGGALELRS
AERNGAMLFYAVNYGAPREFRPLLDGKPIAGAIELISGETVKFPLRLPNRKTMIFEVKP

Enzyme Prediction     

No EC number prediction in MGYG000002473_01297.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH167	363	920	6.7e-79	0.8326359832635983

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd09621	CBM9_like_5	1.18e-52	56	238	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.
cd00241	DOMON_like	1.17e-13	70	220	12	158	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.
cd09619	CBM9_like_4	2.10e-13	59	223	18	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.
pfam02449	Glyco_hydro_42	3.50e-09	473	791	12	354	Beta-galactosidase. This group of beta-galactosidase enzymes belong to the glycosyl hydrolase 42 family. The enzyme catalyzes the hydrolysis of terminal, non-reducing terminal beta-D-galactosidase residues.
COG1874	GanA	2.13e-07	451	907	8	491	Beta-galactosidase GanA [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AVM45530.1	0.0	1	1018	1	1023
QHW30800.1	7.04e-54	44	1001	492	1467
QNK56641.1	6.96e-49	38	1000	295	1434
AIQ58722.1	8.40e-46	44	1001	98	1224
AIQ43288.1	9.65e-45	44	1001	306	1450

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6Y2K_A	5.06e-09	531	842	70	420	ChainA, beta-galactosidase [Marinomonas sp. ef1]
1KWG_A	1.57e-06	594	882	140	448	Crystalstructure of Thermus thermophilus A4 beta-galactosidase [Thermus thermophilus],1KWK_A Crystal structure of Thermus thermophilus A4 beta-galactosidase in complex with galactose [Thermus thermophilus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O54315	2.73e-08	473	893	16	472	Beta-galactosidase BgaA OS=Thermus sp. OX=275 GN=bgaA PE=1 SV=1
A1A399	6.50e-08	455	967	19	560	Beta-galactosidase BgaB OS=Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a) OX=367928 GN=bgaB PE=1 SV=2
Q9X6C6	1.07e-07	477	882	18	448	Beta-galactosidase BgaT OS=Thermus brockianus OX=56956 GN=bgaT PE=1 SV=1
O69315	8.58e-06	594	882	140	448	Beta-galactosidase OS=Thermus thermophilus OX=274 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
0.000590	0.998491	0.000273	0.000222	0.000195	0.000180

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002473_01297.