CAZyme Information: MGYG000001703_04188

Basic Information

• Species: Vibrio fluvialis
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Vibrionaceae; Vibrio; Vibrio fluvialis
• CAZyme ID: MGYG000001703_04188
• CAZy Family: GH116
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1025	MGYG000001703_22|CGC1	114983.44	4.7353

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001703	4750671	Isolate	Bangladesh	Asia

• Gene Location: Start: 35476; End: 38553 Strand: -

Full Sequence      

MINKIPYTSYSGQAGALCSKGNAVEFLQPWYTPISTTPANTGMAVGGIGSTFTLTPQGNT
PNFSFIPGIFVDCEYESIHFNDFYFSVMDEHSLDNLDIPNVGELLLFLKYYPADFSFDIH
HADNKSYILSGIKDCLRSGLFYLNNKSNFERWQIEFSDKTQQAITNDPSSLETQLLVVID
FFNGLLVNNSARALSLTANNGSSVESIDPSDIEYRALYPIAEYEYQGLESVALTRQVISP
IVKNDQMLCSLPMHWNHFEMSNRSDKTQLVTLVQPLRNLIGSTYKKAREGVQDSCCHLVQ
NAISQQHQPVTISGAGFEFHGVSMTSNSPYDGDISGEVLYGVHTQLDGVAAEQVTVTVKP
QVYCSKADQQVERALKTGRTNAHFDRGIYSGREPLSALVCVQVTLKPGETIALRFAQVMD
HSKILLDGWESEKAYARYFDAQSRAQSILNQTLPRLSEIEQNIISQQLEFLDNASQTFVD
NDSALRFATMAMNSLSFLAESTVWDKENVLLVKECVDYPFFNSLDVYFYGSFSLLYLLPE
LDGCVMKHFAKAILNSDEKLRRYWEYEDKPYAELVDEKYQGSRAERGAVIHDLGSPFDIE
PDAYSWHNVKEWKDLAPKFILMVYRHWQKTGNREVVESCWSSVKESIDYLTNLIEDGDTL
PLTRGTDDTFDNLASHGVSIYCGGLWVAGLRAASELALLVGEKELAQGYTQRSKEALETL
ERGLWDEQKGYYHFFITPIQAKHLTGNGFESLEKLGLTLTGNTVHDASLVNAYLDAYDVD
SSVSKRDQRLAKKQRLIDLAPQAFSAEFAKLEADSDNSFGDALLADSYLKQVDLPGLFDS
SRIERTLDFIYQTNFVSNSPKLGVANMTLADGRPHDAFQAQDVWIGVQFSVATALRLAGK
QEQAECLMDTVYQALYSMAKIPFAAPEGFNCSVTVSGKDIAQRFDLKSEVASELLLQLQK
VGHLFADGRVNPELTQNIEEFALSLSKLPSNVDYRDLHTWLLSTGLKYTAGRYFRPGMIY
AYLYR

Enzyme Prediction     

No EC number prediction in MGYG000001703_04188.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH116	512	932	1.5e-106	0.9366391184573003

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam04685	DUF608	5.73e-63	514	930	7	343	Glycosyl-hydrolase family 116, catalytic region. This represents a family of archaeal, bacterial and eukaryotic glycosyl hydrolases, that belong to superfamily GH116. The primary catabolic pathway for glucosylceramide is catalysis by the lysosomal enzyme glucocerebrosidase. In higher eukaryotes, glucosylceramide is the precursor of glycosphingolipids, a complex group of ubiquitous membrane lipids. Mutations in the human protein cause motor-neurone defects in hereditary spastic paraplegia. The catalytic nucleophile, identified in UniProtKB:Q97YG8_SULSO, is a glutamine-335, with the likely acid/base at Asp-442 and the aspartates at Asp-406 and Asp-458 residues also playing a role in the catalysis of glucosides and xylosides that are beta-bound to hydrophobic groups. The family is defined as GH116, which presently includes enzymes with beta-glucosidase, EC:3.2.1.21, beta-xylosidase, EC:3.2.1.37, and glucocerebrosidase EC:3.2.1.45 activity.
COG4354	COG4354	8.25e-45	182	931	55	693	Uncharacterized protein, contains GBA2_N and DUF608 domains [Function unknown].
TIGR01577	oligosac_amyl	1.35e-05	626	732	365	465	oligosaccharide amylase. The name of this type of amylase is based on the characterization of an glucoamylase family enzyme from Thermoactinomyces vulgaris. The T. vulgaris enzyme was expressed in E. coli and, like other glucoamylases, it releases beta-D-glucose from starch. However, unlike previously characterized glucoamylases, this T. vulgaris amylase hydrolyzes maltooligosaccharides (maltotetraose, maltose) more efficiently than starch (1), indicating this enzyme belongs to a class of glucoamylase-type enzymes with oligosaccharide-metabolizing activity.
COG3408	GDB1	5.60e-05	613	732	338	468	Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism].
pfam17389	Bac_rhamnosid6H	6.11e-05	594	733	80	222	Bacterial alpha-L-rhamnosidase 6 hairpin glycosidase domain. This family consists of bacterial rhamnosidase A and B enzymes. L-Rhamnose is abundant in biomass as a common constituent of glycolipids and glycosides, such as plant pigments, pectic polysaccharides, gums or biosurfactants. Some rhamnosides are important bioactive compounds. For example, terpenyl glycosides, the glycosidic precursor of aromatic terpenoids, act as important flavouring substances in grapes. Other rhamnosides act as cytotoxic rhamnosylated terpenoids, as signal substances in plants or play a role in the antigenicity of pathogenic bacteria.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AMF92653.1	0.0	1	1025	1	1025
SPM17517.1	0.0	1	1025	1	1025
QAV05920.1	0.0	45	1025	1	981
QRH14280.1	0.0	1	1025	1	1025
QLE94682.1	0.0	1	1024	1	1022

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5FJS_A	1.27e-41	214	916	133	745	Bacterialbeta-glucosidase reveals the structural and functional basis of genetic defects in human glucocerebrosidase 2 (GBA2) [Thermoanaerobacterium xylanolyticum LX-11],5FJS_B Bacterial beta-glucosidase reveals the structural and functional basis of genetic defects in human glucocerebrosidase 2 (GBA2) [Thermoanaerobacterium xylanolyticum LX-11],5O0S_A Crystal structure of txGH116 (beta-glucosidase from Thermoanaerobacterium xylolyticum) in complex with unreacted beta Cyclophellitol Cyclosulfate probe ME711 [Thermoanaerobacterium xylanolyticum LX-11]
5NPF_A	1.36e-41	214	916	136	748	Crystalstructure of txGH116 (beta-glucosidase from Thermoanaerobacterium xylolyticum) in complex with beta Cyclophellitol Cyclosulfate probe ME594 [Thermoanaerobacterium xylanolyticum]
5BVU_A	1.37e-41	214	916	137	749	Crystalstructure of Thermoanaerobacterium xylolyticum GH116 beta-glucosidase [Thermoanaerobacterium xylanolyticum LX-11],5BX2_A Crystal structure of Thermoanaerobacterium xylanolyticum GH116 beta-glucosidase with 2-deoxy-2-fluoroglucoside [Thermoanaerobacterium xylanolyticum LX-11],5BX3_A Crystal structure of Thermoanaerobacterium xylanolyticum GH116 beta-glucosidase with deoxynojirimycin [Thermoanaerobacterium xylanolyticum LX-11],5BX4_A Crystal structure of Thermoanaerobacterium xylanolyticum GH116 beta-glucosidase with Glucoimidazole [Thermoanaerobacterium xylanolyticum LX-11],5BX5_A Crystal structure of Thermoanaerobacterium xylanolyticum GH116 beta-glucosidase with glucose [Thermoanaerobacterium xylanolyticum LX-11],5NCX_A Crystal structure of Thermoanaerobacterium xylolyticum GH116 beta-glucosidase with an covalent inhibitor [Thermoanaerobacterium xylanolyticum LX-11],5OST_A Beta-glucosidase from Thermoanaerobacterium xylolyticum GH116 in complex with Gluco-1H-imidazole [Thermoanaerobacterium xylanolyticum LX-11]
7W2V_A	1.74e-41	214	916	180	792	ChainA, Glucosylceramidase [Thermoanaerobacterium xylanolyticum LX-11]
7W2W_A	1.74e-41	214	916	180	792	ChainA, Glucosylceramidase [Thermoanaerobacterium xylanolyticum LX-11],7W2X_A Chain A, Glucosylceramidase [Thermoanaerobacterium xylanolyticum LX-11]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9HCG7	6.81e-32	214	734	228	738	Non-lysosomal glucosylceramidase OS=Homo sapiens OX=9606 GN=GBA2 PE=1 SV=2
Q69ZF3	1.16e-31	214	734	219	729	Non-lysosomal glucosylceramidase OS=Mus musculus OX=10090 GN=Gba2 PE=1 SV=2
Q5M868	7.98e-31	214	734	219	729	Non-lysosomal glucosylceramidase OS=Rattus norvegicus OX=10116 GN=Gba2 PE=2 SV=2
Q7KT91	1.01e-21	186	749	198	805	Non-lysosomal glucosylceramidase OS=Drosophila melanogaster OX=7227 GN=CG33090 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.990493	0.009176	0.000206	0.000046	0.000022	0.000066

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001703_04188.